EcoliWiki - User contributions [en]

PMID:211734

2008-05-28T19:04:01Z

Miriam:

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 '''Sobolev, SG, Shestopalova, NM, Linev, MB and Rubin, SG''' [Electron microscopic study of the An-750 strain of Powassan virus isolated in the Soviet Union]''Vopr. Virusol.'' 359-66

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Electron microscopic examinations of brains of white mice inoculated with the An 750 strain isolated for the first time from adult mosquitoes and with the prototype LB strain of Powassan virus were carried out. The method of combination of light and electron microscopy used in the study permitted to compare ultrastructural changes in one cell with the results of light microscopy. Sizes of virions and their localizations in the brain cells were determined. Virus particles were found in large and small neurons as well as in glial elements. Subcellular changes in neurons associated with virus multiplication are described. The causes of differences in sizes of virions measured in ultrathin sections are discussed.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=211734 PubMed] 
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=2111734&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0092-8674(90)90193-I Full text]
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{|class = 'sortable' {{Prettytable}} id='242153'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.G483dac87e0326&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:211734

2008-05-28T19:03:36Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Sobolev, SG, Shestopalova, NM, Linev, MB and Rubin, SG''' [Electron microscopic study of the An-750 strain of Powassan virus isolated in the Soviet Union]''Vopr. Virusol.'' 359-66

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Electron microscopic examinations of brains of white mice inoculated with the An 750 strain isolated for the first time from adult mosquitoes and with the prototype LB strain of Powassan virus were carried out. The method of combination of light and electron microscopy used in the study permitted to compare ultrastructural changes in one cell with the results of light microscopy. Sizes of virions and their localizations in the brain cells were determined. Virus particles were found in large and small neurons as well as in glial elements. Subcellular changes in neurons associated with virus multiplication are described. The causes of differences in sizes of virions measured in ultrathin sections are discussed.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=211734 PubMed] 
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<protect>

{|class = 'sortable' {{Prettytable}} id='242153'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.G483dac87e0326&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:3015881

2008-05-28T19:00:15Z

Miriam:

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 '''Biek, DP and Cohen, SN''' (1986) Identification and characterization of recD, a gene affecting plasmid maintenance and recombination in Escherichia coli.''J. Bacteriol.'' '''167''':594-603

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|{{TableHeadingColor}} |'''Abstract''' || <protect>We isolated mutations that reduce plasmid stability in dividing cell populations and mapped these mutations to a previously undescribed gene, recD, that affects recombination frequency and consequently the formation of plasmid concatemers. Insertions of the transposable element Tn10 into recD resulted in increased concatemerization and loss of pSC101 and ColE1-like replicons during nonselective growth. Both concatemer formation and plasmid instability in recD mutants require a functional recA gene. Mutations in recD are recessive to recD+ and map to a small region of the Escherichia coli chromosome located between recB and argA. Although the recD locus is distinct from loci encoding the two previously identified subunits of the RecBC enzyme, mutations in recD appear to affect the exonuclease activity of this enzyme.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3015881 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=3015881&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3015881 Full text]
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{|class = 'sortable' {{Prettytable}} id='241885'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U4818444ba0d96&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:9190831

2008-05-28T18:57:39Z

Miriam:

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 '''Bibikov, SI, Biran, R, Rudd, KE and Parkinson, JS''' (1997) A signal transducer for aerotaxis in Escherichia coli.''J. Bacteriol.'' '''179''':4075-9

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|{{TableHeadingColor}} |'''Abstract''' || The newly discovered aer locus of Escherichia coli encodes a 506-residue protein with an N terminus that resembles the NifL aerosensor and a C terminus that resembles the flagellar signaling domain of methyl-accepting chemoreceptors. Deletion mutants lacking a functional Aer protein failed to congregate around air bubbles or follow oxygen gradients in soft agar plates. Membranes with overexpressed Aer protein also contained high levels of noncovalently associated flavin adenine dinucleotide (FAD). We propose that Aer is a flavoprotein that mediates positive aerotactic responses in E. coli. Aer may use its FAD prosthetic group as a cellular redox sensor to monitor environmental oxygen levels.
</noinclude>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9190831 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=9190831&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9190831 Full text]
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{|class = 'sortable' {{Prettytable}} id='232307'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.P47aa7959cb1db&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:1542643

2008-05-28T18:56:59Z

Miriam:

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 '''Bibi, E and Kaback, HR''' (1992) Functional complementation of internal deletion mutants in the lactose permease of Escherichia coli.''Proc. Natl. Acad. Sci. U.S.A.'' '''89''':1524-8

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Using the lactose permease of Escherichia coli, a well-characterized membrane protein with 12 transmembrane domains, we demonstrated that certain paired in-frame deletion constructs complement each other functionally. Although cells expressing the deletion mutants individually are unable to catalyze active lactose accumulation, cells simultaneously expressing specific pairs of deletions catalyze transport up to 60% as do cells expressing wild-type permease. Moreover, complementation clearly does not occur at the level of DNA but probably occurs at the protein level. Remarkably, functional complementation is observed only with pairs of permease molecules containing large deletions and is not observed with missense mutations or point deletions. Although the mechanism of functional complementation is obscure, the findings indicate that certain pairs of permease molecules containing specific internal deletions can interact to form a functional complex in the same way phenomenologically as do independently expressed polypeptides corresponding to different N- and C-terminal portions of the permease.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1542643 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=1542643&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=1542643 Full text]
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<protect>

{|class = 'sortable' {{Prettytable}} id='241884'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.H481844376c129&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:9192629

2008-05-28T18:56:08Z

Miriam:

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 '''Bianco, PR and Kowalczykowski, SC''' (1997) The recombination hotspot Chi is recognized by the translocating RecBCD enzyme as the single strand of DNA containing the sequence 5'-GCTGGTGG-3'.''Proc. Natl. Acad. Sci. U.S.A.'' '''94''':6706-11

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|{{TableHeadingColor}} |'''Abstract''' || The RecBCD enzyme of Escherichia coli functions in the seemingly disparate roles of homologous recombination and the degradation of DNA. Which of these two roles it assumes is regulated by the 8-base recombination hotspot, Chi. Using double-stranded DNA substrates that are heteroduplex at the Chi locus we have established the determinants for Chi recognition. Our results show that an actively translocating RecBCD enzyme requires only the sequence information in the 5'-GCTGGTGG-3'-containing strand to recognize and to be regulated by Chi. Furthermore, the RecBCD enzyme can translocate through DNA heteroduplex bubbles as large as 22 bases, and still recognize a Chi sequence embedded in this region. This implies that recognition of Chi occurs following the unwinding of the DNA.
</noinclude>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9192629 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=9192629&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9192629 Full text]
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{|class = 'sortable' {{Prettytable}} id='232306'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.Y47aa7954f313e&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:8449868

2008-05-28T18:53:33Z

Miriam:

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 '''Bianchi, V, Reichard, P, Eliasson, R, Pontis, E, Krook, M, Jörnvall, H and Haggård-Ljungquist, E''' (1993) Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein.''J. Bacteriol.'' '''175''':1590-5

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|{{TableHeadingColor}} |'''Abstract''' || A specific ribonucleoside triphosphate reductase is induced in anaerobic Escherichia coli. This enzyme, as isolated, lacks activity in the test tube and can be activated anaerobically with S-adenosylmethionine, NADPH, and two previously uncharacterized E. coli fractions. The gene for one of these, previously named dA1, was cloned and sequenced. We found an open reading frame coding for a polypeptide of 248 amino acid residues, with a molecular weight of 27,645 and with an N-terminal segment identical to that determined by direct Edman degradation. In a Kohara library, the gene hybridized between positions 3590 and 3600 on the physical map of E. coli. The deduced amino acid sequence shows a high extent of sequence identity with that of various ferredoxin (flavodoxin) NADP+ reductases. We therefore conclude that dA1 is identical with E. coli ferredoxin (flavodoxin) NADP+ reductase. Biochemical evidence from a bacterial strain, now constructed and overproducing dA1 activity up to 100-fold, strongly supports this conclusion. The sequence of the gene shows an apparent overlap with the reported sequence of mvrA, previously suggested to be involved in the protection against superoxide (M. Morimyo, J. Bacteriol. 170:2136-2142, 1988). We suggest that a frameshift introduced during isolation or sequencing of mvrA caused an error in the determination of its sequence.
</noinclude>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8449868 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=8449868&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8449868 Full text]
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{|class = 'sortable' {{Prettytable}} id='235242'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F47aaac325bc76&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:6234203

2008-05-28T18:52:44Z

Miriam:

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 '''Białkowska-Hobrzanska, H and Denhardt, DT''' (1984) The rep mutation. VII. Cloning and analysis of the functional rep gene of Escherichia coli K-12.''Gene'' '''28''':93-102

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The rep gene of Escherichia coli was isolated on a 6-kb PvuII fragment of plasmid pLC44-7 DNA from the Clarke-Carbon collection and cloned into pSC101 (to form pHBH8) and pBR322 (to form pHBH30). The plasmids pHBH8 and pHBH30 were found to complement all rep mutations tested. The functional rep gene and its promoter were mapped to a 3.2-kb XhoI-BalI fragment on the basis of complementation data with deletion and insertion derivatives of the two plasmids; subcloning of various restriction fragments confirmed the assignment. EcoRI, HindIII, and HpaI restriction sites were found to reside within that region of the DNA required for expression of the rep function. A coupled in vitro transcription-translation system was used to show that only those plasmids containing a functional rep gene encoded a protein of about Mr 67 000 (the Mr of the rep protein). No plasmids were found that complemented only the A or B classes of rep mutants (which differ in their ability to support the growth of P2 and M13 phages). This result suggests that rep-A and rep-B are alleles of the same structural gene.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6234203 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=6234203&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0378-1119(84)90091-X Full text]
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<protect>

{|class = 'sortable' {{Prettytable}} id='241883'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.Q4818440c2975b&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:2999067

2008-05-28T18:51:45Z

Miriam:

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 '''Bialkowska-Hobrzanska, H, Gilchrist, CA and Denhardt, DT''' (1985) Escherichia coli rep gene: identification of the promoter and N terminus of the rep protein.''J. Bacteriol.'' '''164''':1004-10

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The functional Escherichia coli rep gene, which encodes the Mr 67,000 Rep helicase, has been localized within a 2.55-kilobase sequence. Its regulatory region has been characterized by the use of rep-lacZ fusions. The direction of transcription of the rep gene is clockwise on the E. coli chromosome, as are the nearby ilvC and rho genes. The sequence of the rep control region was determined, and putative regulatory sequences were identified; no evidence for autoregulation of expression was obtained. Transcription of the gene was not enhanced during the SOS response. The location of the promoter and the beginning of the protein were confirmed by S1 nuclease mapping of the 5' end of rep mRNA and determination of the NH2-terminal sequence of the rep protein.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2999067 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=2999067&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2999067 Full text]
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{|class = 'sortable' {{Prettytable}} id='241882'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.Q48184400cd69c&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:1644768

