EcoliWiki - User contributions [en]

User:Erdaltoprak

2013-02-05T21:27:24Z

66.249.73.133: Fill User: Page!

Click "edit table" in the last row to add information to the table. Click [[Help:Adding_your_information|here]] to find out how to add more information to your user page.



{| id="Z5111793c3adb0" class=" tableEdit User_info_table"

|-
!align=left |Name (Last, First)
||
Toprak, Erdal
|-
!align=left |Organization
||

|-
!align=left |Position
||

|-
!align=left |Address
||

|-
!align=left |Contact Info
||

|-
!align=left |Website(s)
||

|-
!align=left |Interests
||

|-
!align=left |Genes
||

|-
!align=left |Lab members
||

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182905.Z5111793c3adb0&page=182905&pagename={{FULLPAGENAMEE}}&type=1&template=User_info_table edit table] ||
|}


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

User:Erdaltoprak

2013-02-05T21:27:24Z

66.249.73.133: New User: Page!

PMID:11703658

2013-01-12T19:33:54Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="V50f1baa221926" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Journet, L , Bouveret, E , Rigal, A , Lloubes, R , Lazdunski, C and Bénédetti, H ''' (2001) Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm. ''Mol. Microbiol.'' '''42''':331-44
|-
!align=left |Abstract
||
Several proteins of the Tol/Pal system are required for group A colicin import into Escherichia coli. Colicin A interacts with TolA and TolB via distinct regions of its N-terminal domain. Both interactions are required for colicin translocation. Using in vivo and in vitro approaches, we show in this study that colicin A also interacts with a third component of the Tol/Pal system required for colicin import, TolR. This interaction is specific to colicins dependent on TolR for their translocation, strongly suggesting a direct involvement of the interaction in the colicin translocation step. TolR is anchored to the inner membrane by a single transmembrane segment and protrudes into the periplasm. The interaction involves part of the periplasmic domain of TolR and a small region of the colicin A N-terminal domain. This region and the other regions responsible for the interaction with TolA and TolB have been mapped precisely within the colicin A N-terminal domain and appear to be arranged linearly in the colicin sequence. Multiple contacts with periplasmic-exposed Tol proteins are therefore a general principle required for group A colicin translocation.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11703658 PubMed]

|-
!align=left |Keywords
||
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Colicins/chemistry; Colicins/genetics; Colicins/metabolism; Cross-Linking Reagents/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Formaldehyde/metabolism; Membrane Proteins/metabolism; Periplasm/metabolism; Periplasmic Proteins; Plasmids/genetics; Precipitin Tests; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protein Transport

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182893.V50f1baa221926&page=182893&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="B50f1baa23cc7a" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182893.B50f1baa23cc7a&page=182893&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:11703658

2013-01-12T19:33:54Z

66.249.73.133: New PMID: Page!

PMID:8663126

2013-01-12T17:21:11Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="R50f19b8725eee" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Saiki, K , Nakamura, H , Mogi, T and Anraku, Y ''' (1996) Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. ''J. Biol. Chem.'' '''271''':15336-40
|-
!align=left |Abstract
||
Subunit IV of the Escherichia coli bo-type ubiquinol oxidase is a 12-kDa membrane protein encoded by the cyoD gene and is conserved in the bacterial heme-copper terminal oxidases. To probe the functional role of subunit IV, we carried out deletion analysis and chemical cross-linking experiments with a homobifunctional and cleavable reagent. Spectroscopic properties of the mutant oxidases suggest that the C-terminal two-third (Val45 to His109) containing helices II and III is essential for the functional expression of the oxidase complex and for the CuB binding to the heme-copper binuclear center in subunit I. Cross-linking studies indicate that subunit IV is in close vicinity to subunit III. Based on these observations, we propose that subunit IV is present in a cleft formed by subunits I and III and assists the CuB binding to subunit I during biosynthesis or assembly of the oxidase complex.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8663126 PubMed]

|-
!align=left |Keywords
||
Amino Acid Sequence; Catalysis; Cross-Linking Reagents; Electron Transport Complex IV/chemistry; Electron Transport Complex IV/metabolism; Escherichia coli/enzymology; Macromolecular Substances; Molecular Sequence Data; Recombinant Proteins; Sequence Deletion; Structure-Activity Relationship

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182891.R50f19b8725eee&page=182891&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="D50f19b8744596" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182891.D50f19b8744596&page=182891&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:8663126

2013-01-12T17:21:11Z

66.249.73.133: New PMID: Page!