2008-05-27T21:59:20Z

Miriam:

{{RightTOC}}

 '''Bi, E and Lutkenhaus, J''' (1992) Isolation and characterization of ftsZ alleles that affect septal morphology.''J. Bacteriol.'' '''174''':5414-23

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The ftsZ gene encodes an essential cell division protein that specifically localizes to the septum of dividing cells. In this study we characterized the effects of the ftsZ2(Rsa) mutation on cell physiology. We found that this mutation caused an altered cell morphology that included minicell formation and an increased average cell length. In addition, this mutation caused a temperature-dependent effect on cell lysis. During this investigation we fortuitously isolated a novel temperature-sensitive ftsZ mutation that consisted of a 6-codon insertion near the 5' end of the gene. This mutation, designated ftsZ26(Ts), caused an altered polar morphology at the permissive temperature and blocked cell division at the nonpermissive temperature. The altered polar morphology resulted from cell division and correlated with an altered geometry of the FtsZ ring. An intragenic cold-sensitive suppressor of ftsZ26(Ts) that caused cell lysis at the nonpermissive temperature was isolated. These results support the hypothesis that the FtsZ ring determines the division site and interacts with the septal biosynthetic machinery.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1644768 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=1644768&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=1644768 Full text]
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{|class = 'sortable' {{Prettytable}} id='241881'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.S481843f9be090&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:2211499

2008-05-27T21:58:15Z

Miriam:

{{RightTOC}}

 '''Bi, E and Lutkenhaus, J''' (1990) Interaction between the min locus and ftsZ.''J. Bacteriol.'' '''172''':5610-6

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|{{TableHeadingColor}} |'''Abstract''' || In Escherichia coli, distinct but similar minicell phenotypes resulting from mutation at the minB locus and increased expression of ftsZ suggested a possible interaction between these genes. A four- to fivefold increase in FtsZ resulting from increased gene dosage was found to suppress the lethality of minCD expressed from the lac promoter. Since increased MinCD did not affect the level of FtsZ, this suggested that MinCD may antagonize FtsZ to inhibit its cell division activity. This possibility was supported by the finding that alleles of ftsZ isolated as resistant to the cell division inhibitor SulA were also resistant to MinCD. Among the ftsZ(Rsa) alleles, two appeared to be completely resistant to MinCD as demonstrated by the lack of an effect of MinCD on cell length and a minicell phenotype observed in the absence of a significant increase in FtsZ. It was shown that SulA inhibits cell division independently of MinCD.
</noinclude>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2211499 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=2211499&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2211499 Full text]
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{|class = 'sortable' {{Prettytable}} id='236763'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.N47ab24846989e&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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PMID:2158979

2008-05-27T21:57:05Z

Miriam:

{{RightTOC}}

 '''Bi, E and Lutkenhaus, J''' (1990) FtsZ regulates frequency of cell division in Escherichia coli.''J. Bacteriol.'' '''172''':2765-8

{|{{Prettytable}} align = 'center' width= '70%'
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|{{TableHeadingColor}} |'''Abstract''' || Cell division is regulated so that it occurs only once per cell cycle. In Escherichia coli, a rod-shaped bacterium, division normally takes place at the center of the long axis of the cell; however, in the minicell mutant, division can also take place at the cell pole. Such divisions take place at the expense of normal divisions, resulting in an overall increase in nucleated cell length. We report here that increasing the level of FtsZ can completely suppress the cell length of the minicell mutant by increasing the frequency at which cell division events take place. This result suggests that the level of FtsZ controls the frequency of cell division in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2158979 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=2158979&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2158979 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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{|class = 'sortable' {{Prettytable}} id='241077'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.X47ab9e1627ee2&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:2158579

2008-05-27T21:55:55Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Gunby, P''' (1990) Morbidity and Mortality Weekly Report is unique.''JAMA'' '''263''':2583-4

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2158579 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242152'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.E483c836ac64bb&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:3288626

2008-05-27T21:55:34Z

Miriam:

{{RightTOC}}

 '''Bhatnagar, SK and Bessman, MJ''' (1988) Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase.''J. Biol. Chem.'' '''263''':8953-7

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The mutator gene, mutT, has been cloned into an expression vector and overproduced in Escherichia coli. The gene product has been purified to over 90% homogeneity as judged by gel electrophoresis and amino acid analysis. The amino acid composition of the protein and the sequence of the 20 amino acids of the N-terminal region agree well with the nucleotide sequence of the gene reported by Akiyama et al. (Akiyama, M., Horiuchi, T., and Sekiguchi, M. (1987) Mol. Gen. Genet. 206, 9-16) and indicate that the first of the potential initiation codons (position 164) of the open reading frame in the PvuII fragment carrying the mutT gene is the site of initiation of translation of the 15,000-Da polypeptide. A novel nucleoside triphosphatase activity which has a preference for dGTP is associated with the purified protein, and preliminary experiments are consistent with the notion that the mutT gene product is the enzyme responsible for this activity.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3288626 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=3288626&db=pubmed&url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3288626 Full text]
|}

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{|class = 'sortable' {{Prettytable}} id='237477'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.Q47ab3a13902d9&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


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{{RefHelp}}
<references/>

PMID:3011742

2008-05-27T21:47:46Z

Miriam:

{{RightTOC}}

 '''Bhagwat, AS, Sohail, A and Roberts, RJ''' (1986) Cloning and characterization of the dcm locus of Escherichia coli K-12.''J. Bacteriol.'' '''166''':751-5

{|{{Prettytable}} align = 'center' width= '70%'
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|{{TableHeadingColor}} |'''Abstract''' || <protect>The dcm locus of Escherichia coli K-12 has been shown to code for a methylase that methylates the second cytosine within the sequence 5'-CC(A/T)GG-3'. This sequence is also recognized by the EcoRII restriction-modification system coded by the E. coli plasmid N3. The methylase within the EcoRII system methylates the same cytosine as the dcm protein. We have isolated, from a library of E. coli K-12 DNA, two overlapping clones that carry the dcm locus. We show that the two clones carry overlapping sequences that are present in a dcm+ strain, but are absent in a delta dcm strain. We also show that the cloned gene codes for a methylase, that it complements mutations in the EcoRII methylase, and that it protects EcoRII recognition sites from cleavage by the EcoRII endonuclease. We found no phage restriction activity associated with the dcm clones.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3011742 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=3011742&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3011742 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
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{{LitMaterials}}

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<protect>

{|class = 'sortable' {{Prettytable}} id='241880'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U481843c16464f&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:4598003

2008-05-27T20:54:38Z

Miriam:

{{RightTOC}}

 '''Beyersmann, D, Messer, W and Schlicht, M''' (1974) Mutants of Escherichia coli B-r defective in deoxyribonucleic acid initiation: dnaI, a new gene for replication.''J. Bacteriol.'' '''118''':783-9

{|{{Prettytable}} align = 'center' width= '70%'
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|{{TableHeadingColor}} |'''Abstract''' || <protect>Mutagenized E. coli B/r cells were subjected to a procedure designed to select mutants temperature-sensitive for initiation of deoxyribonucleic acid (DNA) replication. Seventeen mutants exhibiting limited residual DNA synthesis at 42 C were obtained and the dna(-) sites were mapped genetically. Sixteen of the sites map near dnaA, dnaB, and dnaC. One mutant (dna-208) maps in a new location between the trp and his genes. We propose to call this mutant dnaI208. In complementation experiments dnaC(+) and dnaI(+) were dominant to dnaC(-) and dnaI(-) alleles, respectively. However, dnaA(-) was dominant to the wild-type allele dnaA(+). All dnaA mutants and four out of six dnaC mutants could be suppressed by F factor integration. The pattern of suppression was specific for each mutant.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4598003 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=4598003&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=4598003 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
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<protect>

{|class = 'sortable' {{Prettytable}} id='241878'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F48184391b0bfa&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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==References==
{{RefHelp}}
<references/>

PMID:4394444

2008-05-27T20:50:09Z

Miriam:

{{RightTOC}}

 '''Lee, KL and Kenney, FT''' (1970) Induction of alanine transaminase by adrenal steroids in cultured hepatoma cells.''Biochem. Biophys. Res. Commun.'' '''40''':469-75

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4394444 PubMed] 
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=4394444&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0006-291X(70)91032-6 Full text]
|}

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{{LitSignificance}}

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{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242151'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.X483c73b518365&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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==References==
{{RefHelp}}
<references/>

PMID:4394444

2008-05-27T20:48:53Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Lee, KL and Kenney, FT''' (1970) Induction of alanine transaminase by adrenal steroids in cultured hepatoma cells.''Biochem. Biophys. Res. Commun.'' '''40''':469-75

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4394444 PubMed] 
|}

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{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{|class = 'sortable' {{Prettytable}} id='242151'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.X483c73b518365&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6369246

2008-05-27T20:47:02Z

Miriam:

{{RightTOC}}

 '''Bencini, DA, Houghton, JE, Hoover, TA, Foltermann, KF, Wild, JR and O'Donovan, GA''' (1983) The DNA sequence of argI from Escherichia coli K12.''Nucleic Acids Res.'' '''11''':8509-18

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The argI gene from E. coli K12 has been sequenced. It contains an open reading frame of 1002 bases which encodes a polypeptide of 334 amino acids. Three such polypeptides are required to form the functional catalytic trimer (c3) of ornithine transcarbamoylase (OTCase-1, EC 2.1.3.3). The molecular mass of the mature trimer deduced from the amino acid sequence is 114,465 daltons. An altered form of argI was produced when a 1.6 kilobase DdeI fragment was subcloned into the HincII site of plasmid pUC8 extending the open reading frame an additional 20 nucleotides. It has been previously reported that the amino-terminal region of the respective polypeptides of argI, argF, and pyrB of E. coli possessed significant homology. In contrast, the homologous promoter/operator regions of argI and argF did not appear to share any homologies with pyrB. However, a closer scrutiny of the nucleotide sequence immediately preceding the pyrBI attenuator revealed a remarkable similarity to the argI and argF control region.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6369246 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=6369246&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6369246 Full text]
|}

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{{LitSignificance}}

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{{LitMaterials}}

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{|class = 'sortable' {{Prettytable}} id='241145'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.M47ab9f98dfeed&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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<references/>

PMID:3027045

2008-05-27T20:46:22Z

Miriam:

{{RightTOC}}

 '''Ben-Bassat, A, Bauer, K, Chang, SY, Myambo, K, Boosman, A and Chang, S''' (1987) Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure.''J. Bacteriol.'' '''169''':751-7