PMID:17395525

2013-01-12T16:32:29Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="C50f1901d979bf" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Brennan, RG and Link, TM ''' (2007) Hfq structure, function and ligand binding. ''Curr. Opin. Microbiol.'' '''10''':125-33
|-
!align=left |Abstract
||
Recent studies on Hfq have provided a deeper understanding of the multiple functions of this pleiotropic post-transcriptional regulator. Insights into the mechanism of Hfq action have come from a variety of approaches. A key finding was the characterization of two RNA binding sites: the Proximal Site, which binds sRNA and mRNA; and the Distal Site, which binds poly(A) tails. Hfq was shown to interact with PAP I, PNP and RNase E, proteins that are involved in mRNA decay and in vitro, was shown to form fibres, the physiological significance of which is unknown. Fluorescence resonance energy transfer (FRET) studies directly demonstrated the role of Hfq as a chaperone that facilitates the interaction between sRNAs and target mRNAs. There are still, however, some unresolved questions.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17395525 PubMed]
Online version:[http://dx.doi.org/10.1016/j.mib.2007.03.015 10.1016/j.mib.2007.03.015]
|-
!align=left |Keywords
||
Autoantigens/chemistry; Autoantigens/metabolism; Binding Sites; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Fluorescence Resonance Energy Transfer; Host Factor 1 Protein/chemistry; Host Factor 1 Protein/metabolism; Humans; Ligands; Models, Molecular; RNA, Bacterial/metabolism; Ribonucleoproteins, Small Nuclear/chemistry; Ribonucleoproteins, Small Nuclear/metabolism; snRNP Core Proteins

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182890.C50f1901d979bf&page=182890&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="R50f1901da936c" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182890.R50f1901da936c&page=182890&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:17395525

2013-01-12T16:32:29Z

66.249.73.133: New PMID: Page!

PMID:8650174

2013-01-12T16:22:54Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="C50f18dde8d29d" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Rohrwild, M , Coux, O , Huang, HC , Moerschell, RP , Yoo, SJ , Seol, JH , Chung, CH and Goldberg, AL ''' (1996) HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. ''Proc. Natl. Acad. Sci. U.S.A.'' '''93''':5808-13
|-
!align=left |Abstract
||
We have isolated a new type of ATP-dependent protease from Escherichia coli. It is the product of the heat-shock locus hslVU that encodes two proteins: HslV, a 19-kDa protein similar to proteasome beta subunits, and HslU, a 50-kDa protein related to the ATPase ClpX. In the presence of ATP, the protease hydrolyzes rapidly the fluorogenic peptide Z-Gly-Gly-Leu-AMC and very slowly certain other chymotrypsin substrates. This activity increased 10-fold in E. coli expressing heat-shock proteins constitutively and 100-fold in cells expressing HslV and HslU from a high copy plasmid. Although HslV and HslU could be coimmunoprecipitated from cell extracts of both strains with an anti-HslV antibody, these two components were readily separated by various types of chromatography. ATP stimulated peptidase activity up to 150-fold, whereas other nucleoside triphosphates, a nonhydrolyzable ATP analog, ADP, or AMP had no effect. Peptidase activity was blocked by the anti-HslV antibody and by several types of inhibitors of the eukaryotic proteasome (a threonine protease) but not by inhibitors of other classes of proteases. Unlike eukaryotic proteasomes, the HslVU protease lacked tryptic-like and peptidyl-glutamyl-peptidase activities. Electron micrographs reveal ring-shaped particles similar to en face images of the 20S proteasome or the ClpAP protease. Thus, HslV and HslU appear to form a complex in which ATP hydrolysis by HslU is essential for peptide hydrolysis by the proteasome-like component HslV.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8650174 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC39143 PMC39143]

|-
!align=left |Keywords
||
ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Endopeptidases/metabolism; Escherichia coli/enzymology; Heat-Shock Proteins/metabolism; Hydrolysis; Microscopy, Electron; Molecular Sequence Data; Serine Endopeptidases/metabolism; Substrate Specificity

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182889.C50f18dde8d29d&page=182889&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="X50f18ddeada15" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182889.X50f18ddeada15&page=182889&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:8650174

2013-01-12T16:22:54Z

66.249.73.133: New PMID: Page!