{|{{Prettytable}} align = 'center' width= '70%'
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|{{TableHeadingColor}} |'''Abstract''' || Methionine aminopeptidase (MAP) catalyzes the removal of amino-terminal methionine from proteins. The Escherichia coli map gene encoding this enzyme was cloned; it consists of 264 codons and encodes a monomeric enzyme of 29,333 daltons. In vitro analyses with purified enzyme indicated that MAP is a metallo-oligopeptidase with absolute specificity for the amino-terminal methionine. The methionine residues from the amino-terminal end of the recombinant proteins interleukin-2 (Met-Ala-Pro-IL-2) and ricin A (Met-Ile-Phe-ricin A) could be removed either in vitro with purified MAP enzyme or in vivo in MAP-hyperproducing strains of E. coli. In vitro analyses of the substrate preference of the E. coli MAP indicated that the residues adjacent to the initiation methionine could significantly influence the methionine cleavage process. This conclusion is consistent, in general, with the deduced specificity of the enzyme based on the analysis of known amino-terminal sequences of intracellular proteins (S. Tsunasawa, J. W. Stewart, and F. Sherman, J. Biol. Chem. 260:5382-5391, 1985).
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3027045 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=3027045&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3027045 Full text]
|}

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{{LitSignificance}}

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{{LitMaterials}}

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{|class = 'sortable' {{Prettytable}} id='237846'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.O47ab42a2633c3&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:7499229

2008-05-27T20:45:28Z

Miriam:

{{RightTOC}}

 '''Belunis, CJ, Clementz, T, Carty, SM and Raetz, CR''' (1995) Inhibition of lipopolysaccharide biosynthesis and cell growth following inactivation of the kdtA gene in Escherichia coli.''J. Biol. Chem.'' '''270''':27646-52

{|{{Prettytable}} align = 'center' width= '70%'
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|{{TableHeadingColor}} |'''Abstract''' || The enzyme 3-deoxy-D-manno-octulosonic acid (Kdo) transferase is encoded by the kdtA gene in Escherichia coli. The enzyme is a single polypeptide that catalyzes the transfer of two Kdo residues to a tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A, designated lipid IVA (Belunis, C.J., and Raetz, C.R.H. (1992) J. Biol. Chem. 267, 9988-9997). To determine if Kdo transfer to lipid IVA is required for growth, we constructed a strain of E. coli with a chromosomal kdtA::kan insertion mutation. In mutants carrying the kdtA::kan allele on the chromosome, cell growth and Kdo transferase activity were dependent upon a copy of the intact kdtA gene on a plasmid. When the kdtA-bearing plasmid was itself temperature sensitive for replication, the growth of these strains was inhibited after several hours at 44 degrees C, and Kdo transferase activity in extracts became undetectable. Concomitantly, the cells accumulated massive amounts of lipid IVA, the precursor of (Kdo)2-lipid IVA. The kdtA::kan mutation could also be complemented by hybrid plasmids bearing the gseA gene of Chlamydia trachomatis. gseA specifies a distinct Kdo transferase that adds three Kdo moieties to lipid IVA. Lipopolysaccharide from E. coli kdtA::kan constructs complemented by gseA reacts strongly with antibodies directed against the genus-specific epitope of Chlamydia, whereas lipopolysaccharide from parental E. coli K-12 does not. Our studies prove that Kdo attachment during lipid A biosynthesis is essential for cell growth and accounts for the conditional lethality associated with mutations in Kdo biosynthesis.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7499229 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=7499229&db=pubmed&url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=7499229 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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{|class = 'sortable' {{Prettytable}} id='233615'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.N47aa917825889&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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{{RefHelp}}
<references/>

PMID:3011793

2008-05-22T21:10:41Z

Miriam:

{{RightTOC}}

 '''Bell, AW, Buckel, SD, Groarke, JM, Hope, JN, Kingsley, DH and Hermodson, MA''' (1986) The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12.''J. Biol. Chem.'' '''261''':7652-8

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The nucleotide sequences of rbsD, rbsA, and rbsC have been determined. These genes encode components of the high affinity ribose transport system in Escherichia coli, and together with the sequences of rbsB (Groarke, J.M., Mahoney, W.C., Hope, J.N., Furlong, C.E., Robb, F.T., Zalkin, H., and Hermodson, M.A. (1983) J. Biol. Chem. 258, 12952-12956) and rbsK (Hope, J.N., Bell, A.W., Hermodson, M.A., and Groarke, J.M. (1986) J. Biol. Chem. 261, 7663-7668), they complete the nucleotide sequence of the first five genes of the rbs operon. Nuclease S1 mapping places the transcriptional start site for the operon 29 base pairs upstream from the most likely translational start site for rbsD. The open reading frames of rbsD, rbsA, and rbsC encode proteins of 139, 501, and 321 amino acid residues, respectively. The character of the proteins varies widely, from very hydrophilic for the rbsA product to exceedingly hydrophobic for the rbsC product. The intercistronic spaces between the three genes are very short, with the stop codons of the upstream genes overlapping the ribosome-binding sites of the downstream genes. This may imply translational control of expression of these genes, the products of which presumably form a membrane-bound transport complex.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3011793 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=3011793&db=pubmed&url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3011793 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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{|class = 'sortable' {{Prettytable}} id='237985'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.D47ab46a642789&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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<references/>

PMID:6308660

2008-05-22T21:08:38Z

Miriam:

{{RightTOC}}

 '''Belfort, M, Maley, G, Pedersen-Lane, J and Maley, F''' (1983) Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product.''Proc. Natl. Acad. Sci. U.S.A.'' '''80''':4914-8

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The nucleotide sequence of a 1,163-base-pair fragment that encodes the entire thyA gene of Escherichia coli K-12 was determined. The strategy involved sequence determination of both DNA strands by using overlapping deletions that had been generated in vitro from the two ends of the fragment with BAL-31 nuclease. The amino-terminal sequence of thymidylate synthase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45), the product of the thyA gene, located the 792-base-pair open reading frame, which codes for the 264 amino acid residues of this enzyme. The amino acid sequence deduced from the nucleotide data was confirmed to the extent of 40% by partial sequence analysis of the enzyme purified from extracts of the amplified cloned gene. Transcriptional and translational control areas were apparent in the regions flanking the structural gene. The 5-fluorodeoxyuridylate-binding residue of the active site was identified as cysteine-146. Comparison of the E. coli and Lactobacillus casei synthase sequences reveals consistent homology (62%) over extensive regions. This homology is particularly striking in a very hydrophobic region bordering cysteine-146. In the two enzymes, this region, which probably defines the active site, is 82% homologous. However, a dramatic difference between the two sequences is reflected by the surprising finding that a 51-amino-acid stretch, present midway through the L. casei sequence, is completely absent from the E. coli enzyme.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6308660 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=6308660&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6308660 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='238325'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.E47ab4e6064fc9&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:4352176

2008-05-22T21:07:23Z

Miriam:

{{RightTOC}}

 '''Belfort, M and Wulff, DL''' (1973) Genetic and biochemical investigation of the Escherichia coli mutant hfl-1 which is lysogenized at high frequency by bacteriophage lambda.''J. Bacteriol.'' '''115''':299-306

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>The Escherichia coli mutant hfl-1 is lysogenized at very high frequency by bacteriophage lambda. The normal requirement for the lambdacIII gene product in the establishment of repression is not observed in hfl-1 strains. These phenotypic characteristics are specified by a single locus at 82.5 min on the E. coli map in extremely close proximity to the purA gene, cotransduction frequencies ranging from 97 to 100% depending on the particular purA marker used. The lactose operon is shown to function normally in this strain, and there are also no demonstrable differences in ribonucleic acid polymerase activity or cyclic-adenosine monophosphate levels. Alterations in the cell envelope are indicated by a slight rifamycin resistance, which is reversible by pretreating the cells with ethylenediaminetetraacetic acid, and by a resistance to penicillin and a sensitivity to high concentrations of sodium dodecyl sulfate. It is not known whether this change in cell surface is the primary lesion, or a pleiotropic effect of some more basic metabolic shift.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4352176 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=4352176&db=pubmed&url=http://jb.asm.org/cgi/pmidlookup?view=long&pmid=4352176 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241873'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.K481842bf4913c&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:3513164

2008-05-22T21:06:38Z

Miriam:

{{RightTOC}}

 '''Belfaiza, J, Parsot, C, Martel, A, de la Tour, CB, Margarita, D, Cohen, GN and Saint-Girons, I''' (1986) Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region.''Proc. Natl. Acad. Sci. U.S.A.'' '''83''':867-71

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The metC gene of Escherichia coli K-12 was cloned and the nucleotide sequence of the metC gene and its flanking regions was determined. The translation initiation codon was identified by sequencing the NH2-terminal part of beta-cystathionase, the MetC gene product. The metC gene (1185 nucleotides) encodes a protein having 395 amino acid residues. The 5' noncoding region was found to contain a "Met box" homologous to sequences suggestive of operator structures upstream from other methionine genes that are controlled by the product of the pleiotropic regulatory metJ gene. The deduced amino acid sequence of beta-cystathionase showed extensive homology with that of the MetB protein (cystathionine gamma-synthase) that catalyzes the preceding step in methionine biosynthesis. The homology strongly suggests that the structural genes for the MetB and MetC proteins evolved from a common ancestral gene.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3513164 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=3513164&db=pubmed&url=http://www.pnas.org/cgi/pmidlookup?view=long&pmid=3513164 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='240128'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.J47ab7f5e337ee&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:3532030

2008-05-22T21:05:46Z

Miriam:

{{RightTOC}}

 '''Béjar, S, Cam, K and Bouché, JP''' (1986) Control of cell division in Escherichia coli. DNA sequence of dicA and of a second gene complementing mutation dicA1, dicC.''Nucleic Acids Res.'' '''14''':6821-33

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A mutation in a gene dicA of Escherichia coli leads to temperature-sensitive cell division, by allowing expression of a nearby division inhibition gene dicB (1). We have now established the sequence of the DicA region and identified DicA as a 15.5 KD protein. A second gene dicC transcribed divergently from dicA and coding for an 8.5 KD protein can also complement mutation dicA1 when provided on a multicopy plasmid.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3532030 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=3532030&db=pubmed&url=http://nar.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=3532030 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241872'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.D481842aa3f1a1&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6296046

2008-05-22T21:04:13Z

Miriam:

{{RightTOC}}

 '''Béjar, S and Bouché, JP''' (1983) Molecular cloning of the region of the terminus of Escherichia coli K-12 DNA replication.''J. Bacteriol.'' '''153''':604-9

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A series of plasmids have been isolated either by ligation of defined restriction fragments to plasmid pBR325 or by screening of a cosmid bank by in situ colony hybridization. Together with one previously isolated plasmid, they spanned 86% of the 30.5- to 34-min region of the genetic map of Escherichia coli K-12. Physical analysis of these plasmids and hybridizations to Southern blots confirmed the endonuclease map of this region, with the exception of a 9.3-kilobase pair inversion.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6296046 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=6296046&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6296046 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241870'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.A481842919323b&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:7024253

2008-05-22T21:03:14Z

Miriam:

{{RightTOC}}

 '''Beher, MG and Schnaitman, CA''' (1981) Regulation of the OmpA outer membrane protein of Escherichia coli.''J. Bacteriol.'' '''147''':972-85

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>The role of lipopolysaccharide in regulating the expression of the ompA outer membrane protein gene of Escherichia coli K-12 was studied by isolating mutants defective in the biosynthesis of lipopolysaccharide and by examining transcription of lacZ in strains carrying operon fusions in which lacZ is expressed from the ompA promoter. By selecting for simultaneous resistance to phages K3 and U3, we obtained mutants defective in rfaC (biosynthesis of core heptose) and in rfaP (phosphorylation of core heptose), and both of these mutant strains failed to express OmpA protein in the outer membrane. Expression of lacZ from the ompA or by foreign ompA alleles which are not expressed in E. coli K-12. Expression was increased in strains carrying rfaC and rfaP mutations. No precursor or degraded form of OmpA protein accumulated in cells which could not express the protein in the outer membrane. This lack of accumulation of precursor was observed even in the presence of phenethyl alcohol, which caused accumulation of OmpA precursor in wild-type cells. We present a model for the regulation of this gene which is consistent with these observations and which involves modulation of transcription coupled to translation of the protein.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7024253 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=7024253&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=7024253 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241869'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.I4818428a79541&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:3894330

2008-05-22T21:02:37Z

Miriam:

{{RightTOC}}

 '''Begg, KJ and Donachie, WD''' (1985) Cell shape and division in Escherichia coli: experiments with shape and division mutants.''J. Bacteriol.'' '''163''':615-22

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Double mutants which carry mutations in genes (rodA, pbpA) required for cell elongation (i.e., maintenance of rod shape) in combination with mutations in genes (ftsA, ftsI, ftsQ, or ftsZ) required for septation were constructed. Such mutants were able to grow for about two mass doublings at a normal rate at the restrictive temperature (42 degrees C). The morphology of the cells formed under these conditions was interpreted by assuming the existence of a generalized system for peptidoglycan growth together with two additional systems which modify the shape of the growing peptidoglycan layer. The results also showed that different fts genes probably control different stages in septation. ftsZ (sulB or sfiB) appears to be required for the earliest step in septation, ftsQ and ftsI (pbpB or sep) are required for a later step or steps, and ftsA is required only for the latest stages in septation.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3894330 PubMed] [http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=3894330&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3894330 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242130'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.M4835df3147066&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:3894330

2008-05-22T21:01:38Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Begg, KJ and Donachie, WD''' (1985) Cell shape and division in Escherichia coli: experiments with shape and division mutants.''J. Bacteriol.'' '''163''':615-22

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Double mutants which carry mutations in genes (rodA, pbpA) required for cell elongation (i.e., maintenance of rod shape) in combination with mutations in genes (ftsA, ftsI, ftsQ, or ftsZ) required for septation were constructed. Such mutants were able to grow for about two mass doublings at a normal rate at the restrictive temperature (42 degrees C). The morphology of the cells formed under these conditions was interpreted by assuming the existence of a generalized system for peptidoglycan growth together with two additional systems which modify the shape of the growing peptidoglycan layer. The results also showed that different fts genes probably control different stages in septation. ftsZ (sulB or sfiB) appears to be required for the earliest step in septation, ftsQ and ftsI (pbpB or sep) are required for a later step or steps, and ftsA is required only for the latest stages in septation.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3894330 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242130'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.M4835df3147066&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:7592387

2008-05-22T20:59:48Z

Miriam:

{{RightTOC}}

 '''Begg, KJ, Dewar, SJ and Donachie, WD''' (1995) A new Escherichia coli cell division gene, ftsK.''J. Bacteriol.'' '''177''':6211-22

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A mutation in a newly discovered Escherichia coli cell division gene, ftsK, causes a temperature-sensitive late-stage block in division but does not affect chromosome replication or segregation. This defect is specifically suppressed by deletion of dacA, coding for the peptidoglycan DD-carboxypeptidase, PBP 5. FtsK is a large polypeptide (147 kDa) consisting of an N-terminal domain with several predicted membrane-spanning regions, a proline-glutamine-rich domain, and a C-terminal domain with a nucleotide-binding consensus sequence. FtsK has extensive sequence identity with a family of proteins from a wide variety of prokaryotes and plasmids. The plasmid proteins are required for intercellular DNA transfer, and one of the bacterial proteins (the SpoIIIE protein of Bacillus subtilis) has also been implicated in intracellular chromosomal DNA transfer.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7592387 PubMed] 
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=7592387&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=7592387 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242129'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.W4835d95b6e8da&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:7592387

2008-05-22T20:36:44Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Begg, KJ, Dewar, SJ and Donachie, WD''' (1995) A new Escherichia coli cell division gene, ftsK.''J. Bacteriol.'' '''177''':6211-22

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A mutation in a newly discovered Escherichia coli cell division gene, ftsK, causes a temperature-sensitive late-stage block in division but does not affect chromosome replication or segregation. This defect is specifically suppressed by deletion of dacA, coding for the peptidoglycan DD-carboxypeptidase, PBP 5. FtsK is a large polypeptide (147 kDa) consisting of an N-terminal domain with several predicted membrane-spanning regions, a proline-glutamine-rich domain, and a C-terminal domain with a nucleotide-binding consensus sequence. FtsK has extensive sequence identity with a family of proteins from a wide variety of prokaryotes and plasmids. The plasmid proteins are required for intercellular DNA transfer, and one of the bacterial proteins (the SpoIIIE protein of Bacillus subtilis) has also been implicated in intracellular chromosomal DNA transfer.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7592387 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242129'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.W4835d95b6e8da&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6089173

2008-05-21T17:34:23Z

Miriam: New PMID: Page!

{{RightTOC}}

 '''Clegg, DO and Koshland, DE''' (1984) The role of a signaling protein in bacterial sensing: behavioral effects of increased gene expression.''Proc. Natl. Acad. Sci. U.S.A.'' '''81''':5056-60

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A recombinant DNA approach has been used to study intracellular signaling in the bacterial sensing system. The Escherichia coli cheY gene, whose function is unknown, has been subcloned behind the synthetic inducible tac promoter. The resulting plasmid directs the synthesis of the Y protein in response to isopropyl beta-D-thiogalactoside, independent of its usual operon control. When this construct was introduced into wild-type and mutant cells, the Y protein caused a clockwise rotational bias in the flagellar motors. This effect was observed even in heavily biased counterclockwise strains lacking most of the central chemotaxis processing genes. The results show that the Y protein has a direct influence on flagellar rotation not requiring other processing genes of the sensing system. The Y protein appears to bind directly to a part of the flagellar motor, probably the flaA gene product, and it is probably the key element in biasing the motor toward the clockwise rotational direction.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6089173 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='242085'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.D48345d1ebbbff&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

User:Miriam

2008-05-21T15:52:34Z

Miriam:

My name is Miriam Garcia. I'm a pre-med management major, Spanish minor here at Texas A&M. I am a curator for Dr. Jerry Tsai. If you need to contact me email me at mrm1177@tamu.edu. Thanks, Gig 'em, and God Bless!!!

== Sequence Possibilities ==

'''Needs numbering on both sides and should only be 5 columns wide:'''

GTTAACTACG TCAGGTGGCA CTTTTCGGGG AAATGTGCGC GGAACCCCTA TTTGTTTATT TTTCTAAATA
CATTCAAATA TGTATCCGCT CATGAGACAA TAACCCTGAT AAATGCTTCA ATAATATTGA AAAAGGAAGA
GTATGAGTAT TCAACATTTC CGTGTCGCCC TTATTCCCTT TTTTGCGGCA TTTTGCCTTC CTGTTTTTGC
TCACCCAGAA ACGCTGGTGA AAGTAAAAGA TGCTGAAGAT CAGTTGGGTG CACGAGTGGG TTACATCGAA
CTGGATCTCA ACAGCGGTAA GATCCTTGAG AGTTTTCGCC CCGAAGAACG TTCTCCAATG ATGAGCACTT
TTAAAGTTCT GCTATGTGGC GCGGTATTAT CCCGTGTTGA CGCCGGGCAA GAGCAACTCG GTCGCCGCAT
ACACTATTCT CAGAATGACT TGGTTGAGTA CTCACCAGTC ACAGAAAAGC ATCTTACGGA TGGCATGACA
GTAAGAGAAT TATGCAGTGC TGCCATAACC ATGAGTGATA ACACTGCGGC CAACTTACTT CTGACAACGA
TCGGAGGACC GAAGGAGCTA ACCGCTTTTT TGCACAACAT GGGGGATCAT GTAACTCGCC TTGATCGTTG
GGAACCGGAG CTGAATGAAG CCATACCAAA CGACGAGCGT GACACCACGA TGCCTGTAGC AATGGCAACA
ACGTTGCGCA AACTATTAAC TGGCGAACTA CTTACTCTAG CTTCCCGGCA ACAATTAATA GACTGGATGG
AGGCGGATAA AGTTGCAGGA CCACTTCTGC GCTCGGCCCT TCCGGCTGGC TGGTTTATTG CTGATAAATC
TGGAGCCGGT GAGCGTGGGT CTCGCGGTAT CATTGCAGCA CTGGGGCCAG ATGGTAAGCC CTCCCGTATC
GTAGTTATCT ACACGACGGG GAGTCAGGCA ACTATGGATG AACGAAATAG ACAGATCGCT GAGATAGGTG
CCTCACTGAT TAAGCATTGG TAACTGTCAG ACCAAGTTTA CTCATATATA CTTTAGATTG ATTTACCCCG
GTTGATAATC AGAAAAGCCC CAAAAACAGG AAGATTGTAT AAGCAAATAT TTAAATTGTA AACGTTAATA
TTTTGTTAAA ATTCGCGTTA AATTTTTGTT AAATCAGCTC ATTTTTTAAC CAATAGGCCG AAATCGGCAA
AATCCCTTAT AAATCAAAAG AATAGCCCGA GATAGGGTTG AGTGTTGTTC CAGTTTGGAA CAAGAGTCCA
CTATTAAAGA ACGTGGACTC CAACGTCAAA GGGCGAAAAA CCGTCTATCA GGGCGATGGC CCACTACGTG
AACCATCACC CAAATCAAGT TTTTTGGGGT CGAGGTGCCG TAAAGCACTA AATCGGAACC CTAAAGGGAG
CCCCCGATTT AGAGCTTGAC GGGGAAAGCG AACGTGGCGA GAAAGGAAGG GAAGAAAGCG AAAGGAGCGG
GCGCTAGGGC GCTGGCAAGT GTAGCGGTCA CGCTGCGCGT AACCACCACA CCCGCCGCGC TTAATGCGCC
GCTACAGGGC GCGTAAAAGG ATCTAGGTGA AGATCCTTTT TGATAATCTC ATGACCAAAA TCCCTTAACG
TGAGTTTTCG TTCCACTGAG CGTCAGACCC CGTAGAAAAG ATCAAAGGAT CTTCTTGAGA TCCTTTTTTT
CTGCGCGTAA TCTGCTGCTT GCAAACAAAA AAACCACCGC TACCAGCGGT GGTTTGTTTG CCGGATCAAG
AGCTACCAAC TCTTTTTCCG AAGGTAACTG GCTTCAGCAG AGCGCAGATA CCAAATACTG TTCTTCTAGT
GTAGCCGTAG TTAGGCCACC ACTTCAAGAA CTCTGTAGCA CCGCCTACAT ACCTCGCTCT GCTAATCCTG
TTACCAGTGG CTGCTGCCAG TGGCGATAAG TCGTGTCTTA CCGGGTTGGA CTCAAGACGA TAGTTACCGG
ATAAGGCGCA GCGGTCGGGC TGAACGGGGG GTTCGTGCAC ACAGCCCAGC TTGGAGCGAA CGACCTACAC
CGAACTGAGA TACCTACAGC GTGAGCTATG AGAAAGCGCC ACGCTTCCCG AAGGGAGAAA GGCGGACAGG
TATCCGGTAA GCGGCAGGGT CGGAACAGGA GAGCGCACGA GGGAGCTTCC AGGGGGAAAC GCCTGGTATC
TTTATAGTCC TGTCGGGTTT CGCCACCTCT GACTTGAGCG TCGATTTTTG TGATGCTCGT CAGGGGGGCG
GAGCCTATGG AAAAACGCCA GCAACGCGGC CTTTTTACGG TTCCTGGCCT TTTGCTGGCC TTTTGCTCAC
ATGTAATGTG AGTTAGCTCA CTCATTAGGC ACCCCAGGCT TTACACTTTA TGCTTCCGGC TCGTATGTTG
TGTGGAATTG TGAGCGGATA ACAATTTCAC ACAGGAAACA GCTATGACCA TGATTACGCC AAGCTACGTA
ATACGACTCA CTATAGGGGC CCGTGCAATT GAAGCCGGCT GGCGCCAAGC TTCTCTGCAG GATATCTGGA
TCCACGAATT CGCTAGCTTC GGCCGTGACG CGTCTCCGGA TGTACAGGCA TGCGTCGACC CTCTAGTCAA
GGCCTATAGT GAGTCGTATT ACGGACTGGC CGTCGTTTTA CAACGTCGTG ACTGGGAAAA CCCTGGCGTT
ACCCAACTTA ATCGCCTTGC AGCACATCCC CCTTTCGCCA GCTGGCGTAA TAGCGAAGAG GCCCGCACCG
ATCGCCCTTC CCAACAGTTG CGCAGCCTGA ATGGCGAATG GCGCTTCGCT TGGTAATAAA GCCCGCTTCG
GCGGGCTTTT TTTT