PMID:11515498

2013-01-12T16:21:13Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="X50f18d792b639" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Ohmori, H , Friedberg, EC , Fuchs, RP , Goodman, MF , Hanaoka, F , Hinkle, D , Kunkel, TA , Lawrence, CW , Livneh, Z , Nohmi, T , Prakash, L , Prakash, S , Todo, T , Walker, GC , Wang, Z and Woodgate, R ''' (2001) The Y-family of DNA polymerases. ''Mol. Cell'' '''8''':7-8
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11515498 PubMed]

|-
!align=left |Keywords
||
Animals; DNA-Directed DNA Polymerase/classification; DNA-Directed DNA Polymerase/genetics; Databases, Factual; Humans; Multigene Family; Phylogeny; Terminology as Topic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182888.X50f18d792b639&page=182888&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="D50f18d793d0f3" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182888.D50f18d793d0f3&page=182888&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:11515498

2013-01-12T16:21:13Z

66.249.73.133: New PMID: Page!

PMID:4922636

2013-01-12T16:10:17Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="F50f18ae9458ec" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Moses, RE and Richardson, CC ''' (1970) A new DNA polymerase activity of Escherichia coli. I. Purification and properties of the activity present in E. coli polA1. ''Biochem. Biophys. Res. Commun.'' '''41''':1557-64
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4922636 PubMed]

|-
!align=left |Keywords
||
Antibodies; Chromatography, Ion Exchange; DNA Nucleotidyltransferases/antagonists & inhibitors; DNA Nucleotidyltransferases/isolation & purification; Escherichia coli/enzymology; Ethylmaleimide; Magnesium; Nucleic Acid Denaturation; Nucleotides; Sulfhydryl Compounds/antagonists & inhibitors; Templates, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182887.F50f18ae9458ec&page=182887&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="C50f18ae94ed46" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182887.C50f18ae94ed46&page=182887&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4922636

2013-01-12T16:10:17Z

66.249.73.133: New PMID: Page!

PMID:4891262

2013-01-12T16:05:16Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="J50f189bc60dce" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Wilkins, BM ''' (1969) Chromosome transfer from F-lac+ strains of Escherichia coli K-12 mutant at recA, recB, or recC. ''J. Bacteriol.'' '''98''':599-604
|-
!align=left |Abstract
||
The frequency of chromosome transfer from various recombination-deficient F-lac(+) donor strains was estimated by standardizing the yield of conjugants receiving a male chromosomal marker against the level of episome transfer in the mating mixture. The efficiency of chromosome transfer from newly formed F-lac(+) cells carrying recB21 or recC22 was more than 50% of the wild-type value, although it was about 10 and 20%, respectively, if the male cell lines had become established. In contrast, recA13 donors transmitted the chromosome with less than 10(-4) of the normal frequency. If chromosome transfer from F-lac(+) strains reflects the cutting and subsequent joining of homologous single strands of episomal and chromosomal deoxyribonucleic acid by recombination, these results imply that the completed unions are not made in recA cells, but can be effected with more than 50% of normal efficiency in newly formed partial diploids mutant at either recB or recC. Thus, the defective stage in recA mutants may precede strand joining, whereas the deficiency in recB or recC cells may involve a later step in recombinant formation.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4891262 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC284860 PMC284860]

|-
!align=left |Keywords
||
Chromosomes, Bacterial; Conjugation, Genetic; Escherichia coli; Extrachromosomal Inheritance; Mutation; Recombination, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182886.J50f189bc60dce&page=182886&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="M50f189bc79871" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182886.M50f189bc79871&page=182886&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4891262

2013-01-12T16:05:16Z

66.249.73.133: New PMID: Page!

PMID:4290578

2013-01-12T16:05:15Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="N50f189bb70df7" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Fraenkel, DG ''' (1967) Genetic mapping of mutations affecting phosphoglucose isomerase and fructose diphosphatase in Escherichia coli. ''J. Bacteriol.'' '''93''':1582-7
|-
!align=left |Abstract
||
The loci on the Escherichia coli genome of mutations affecting phosphoglucose isomerase (pgi) and fructose diphosphatase (fdp) have been determined by conjugation and transduction experiments, chiefly three-factor crosses. The loci for these two constitutive enzymes of central intermediary metabolism lie in the same region of the chromosome, but they are not cotransducible. The order of some markers in this region of the chromosome is arg(ACFH) metA pgi malB uvrA fdp pyrB thr.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4290578 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC276653 PMC276653]

|-
!align=left |Keywords
||
Chromosome Mapping; Escherichia coli/enzymology; Fructose-Bisphosphatase/metabolism; Glucose-6-Phosphate Isomerase/metabolism; Molecular Biology; Mutation

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182885.N50f189bb70df7&page=182885&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="X50f189bb8a21f" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182885.X50f189bb8a21f&page=182885&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4290578

2013-01-12T16:05:15Z

66.249.73.133: New PMID: Page!

PMID:3905517

2013-01-12T15:57:17Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="T50f187dd33c71" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''van Buul, CP and van Knippenberg, PH ''' (1985) Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA. ''Gene'' '''38''':65-72
|-
!align=left |Abstract
||
The ksgA gene of Escherichia coli encodes a methyltransferase (MeT) that specifically dimethylates two adjacent adenosines near the 3' end of 16S RNA in the 30S particle. Its inactivation leads to kasugamycin (Ksg) resistance. Several plasmids were constructed with inserts which complemented chromosomal ksgA mutations. One of these inserts was sequenced and found to contain an open reading frame (ORF) sufficient to code for the previously identified 30-kDal MeT. We have compared the amino acid (aa) sequence of the ksgA-encoded enzyme with three published sequences of MeT involved in dimethylation of an adenosine residue in 23S RNA and rendering the organisms resistant to the MLS antibiotics. The homologous patches in the sequences of all four enzymes suggest that those might correspond to contact points for the common substrates, e.g., for the adenosine residue(s) and S-adenosylmethionine (SAM).
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3905517 PubMed]

|-
!align=left |Keywords
||
Amino Acid Sequence; Aminoglycosides; Anti-Bacterial Agents; Base Sequence; Cloning, Molecular; Codon; Drug Resistance, Microbial; Escherichia coli/genetics; Gene Expression Regulation; Genes, Bacterial; Methylation; Methyltransferases/genetics; Methyltransferases/metabolism; RNA, Ribosomal/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182884.T50f187dd33c71&page=182884&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="U50f187dd5155f" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182884.U50f187dd5155f&page=182884&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:3905517

2013-01-12T15:57:17Z

66.249.73.133: New PMID: Page!

PMID:16946247

2013-01-12T15:56:32Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="A50f187b029c76" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Ciampi, MS ''' (2006) Rho-dependent terminators and transcription termination. ''Microbiology (Reading, Engl.)'' '''152''':2515-28
|-
!align=left |Abstract
||
Rho-dependent transcription terminators participate in sophisticated genetic regulatory mechanisms, in both bacteria and phages; they occur in regulatory regions preceding the coding sequences of genes and within coding sequences, as well as at the end of transcriptional units, to prevent readthrough transcription. Most Rho-dependent terminators have been found in enteric bacteria, but they also occur in Gram-positive bacteria and may be widespread among bacteria. Rho-dependent termination requires both cis-acting elements, on the mRNA, and trans-acting factors. The only cis-acting element common to Rho-dependent terminators is richness in rC residues. Additional sequence elements have been observed at different Rho termination sites. These 'auxiliary elements' may assist in the termination process; they differ among terminators, their occurrence possibly depending on the function and sequence context of the terminator. Specific nucleotides required for termination have also been identified at Rho sites. Rho is the main factor required for termination; it is a ring-shaped hexameric protein with ATPase and helicase activities. NusG, NusA and NusB are additional factors participating in the termination process. Rho-dependent termination occurs by binding of Rho to ribosome-free mRNA, C-rich sites being good candidates for binding. Rho's ATPase is activated by Rho-mRNA binding, and provides the energy for Rho translocation along the mRNA; translocation requires sliding of the message into the central hole of the hexamer. When a polymerase pause site is encountered, the actual termination occurs, and the transcript is released by Rho's helicase activity. Many aspects of this process are still being studied. The isolation of mutants suppressing termination, site-directed mutagenesis of cis-acting elements in Rho-dependent termination, and biochemistry, are and will be contributing to unravelling the still undefined aspects of the Rho termination machinery. Analysis of the more sophisticated regulatory mechanisms relying on Rho-dependent termination may be crucial in identifying new essential elements for termination.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16946247 PubMed]
Online version:[http://dx.doi.org/10.1099/mic.0.28982-0 10.1099/mic.0.28982-0]
|-
!align=left |Keywords
||
Gene Expression Regulation, Bacterial; Models, Genetic; Rho Factor/chemistry; Rho Factor/genetics; Rho Factor/metabolism; Terminator Regions, Genetic/genetics; Transcription, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182883.A50f187b029c76&page=182883&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="X50f187b067432" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182883.X50f187b067432&page=182883&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:16946247

2013-01-12T15:56:32Z

66.249.73.133: New PMID: Page!