'''Needs numbering on one side:'''

1 GGTACCCTGT GAATGCGCAA ACCAACCCTT GGCAGAACAT ATCCATCGCG
51 TCCGCCATCT CCAGCAGCCG CACGCGGCGC ATCTCGGGCA GCGTTGGGTC
101 CTGGCCACGG GTGCGCATGA TCGTGCTCCT GTCGTTGAGG ACCCGGCTAG
151 GCTGGCGGGG TTGCCTTACT GGTTAGCAGA ATGAATCACC GATACGCGAG
201 CGAACGTGAA GCGACTGCTG CTGCAAAACG TCTGCGACCT GAGCAACAAC
251 ATGAATGGTC TTCGGTTTCC GTGTTTCGTA AAGTCTGGAA ACGCGGAAGT
301 CAGCGCCCTG CACCATTATG TTCCGGATCT ATGTCGGGTG CGGAGAAAGA
351 GGTAATGAAA TGGCAGATCC CTGGCTTGTT GTCCACAACC GTTAAACCTT
401 AAAAGCTTTA AAAGCCTTAT ATATTCTTTT TTTTCTTATA AAACTTAAAA
451 CCTTAGAGGC TATTTAAGTT GCTGATTTAT ATTAATTTTA TTGTTCAAAC
501 ATGAGAGCTT AGTACGTGAA ACATGAGAGC TTAGTACGTT AGCCATGAGA
551 GCTTAGTACG TTAGCCATGA GGGTTTAGTT CGTTAAACAT GAGAGCTTAG
601 TACGTTAAAC ATGAGAGCTT AGTACGTGAA ACATGAGAGC TTAGTACGTA
651 CTATCAACAG GTTGAACTGC TGATCTTCGG ATCTATGTCG GGTGCGGAGA
701 AAGAGGTAAT GAAATGGCAG ATCCCTGGCT TGTTGTCCAC AACCGTTAAA
751 CCTTAAAAGC TTTAAAAGCC TTATATATTC TTTTTTTTCT TATAAAACTT
801 AAAACCTTAG AGGCTATTTA AGTTGCTGAT TTATATTAAT TTTATTGTTC
851 AAACATGAGA GCTTAGTACG TGAAACATGA GAGCTTAGTA CGTTAGCCAT
901 GAGAGCTTAG TACGTTAGCC ATGAGGGTTT AGTTCGTTAA ACATGAGAGC
951 TTAGTACGTT AAACATGAGA GCTTAGTACG TGAAACATGA GAGCTTAGTA

'''Needs numbering on one side and alignment fixed:'''

1 GGTACCCTGT GAATGCGCAA ACCAACCCTT GGCAGAACAT ATCCATCGCG
51 TCCGCCATCT CCAGCAGCCG CACGCGGCGC ATCTCGGGCA GCGTTGGGTC
101 CTGGCCACGG GTGCGCATGA TCGTGCTCCT GTCGTTGAGG ACCCGGCTAG
151 GCTGGCGGGG TTGCCTTACT GGTTAGCAGA ATGAATCACC GATACGCGAG
201 CGAACGTGAA GCGACTGCTG CTGCAAAACG TCTGCGACCT GAGCAACAAC
251 ATGAATGGTC TTCGGTTTCC GTGTTTCGTA AAGTCTGGAA ACGCGGAAGT
301 CAGCGCCCTG CACCATTATG TTCCGGATCT ATGTCGGGTG CGGAGAAAGA
351 GGTAATGAAA TGGCAGATCC CTGGCTTGTT GTCCACAACC GTTAAACCTT
401 AAAAGCTTTA AAAGCCTTAT ATATTCTTTT TTTTCTTATA AAACTTAAAA
451 CCTTAGAGGC TATTTAAGTT GCTGATTTAT ATTAATTTTA TTGTTCAAAC
501 ATGAGAGCTT AGTACGTGAA ACATGAGAGC TTAGTACGTT AGCCATGAGA
551 GCTTAGTACG TTAGCCATGA GGGTTTAGTT CGTTAAACAT GAGAGCTTAG
601 TACGTTAAAC ATGAGAGCTT AGTACGTGAA ACATGAGAGC TTAGTACGTA
651 CTATCAACAG GTTGAACTGC TGATCTTCGG ATCTATGTCG GGTGCGGAGA
701 AAGAGGTAAT GAAATGGCAT CCGGATCTGC ATCGCAGGAT GCTGCTGGCT
751 ACCCTGTGGA ACACCTACAT CTGTATTAAC GAAGCGCTGG AGATGGCGGA
801 CGCGATGGAT ATGTTCTGCC AAGGGTTGGT TTGCGCATTC ACAGTTCTCC
851 GCAAGAATTG ATTGGCTCCA ATTCTTGGAG TGGTGAATCC GTTAGCGAGG
901 TGCCGCCGGC TTCCATTCAG GTCGAGGTGG CCCGGCTCCA TGCACCGCGA
951 CGCAACGCGG GGAGGCAGAC AAGGTATAGG GCGGCGCCTA CAATCCATGC
1001 CAACCCGTTC CATGTGCTCG CCGAGGCGGC ATAAATCGCC GTGACGATCA
1051 GCGGTCCAAT GATCGAAGTT AGGCTGGTAA GAGCCGCGAG CGATCCTTGA
1101 AGCTGTCCCT GATGGTCGTC ATCTACCTGC CTGGACAGCA TGGCCTGCAA
1151 CGCGGGCATC CCGATGCCGC CGGAAGCGAG AAGAATCATA ATGGGGAAGG
1201 CCATCCAGCC TCGCGTCGCG AACGCCAGCA AGACGTAGCC CAGCGCGTCG
1251 GCCGCCATGC CGGCGATAAT GGCCTGCTTC TCGCCGAAAC GTTTGGTGGC
1301 GGGACCAGTG ACGAAGGCTT GAGCGAGGGC GTGCAAGATT CCGAATACCG
1351 CAAGCGACAG GCCGATCATC GTCGCGCTCC AGCGAAAGCG GTCCTCGCCG
1401 AAAATGACCC AGAGCGCTGC CGGCACCTGT CCTACGAGTT GCATGATAAA
1451 GAAGACAGTC ATAAGTGCGG CGACAGTAGT CATGCCCCGC GCCCACCGGA
1501 AGGAGCTGAC TGGGTTGAAG GCTCTCAAGG GCATCGGTCG ACGCTCTCCC
1551 TTATGCGACT CCTGCATTAG GAAGCAGCCC AGTAGTAGGT TGAGGCCGTT
1601 GAGCACCGCC GCCGCAAGGA ATGGTGCATG CAAGGAGATG GCGCCCAACA
1651 GTCCCCCGGC CACGGGGCCT GCCACCATAC CCACGCCGAA ACAAGCGCTC
1701 ATGAGCCCGA AGTGGCGAGC CCGATCTTCC CCATCGGTGA TGTCGGCGAT
1751 ATAGGCGCCA GCAACCGCAC CTGTGGCGCC GGTGATGCCG GCCACGATGC
1801 GTCCGGCGTA GAGGATCCAC AGGACGGGTG TGGTCGCCAT GATCGCGTAG
1851 TCGATAGTGG CTCCAAGTAG CGAAGCGAGC AGGACTGGGC GGCGGCCAAA
1901 GCGGTCGGAC AGTGCTCCGA GAACGGGTGC GCATAGAAAT TGCATCAACG
1951 CATATAGCGC TAGCAGCACG CCATAGTGAC TGGCGATGCT GTCGGAATGG
2001 ACGATATCCC GCAAGAGGCC CGGCAGTACC GGCATAACCA AGCCTATGCC
2051 TACAGCATCC AGGGTGACGG TGCCGAGGAT GACGATGAGC GCATTGTTAG
2101 ATTTCATACA CGGTGCCTGA CTGCGTTAGC AATTTAACTG TGATAAACTA
2151 CCGCATTAAA GCTTATCGAT GATAAGCGCT GGCATTGACC CTGAGTGATT
2201 TTTCTCTGGT CCCGCCGCAT CCATACCGCC AGTTGTTTAC CCTCACAACG
2251 TTCCAGTAAC CGGGCATGTT CATCATCAGT AACCCGTATC GTGAGCATCC
2301 TCTCTCGTTT CATCGGTATC ATTACCCCCA TGAACAGAAA TCCCCCTTAC
2351 ACGGAGGCAT CAGTGACCAA ACAGGAAAAA ACCGCCCTTA ACATGGCCCG
2401 CTTTATCAGA AGCCAGACAT TAACGCTTCT GGAGAAACTC AACGAGCTGG
2451 ACGCGGATGA ACAGGCAGAG CTCTTACTGT CATGCCATCC GTATGTTTAA
2501 ACACAATAAA GTCTTAAACT GAACAAAATA GATCTAAACT ATGACAATAA
2551 AGTCTTAAAC TAGACAGAAT AGTTGTAAAC TGAAATCAGT CCAGTTATGC
2601 TGTGAAAAAG CATACTGGAC TTTTGTTATG GCTAAAGCAA ACTCTTCATT
2651 TTCTGAAGTG CAAATTGCCC GTCGTATTAA AGAGGGGCGT GGGGTCGACG
2701 CGGCCGCTAA CTATAACGGT CCTAAGGTAG CGAGTTTGGC GCGCCAAACG
2751 ATATCGGATC CAGGCGTTTA AGGGCACCAA TAACTGCCTT AAAAAAATTA
2801 CGCCCCGCCC TGCCACTCAT CGCAGTACTG TTGTAATTCA TTAAGCATTC
2851 TGCCGACATG GAAGCCATCA CAAACGGCAT GATGAACCTG AATCGCCAGC
2901 GGCATCAGCA CCTTGTCGCC TTGCGTATAA TATTTGCCCA TGGTGAAAAC
2951 GGGGGCGAAG AAGTTGTCCA TATTGGCCAC GTTTAAATCA AAACTGGTGA
3001 AACTCACCCA GGGATTGGCT GAGACGAAAA ACATATTCTC AATAAACCCT
3051 TTAGGGAAAT AGGCCAGGTT TTCACCGTAA CACGCCACAT CTTGCGAATA
3101 TATGTGTAGA AACTGCCGGA AATCGTCGTG GTATTCACTC CAGAGCGATG
3151 AAAACGTTTC AGTTTGCTCA TGGAAAACGG TGTAACAAGG GTGAACACTA
3201 TCCCATATCA CCAGCTCACC GTCTTTCATT GCCATACGGA ATTCCGGATG
3251 AGCATTCATC AGGCGGGCAA GAATGTGAAT AAAGGCCGGA TAAAACTTGT
3301 GCTTATTTTT CTTTACGGTC TTTAAAAAGG CCGTAATATC CAGCTGAACG
3351 GTCTGGTTAT AGGTACATTG AGCAACTGAC TGAAATGCCT CAAAATGTTC
3401 TTTACGATGC CATTGGGATA TATCAACGGT GGTATATCCA GTGATTTTTT
3451 TCTCCATTTT AGCTTCCTTA GCTCCTGAAA ATCTCGATAA CTCAAAAAAT
3501 ACGCCCGGTA GTGATCTTAT TTCATTATGG TGAAAGTTGG AACCTCTTAC
3551 GTGCCGATCA ACGTCTCATT TTCGCCAAAA GTTGGCCCAG GGCTTCCCGG
3601 TATCAACAGG GACACCAGGA TTTATTTATT CTGCGAAGTG ATCTTCCGTC
3651 ACAGGTATGG ATCCGATATC ATTTAAATCT AGGGATAACA GGGTAATACT
3701 AGTGTCGACC AACCAGATAA GTGAAATCTA GTTCCAAACT ATTTTGTCAT
3751 TTTTAATTTT CGTATTAGCT TACGACGCTA CACCCAGTTC CCATCTATTT
3801 TGTCACTCTT CCCTAAATAA TCCTTAAAAA CTCCATTTCC ACCCCTCCCA
3851 GTTCCCAACT TTATTGTGTT TAAACACCGT AAGATGCTTT TCAGTGACT

'''Capitalization error:'''

1 GTTctagagg atctttgtga aggaacctta cttctgtggt gtgacataat
51 tggacaaact acctacagag atttaaagct ctaaggtaaa tataaaattt
101 ttaagtgtat aatgtgttaa actactgatt ctaattgttt gtgtatttta
151 gattccaacc tatggaactt atgaatggga gcagtggtgg aatgccttta
201 atgaggaaaa cctgttttgc tcagaagaaa tgccatctag tgatgatgag
251 gctactgctg actctcaaca ttctactctc aaaagaagag aaaggtagag
301 acccaaggac tttccttcag aattgctaag ttttttgagt catgctgtgt
351 ttagtaatag aactcttgct tgctttgcta tttacaacca caaaggaaaa
401 agctgcactg ctatacaaga aaattatgga aaaatattct gtaaccttta
451 taagtaggca taacagttat aatcataaca tactgttttt tcttactcca
501 cacaggcata gagtgtctgc tattaataac tatgctcaaa aattgtgtac
551 ctttagcttt ttaatttgta aaggggttaa taaggaatat ttgatgtata
601 gtgccttgac tagagatcat aatcagccat accacatttg tagaggtttt
651 acttgcttta aaaaacctcc cacacctccc cctgaacctg aaacataaaa
701 tgaatgcaat tgttgttgtt aacttgttta ttgcagctta taatggttac
751 aaataaagca atagcatcac aaatttcaca aataaagcat ttttttcact
801 gcattctagt tgtggtttgt ccaaactcat caatgtatct tatcatgtct
851 ggatcAACTA CGTCAGGTGG CACTTTTCGG GGAAATGTGC GCGGAACCCC
901 TATTTGTTTA TTTTTCTAAA TACATTCAAA TATGTATCCG CTCATGAGAC
951 AATAACCCTG ATAAATGCTT CAATAATATT GAAAAAGGAA GAGTATGAGT
1001 ATTCAACATT TCCGTGTCGC CCTTATTCCC TTTTTTGCGG CATTTTGCCT
1051 TCCTGTTTTT GCTCACCCAG AAACGCTGGT GAAAGTAAAA GATGCTGAAG
1101 ATCAGTTGGG TGCACGAGTG GGTTACATCG AACTGGATCT CAACAGCGGT
1151 AAGATCCTTG AGAGTTTTCG CCCCGAAGAA CGTTCTCCAA TGATGAGCAC
1201 TTTTAAAGTT CTGCTATGTG GCGCGGTATT ATCCCGTGTT GACGCCGGGC
1251 AAGAGCAACT CGGTCGCCGC ATACACTATT CTCAGAATGA CTTGGTTGAG
1301 TACTCACCAG TCACAGAAAA GCATCTTACG GATGGCATGA CAGTAAGAGA
1351 ATTATGCAGT GCTGCCATAA CCATGAGTGA TAACACTGCG GCCAACTTAC
1401 TTCTGACAAC GATCGGAGGA CCGAAGGAGC TAACCGCTTT TTTGCACAAC
1451 ATGGGGGATC ATGTAACTCG CCTTGATCGT TGGGAACCGG AGCTGAATGA
1501 AGCCATACCA AACGACGAGC GTGACACCAC GATGCCTGTA GCAATGGCAA
1551 CAACGTTGCG CAAACTATTA ACTGGCGAAC TACTTACTCT AGCTTCCCGG
1601 CAACAATTAA TAGACTGGAT GGAGGCGGAT AAAGTTGCAG GACCACTTCT
1651 GCGCTCGGCC CTTCCGGCTG GCTGGTTTAT TGCTGATAAA TCTGGAGCCG
1701 GTGAGCGTGG GTCTCGCGGT ATCATTGCAG CACTGGGGCC AGATGGTAAG
1751 CCCTCCCGTA TCGTAGTTAT CTACACGACG GGGAGTCAGG CAACTATGGA
1801 TGAACGAAAT AGACAGATCG CTGAGATAGG TGCCTCACTG ATTAAGCATT
1851 GGTAACTGTC AGACCAAGTT TACTCATATA TACTTTAGAT TGATTTACCC
1901 CGGTTGATAA TCAGAAAAGC CCCAAAAACA GGAAGATTGT ATAAGCAAAT
1951 ATTTAAATTG TAAACGTTAA TATTTTGTTA AAATTCGCGT TAAATTTTTG
2001 TTAAATCAGC TCATTTTTTA ACCAATAGGC CGAAATCGGC AAAATCCCTT
2051 ATAAATCAAA AGAATAGCCC GAGATAGGGT TGAGTGTTGT TCCAGTTTGG
2101 AACAAGAGTC CACTATTAAA GAACGTGGAC TCCAACGTCA AAGGGCGAAA
2151 AACCGTCTAT CAGGGCGATG GCCCACTACG TGAACCATCA CCCAAATCAA
2201 GTTTTTTGGG GTCGAGGTGC CGTAAAGCAC TAAATCGGAA CCCTAAAGGG
2251 AGCCCCCGAT TTAGAGCTTG ACGGGGAAAG CGAACGTGGC GAGAAAGGAA
2301 GGGAAGAAAG CGAAAGGAGC GGGCGCTAGG GCGCTGGCAA GTGTAGCGGT
2351 CACGCTGCGC GTAACCACCA CACCCGCCGC GCTTAATGCG CCGCTACAGG
2401 GCGCGTAAAA GGATCTAGGT GAAGATCCTT TTTGATAATC TCATGACCAA
2451 AATCCCTTAA CGTGAGTTTT CGTTCCACTG AGCGTCAGAC CCCGTAGAAA
2501 AGATCAAAGG ATCTTCTTGA GATCCTTTTT TTCTGCGCGT AATCTGCTGC
2551 TTGCAAACAA AAAAACCACC GCTACCAGCG GTGGTTTGTT TGCCGGATCA
2601 AGAGCTACCA ACTCTTTTTC CGAAGGTAAC TGGCTTCAGC AGAGCGCAGA
2651 TACCAAATAC TGTTCTTCTA GTGTAGCCGT AGTTAGGCCA CCACTTCAAG
2701 AACTCTGTAG CACCGCCTAC ATACCTCGCT CTGCTAATCC TGTTACCAGT
2751 GGCTGCTGCC AGTGGCGATA AGTCGTGTCT TACCGGGTTG GACTCAAGAC
2801 GATAGTTACC GGATAAGGCG CAGCGGTCGG GCTGAACGGG GGGTTCGTGC
2851 ACACAGCCCA GCTTGGAGCG AACGACCTAC ACCGAACTGA GATACCTACA
2901 GCGTGAGCTA TGAGAAAGCG CCACGCTTCC CGAAGGGAGA AAGGCGGACA
2951 GGTATCCGGT AAGCGGCAGG GTCGGAACAG GAGAGCGCAC GAGGGAGCTT
3001 CCAGGGGGAA ACGCCTGGTA TCTTTATAGT CCTGTCGGGT TTCGCCACCT
3051 CTGACTTGAG CGTCGATTTT TGTGATGCTC GTCAGGGGGG CGGAGCCTAT
3101 GGAAAAACGC CAGCAACGCG GCCTTTTTAC GGTTCCTGGC CTTTTGCTGG
3151 CCTTTTGCTC ACATGTATCA GCCATATCAC ATTTGTAGAG GTTTTACtTG
3201 CTTTAAAAAA CCTCCCACAC CTCCCCCTGA ACCTGAAACA TAAAATGAAT
3251 GCAATTGTTG TTAACTTGTT TATTGCAGCT TATAATGGTT ACAAATAAAG
3301 CAATAGCATC ACAAATTTCA CAAATAAAGC ATTTTTCACT GCATTCTAGT
3351 TGTGGTTTGT CCAAACTCAT CAATGTATCT TATCATGTCT GGATCAGCCA
3401 TATCACATTT GTAGAGGTTT TACTTGCTTT AAAAAACCTC CCACACCTCC
3451 CCCTGAACCT GAAACATAAA ATGAATGCAA TTGTTGTTAA CTTGTTTATT
3501 GCAGCTTATA ATGGTTACAA ATAAAGCAAT AGCATCACAA ATTTCACAAA
3551 TAAAGCATTT TTTTCACTGC ATTCTAGTTG TGGTTTGTCC AAACTCATCA
3601 ATGTATCTTA TCATGTCTGC CATGTAATGT GAGTTAGCTC ACTCATTAGG
3651 CACCCCAGGC TTTACACTTT ATGCTTCCGG CTCGTATGTT GTGTGGAATT
3701 GTGAGCGGAT AACAATTTCA CACAGGAAAC AGCTATGACC ATGATTACGC
3751 CAAGCTACgg gcggagtact gtcctccgag cggagtactg tcctccgagc
3801 ggagtactgt cctccgagcg gagtactgtc ctccgagcgg agtactgtcc
3851 tccgagcgga gactctagag ggtatataat ggGGGCCGTC AGCTACTACC
3901 AGAGCTCATG GGCCCGTGCA ATTGAAGCCG GCTGGCGCCA AGCTTGGTAC
3951 CGAGCTCGGA TCCAGCCACC ATGGGAGTCA AAGTTCTGTT TGCCCTGATC
4001 TGCATCGCTG TGGCCGAGGC CAAGCCCACC GAGAACAACG AAGACTTCAA
4051 CATCGTGGCC GTGGCCAGCA ACTTCGCGAC CACGGATCTC GATGCTGACC
4101 GCGGGAAGTT GCCCGGCAAG AAGCTGCCGC TGGAGGTGCT CAAAGAGATG
4151 GAAGCCAATG CCCGGAAAGC TGGCTGCACC AGGGGCTGTC TGATCTGCCT
4201 GTCCCACATC AAGTGCACGC CCAAGATGAA GAAGTTCATC CCAGGACGCT
4251 GCCACACCTA CGAAGGCGAC AAAGAGTCCG CACAGGGCGG CATAGGCGAG
4301 GCGATCGTCG ACATTCCTGA GATTCCTGGG TTCAAGGACT TGGAGCCCAT
4351 GGAGCAGTTC ATCGCACAGG TCGATCTGTG TGTGGACTGC ACAACTGGCT
4401 GCCTCAAAGG GCTTGCCAAC GTGCAGTGTT CTGACCTGCT CAAGAAGTGG
4451 CTGCCGCAAC GCTGTGCGAC CTTTGCCAGC AAGATCCAGG GCCAGGTGGA
4501 CAAGATCAAG GGGGCCGGTG GTGACTAAGC GGCCGCTAGC GATCGCGGCG
4551 CGCCACGCGT CTCCGGATGT ACAGGCATGC GTCGACCCTC TAGTCAAGGC
4601 CTATAGTGAG TCGTATTACG GACTGGCCGT CGTTTTACAA CGTCGTGACT
4651 GGGAAAACCC TGGCGTTACC CAACTTAATC GCCTTGCAGC ACATCCCCCT
4701 TTCGCCAGCT GGCGTAATAG CGAAGAGGCC CGCACCGATC GCCCTTCCCA
4751 ACAGTTGCGC AGCCTGAATG GCGAATGGCG CTTCGCTTGG TAATAAAGCC
4801 CGCTTCGGCG GGCTTTTTTT T

PMID:6998961

2008-05-15T18:33:10Z

Miriam:

{{RightTOC}}

 '''Begg, KJ, Hatfull, GF and Donachie, WD''' (1980) Identification of new genes in a cell envelope-cell division gene cluster of Escherichia coli: cell division gene ftsQ.''J. Bacteriol.'' '''144''':435-7

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>We report the identification, cloning, and mapping of a new cell division gene, ftsQ. This gene formed part of a cluster of three division genes (in the order ftsQ ftsA ftsZ) which itself formed part of a larger cluster of at least 10 genes, all of which were involved in some step in cell division, cell envelope synthesis, or both. The ftsQAZ group was transcribed from at least two independent promoters.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6998961 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=6998961&db=pubmed&url=http://jb.asm.org/cgi/pmidlookup?view=long&pmid=6998961 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241867'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.P4818424cab822&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:2254246

2008-05-15T18:32:40Z

Miriam:

{{RightTOC}}

 '''Begg, KJ, Takasuga, A, Edwards, DH, Dewar, SJ, Spratt, BG, Adachi, H, Ohta, T, Matsuzawa, H and Donachie, WD''' (1990) The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide.''J. Bacteriol.'' '''172''':6697-703

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>The rodA(Sui) mutation allows cell division to take place at 42 degrees C in ftsI23 mutant cells, which produce a thermolabile penicillin-binding protein 3 (PBP3, the septation-specific peptidoglycan transpeptidase). We show here that the mutation in rodA is a single-base change from a glutamine to a chain termination (amber) codon, and that an amber suppressor (supE) present in the strain restores the ability to produce a reduced level of normal RodA protein. The reduced level of RodA is accompanied by an increase in the levels of two other proteins (PBP2 and PBP5) encoded by genes in the rodA operon. We show that an increased level of PBP5 is by itself sufficient to restore cell division to ftsI23 cells at 42 degrees C. Two other treatments were found to restore division capacity to the mutant: an increase in PBP6 (which is a D-alanine carboxypeptidase like PBP5) or suitable concentrations of D-cycloserine. All of the above treatments have the effect of reducing the number of pentapeptide side chains in peptidoglycan and increasing the number of tripeptides. We conclude that the effect of the rodA(Sui) mutation is to indirectly increase the availability of tripeptide side chains, which are used preferentially by PBP3 as acceptors in transpeptidation. A change in the proportions of different kinds of peptide side chain in the peptidoglycan can therefore determine whether cells will divide.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2254246 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=2254246&db=pubmed&url=http://jb.asm.org/cgi/pmidlookup?view=long&pmid=2254246 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241866'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U481842347e8cd&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:2989779

2008-05-15T18:32:09Z

Miriam:

{{RightTOC}}

 '''Bedwell, D, Davis, G, Gosink, M, Post, L, Nomura, M, Kestler, H, Zengel, JM and Lindahl, L''' (1985) Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli.''Nucleic Acids Res.'' '''13''':3891-903

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>In Escherichia coli some 19 transcription units encoding the 52 ribosomal proteins are scattered throughout the genome. One of the units, the alpha operon, encodes genes for the ribosomal proteins S13, S11, S4 and L17 as well as the alpha subunit of RNA polymerase. We report here the complete 3.0 kb nucleotide sequence of the alpha operon. In addition, we have determined by S1 nuclease mapping the site of transcription termination in this operon.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2989779 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=2989779&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2989779 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241865'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.I4818422c1bc1e&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6185687

2008-05-15T18:31:39Z

Miriam:

{{RightTOC}}

 '''Bedouelle, H, Schmeissner, U, Hofnung, M and Rosenberg, M''' (1982) Promoters of the malEFG and malK-lamB operons in Escherichia coli K12.''J. Mol. Biol.'' '''161''':519-31

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6185687 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=6185687&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0022-2836(82)90405-3 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241864'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.O4818421c9b7cc&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:8593953

2008-05-15T18:31:03Z

Miriam:

{{RightTOC}}

 '''Becker-Hapak, M and Eisenstark, A''' (1995) Role of rpoS in the regulation of glutathione oxidoreductase (gor) in Escherichia coli.''FEMS Microbiol. Lett.'' '''134''':39-44

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>RpoS (sigma-38) is the major regulator of genes for survival of Escherichia coli in the stationary phase. OxyR is a transcriptional regulator that responds to H2O2 induced stress in exponential phase. Once considered to act independently of each other, they are now known to be integrally involved in the expression of several oxidative stress genes. While it is known that in the exponential phase, OxyR is the transcriptional regulator of gor, this study has shown that RpoS regulates gor in the stationary phase. beta-Galactosidase activity of a gor::lacZ promoter fusion showed no induction in a oxyR rpoS double mutant. Challenge of a gor mutant to several oxidants showed that the gene product was not functioning as a classic antioxidant.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8593953 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=8593953&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/037810979500378I Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241860'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.C481841ee6373b&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:1537811

2008-05-15T18:30:28Z

Miriam:

{{RightTOC}}

 '''Becker, S and Plapp, R''' (1992) Location of the dcp gene on the physical map of Escherichia coli.''J. Bacteriol.'' '''174''':1698-9

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1537811 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=1537811&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=1537811 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241859'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.R481841e24c664&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:6253901

2008-05-15T18:29:56Z

Miriam:

{{RightTOC}}

 '''Beck, E and Bremer, E''' (1980) Nucleotide sequence of the gene ompA coding the outer membrane protein II of Escherichia coli K-12.''Nucleic Acids Res.'' '''8''':3011-27

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>A nucleotide sequence of 2271 basepairs has been determined from cloned E. coli DNA which contains ompA. Withing that sequence, starting at nucleotide 1037, an open translational reading frame encodes a protein of 367 amino acids which starting with amino acid 22 agrees with the primary structure of protein II. The preceeding 21 amino acids constitute a typical signal sequence. There is a non-translated region of 360 nucleotides in front of the translational start. The insertion point of an IS1 element 110 nucleotides upstream from the start codon and an amber codon at the position of amino acid residue 28 have been localized in the DNA from two ompA mutants.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6253901 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=6253901&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6253901 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241857'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.I481841c805e18&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:2990907

2008-05-15T18:29:23Z

Miriam:

{{RightTOC}}

 '''Bech, FW, Jørgensen, ST, Diderichsen, B and Karlström, OH''' (1985) Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene.''EMBO J.'' '''4''':1059-66

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Escherichia coli relB mutants react to amino acid starvation by several abnormal responses, including accumulation of a translational inhibitor. We have isolated a relB-complementing plasmid from the Clarke and Carbon E. coli DNA library. From this plasmid we sequenced a 2140-bp segment which included the relB gene by the following two criteria: (i) it complements chromosomal relB mutations, (ii) the corresponding DNA segment cloned from chromosomal DNA of three relB mutants was defective in relB complementation. All three mutations fell within an open reading frame of 79 amino acids. A polypeptide of 9 kd compatible with this open reading frame was synthesized in maxicells and is in all probability the product of the relB gene. By nuclease S1 mapping we have determined the transcription start and stop of an 870 base transcript of the relB gene.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2990907 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=2990907&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2990907 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241856'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B4818419ed3bbb&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:3902576

2008-05-15T18:28:36Z

Miriam:

{{RightTOC}}

 '''Becerril, B, Valle, F, Merino, E, Riba, L and Bolivar, F''' (1985) Repetitive extragenic palindromic (REP) sequences in the Escherichia coli gdhA gene.''Gene'' '''37''':53-62

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Deletions of the 3' flanking DNA region of the glutamate dehydrogenase (GDH) structural gene from Escherichia coli K-12, have been produced on a plasmid that carries the complete gdhA gene. Those deletions include part of the repetitive extragenic palindromic (REP) sequences proposed by Stern et al. [Cell 37 (1984) 1015-1026], as a novel and major feature of the bacterial genome. The effect of these deletions on the final GDH level in the cell, has been determined. A broader compilation, analysis and alternative functions of the REP sequences, is also presented.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3902576 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=3902576&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0378-1119(85)90257-4 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241855'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.I4818417b71cad&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:2998936

2008-05-15T18:28:00Z

Miriam:

{{RightTOC}}

 '''Barbier, CS and Short, SA''' (1985) Studies on deo operon regulation in Escherichia coli: cloning and expression of the cytR structural gene.''Gene'' '''36''':37-44

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The structural gene that encodes one repressor (the cytR-encoded repressor) of the Escherichia coli deo operon has been cloned from a lambda dmet transducing phage into the multicopy plasmid pBR322 by selecting for ApR, Lac- transformants of E. coli SS110(delta lac, cytR, tsx::lac). Restriction maps for the cytR+ plasmids have been generated and the position of the cytR gene on the cloned insert of these plasmids has been determined through deletion analysis. Results from maxicell experiments employing pCB001 and its cytR- derivatives suggest that the cytR gene encodes a protein with a subunit Mr of 37 000. In contrast to the complete repression of the deo operon obtained when deoR+ plasmids were introduced into E. coli SS201 (deoR, cytR), transformation of this DeoR-, CytR- strain with any of the cytR+ plasmids yields only clones which have phenotypes and Deo enzyme levels characteristic of a DeoR- single mutant. The data presented in this study are consistent with the interpretation that, in E. coli, the deoR-encoded repressor controls deo operon transcription initiating from both deo promoter-operator sites, PO1 and PO2. In contrast, the cytR-encoded repressor regulates deo operon expression only through deo promoter-operator site PO2.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2998936 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=2998936&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0378-1119(85)90067-8 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='241677'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.R480a2f1f4e340&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:4588690

2008-05-15T18:27:25Z

Miriam:

{{RightTOC}}

 '''Barak, Z and Gilvarg, C''' (1974) Triornithine-resistant strains of Escherichia coli. Isolation, definition, and genetic studies.''J. Biol. Chem.'' '''249''':143-8

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || No abstract in PubMed
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4588690 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3051&itool=AbstractPlus-def&uid=4588690&db=pubmed&url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=4588690 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='241676'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.J480a2e1126034&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:9473056

2008-05-15T18:26:12Z

Miriam:

{{RightTOC}}

 '''Barak, R, Abouhamad, WN and Eisenbach, M''' (1998) Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli.''J. Bacteriol.'' '''180''':985-8

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli strains overproducing the response regulator CheY respond to acetate by increasing their clockwise bias of flagellar rotation, even when they lack other chemotaxis proteins. With acetate metabolism mutants, we demonstrate that both acetate kinase and acetyl coenzyme A synthetase are involved in this response. Thus, a response was observed when one of these enzymes was missing but not when both were absent.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9473056 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=9473056&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9473056 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='231124'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.G47aa549d683ab&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:8955390

2008-05-15T18:25:38Z

Miriam:

{{RightTOC}}

 '''Baquero, MR, Bouzon, M, Quintela, JC, Ayala, JA and Moreno, F''' (1996) dacD, an Escherichia coli gene encoding a novel penicillin-binding protein (PBP6b) with DD-carboxypeptidase activity.''J. Bacteriol.'' '''178''':7106-11

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || In the course of a study of genes located at min 44 of the Escherichia coli genome, we identified an open reading frame with the capacity to encode a 43-kDa polypeptide whose predicted amino acid sequence is strikingly similar to those of the well-known DD-carboxipeptidases penicillin-binding proteins PBP5 and PBP6. The gene product was shown to bind [3H]benzylpenicillin and to have DD-carboxypeptidase activity on pentapeptide muropeptides in vivo. Therefore, we called the protein PBP6b and the gene dacD. As with other E. coli DD-carboxypeptidases, PBP6b is not essential for cell growth. A quadruple dacA dacB dacC dacD mutant was constructed and shown to grow as well as its isogenic wild-type strain, indicating that the loss of any known PBP-associated DD-carboxypeptidase activity is not deleterious for E. coli. We also identified the homologous gene of dacD in Salmonella typhimurium as one of the components of the previously described phsBCDEF gene cluster.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8955390 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=8955390&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8955390 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='232715'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.Q47aa81396e66d&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:2939254

2008-05-15T18:25:07Z

Miriam:

{{RightTOC}}

 '''Banuett, F, Hoyt, MA, McFarlane, L, Echols, H and Herskowitz, I''' (1986) hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda cII protein.''J. Mol. Biol.'' '''187''':213-24

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The level of the viral cII protein has been proposed to be the crucial determinant in the lysis-lysogeny decision of bacteriophage lambda. A new Escherichia coli locus (hflB) has been identified in which a mutation (hflB29) leads to high frequency of lysogeny by lambda. A double mutant defective in both hflB and the previously identified hflA gene displays a more severe Hfl- phenotype than either single mutant. The hflB locus is at 69 minutes on the E. coli map, 85% co-transducible with argG. The hflB29 mutation results in increased stability of the phage cII protein (increasing its half-life twofold) and is recessive to hflB+. We conclude that the hflB+ locus is a negative regulator of cII, perhaps coding for or regulating a protease that acts on cII. In addition, we observe that the can1 mutation, an alteration of the cII gene that results in enhanced lysogenization, leads to increased stability of cII protein. These observations reinforce the view that the level of cII is a key factor in the lysis-lysogeny decision of lambda.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2939254 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3048&itool=AbstractPlus-def&uid=2939254&db=pubmed&url=http://linkinghub.elsevier.com/retrieve/pii/0022-2836(86)90229-9 Full text]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==


{|class = 'sortable' {{Prettytable}} id='237998'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.T47ab46f0e3d97&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}


==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:3040675

2008-05-15T18:24:26Z

Miriam:

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 '''Banuett, F and Herskowitz, I''' (1987) Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage lambda.''J. Bacteriol.'' '''169''':4076-85

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|{{TableHeadingColor}} |'''Abstract''' || We report the cloning of the Escherichia coli hflA locus, which governs stability of phage lambda cII protein and which has been proposed to encode or regulate a cII-specific protease. The hflA locus was cloned on an 18-kilobase DNA fragment by selecting for plasmids that carry the neighboring purA gene. The boundaries of hflA were delimited by analysis of deletions and insertions constructed in vitro and by use of transposon Tn1000. Maxicell analysis of the proteins encoded by the hflA-containing fragment shows that hflA consists of at least two nonoverlapping genes, hflC and hflK, encoding polypeptides of 37,000 (C) and 46,000 (K) daltons. We observe that insertions into one gene eliminate the corresponding polypeptide and greatly reduce synthesis of the other. We suggest that these two polypeptides (K and C) interact to form a multimeric complex and that free subunits are unstable. We have constructed two types of fusions between hflA and lacZ. One is an hflC-lacZ protein fusion constructed in vitro; the other is an hfl-lacZ operon fusion in which a Mu dX(Apr lac) has inserted into the hflK gene. We have used the operon fusion to infer the direction of transcription of the hflK gene--toward hflC and in the same direction as hflC. Last, we describe evidence that hflA contains an additional gene, hflX, encoding a 50,000-dalton polypeptide.
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3040675 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=3040675&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=3040675 Full text]
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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PMID:6286596

2008-05-15T18:23:52Z

Miriam:

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 '''Bankaitis, VA and Bassford, PJ''' (1982) Regulation of adenylate cyclase synthesis in Escherichia coli: studies with cya-lac operon and protein fusion strains.''J. Bacteriol.'' '''151''':1346-57

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|{{TableHeadingColor}} |'''Abstract''' || We have isolated cya-lac operon and protein fusions in Escherichia coli K-12, and we used these to study the regulation of cya, the structural gene for adenylate cyclase. Data obtained from these fusion strains suggest that neither cyclic AMP (cAMP) nor the cAMP receptor protein plays a major role in transcriptional or translational regulation of cya expression. Modulation of intracellular cAMP concentrations elicited only weak repression of cya-lac fusion activity under conditions of high intracellular cAMP, relative to fusion activity under conditions of low intracellular cAMP. The functional cAMP receptor protein was required for this effect. Incorporation of delta crp into cya-lac fusion strains did not affect fusion expression in glucose-grown cells as compared with similarly cultured isogenic crp+ strains. Furthermore, 20 independently obtained mutants derived from a cya-lacZ protein fusion strain exhibiting a weak Lac+ phenotype were isolated, and it was determined that the mutants had beta-galactosidase activities ranging from 2- to 77-fold greater than those of the parental strain. None of the mutations responsible for this increase in fusion activity map in the crp locus. We used these mutants to aid in the identification of a 160,000-dalton cya-lacZ hybrid protein. Finally, chromosome mobilization experiments, using cya-lac fusion strains, allowed us to infer a clockwise direction of transcription for the cya gene relative to the standard E. coli genetic map.
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6286596 PubMed]
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=6286596&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=6286596 Full text]
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{|class = 'sortable' {{Prettytable}} id='241674'
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.C480a29dcea935&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
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