PMID:20497332

2013-01-12T15:52:28Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="X50f186bc529db" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Gibson, JL , Lombardo, MJ , Thornton, PC , Hu, KH , Galhardo, RS , Beadle, B , Habib, A , Magner, DB , Frost, LS , Herman, C , Hastings, PJ and Rosenberg, SM ''' (2010) The sigma(E) stress response is required for stress-induced mutation and amplification in Escherichia coli. ''Mol. Microbiol.'' '''77''':415-30
|-
!align=left |Abstract
||
Pathways of mutagenesis are induced in microbes under adverse conditions controlled by stress responses. Control of mutagenesis by stress responses may accelerate evolution specifically when cells are maladapted to their environments, i.e. are stressed. Stress-induced mutagenesis in the Escherichia coli Lac assay occurs either by 'point' mutation or gene amplification. Point mutagenesis is associated with DNA double-strand-break (DSB) repair and requires DinB error-prone DNA polymerase and the SOS DNA-damage- and RpoS general-stress responses. We report that the RpoE envelope-protein-stress response is also required. In a screen for mutagenesis-defective mutants, we isolated a transposon insertion in the rpoE P2 promoter. The insertion prevents rpoE induction during stress, but leaves constitutive expression intact, and allows cell viability. rpoE insertion and suppressed null mutants display reduced point mutagenesis and maintenance of amplified DNA. Furthermore, sigma(E) acts independently of stress responses previously implicated: SOS/DinB and RpoS, and of sigma(32), which was postulated to affect mutagenesis. I-SceI-induced DSBs alleviated much of the rpoE phenotype, implying that sigma(E) promoted DSB formation. Thus, a third stress response and stress input regulate DSB-repair-associated stress-induced mutagenesis. This provides the first report of mutagenesis promoted by sigma(E), and implies that extracytoplasmic stressors may affect genome integrity and, potentially, the ability to evolve.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20497332 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2909356 PMC2909356]
Online version:[http://dx.doi.org/10.1111/j.1365-2958.2010.07213.x 10.1111/j.1365-2958.2010.07213.x]
|-
!align=left |Keywords
||
DNA Breaks, Double-Stranded; DNA Repair; DNA Transposable Elements; DNA, Bacterial/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutagenesis, Insertional; Point Mutation; Promoter Regions, Genetic; SOS Response (Genetics); Sigma Factor/genetics; Sigma Factor/metabolism; Stress, Physiological

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182882.X50f186bc529db&page=182882&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="W50f186bc8887c" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182882.W50f186bc8887c&page=182882&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:20497332

2013-01-12T15:52:28Z

66.249.73.133: New PMID: Page!

PMID:8643363

2013-01-12T14:41:11Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="F50f17606e5e13" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Liu, H , Yap, LP , Stehlin, C and Musier-Forsyth, K ''' (1995) Molecular recognition of tRNA(Pro) by Escherichia coli proline-tRNA synthetase. ''Nucleic Acids Symp. Ser.'' '''''':176-8
|-
!align=left |Abstract
||
We have investigated the molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase (ProRS) in vitro using semi-synthetic tRNAs and site-directed mutagenesis of full-length tRNA transcripts. These studies have led to an improved understanding of how this class II synthetase interacts with its tRNA substrate. The ability to efficiently aminoacylate a tRNA(Pro) molecule assembled by annealing together a shorter, chemically synthesized oligonucleotide and a 3/4 tRNA prepared enzymatically, has facilitated the identification of RNA structural features that are critical for aminoacylation by ProRS. This approach has been successful using either a 3'-3/4 tRNA annealed to a 5'-oligonucleotide or a 5'-3/4 tRNA annealed to a 3'-oligonucleotide. These studies show that ProRS appears to be particularly sensitive to mutations that result in structural changes in the core region of tRNA(Pro). Moreover, the so-called "variable pocket" nucleotides appear to be dispensable for aminoacylation. We have also identified a specific 2'-hydroxyl-base interaction between the ribose of U8 and the 2-amino group of G46 that makes a thermodynamically significant contribution to tRNA(Pro) aminoacylation by E. coli ProRS.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8643363 PubMed]

|-
!align=left |Keywords
||
Amino Acyl-tRNA Synthetases/metabolism; Base Sequence; Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Hydroxylation; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RNA, Transfer, Pro/chemistry; RNA, Transfer, Pro/genetics; RNA, Transfer, Pro/metabolism; Thermodynamics

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182881.F50f17606e5e13&page=182881&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="S50f1760736efb" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182881.S50f1760736efb&page=182881&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:8643363

2013-01-12T14:41:10Z

66.249.73.133: New PMID: Page!

PMID:13499364

2013-01-12T10:42:05Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="I50f13dfd83eba" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''KORNBERG, SR ''' (1957) Adenosine triphosphate synthesis from polyphosphate by an enzyme from Escherichia coli. ''Biochim. Biophys. Acta'' '''26''':294-300
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=13499364 PubMed]

|-
!align=left |Keywords
||
Adenosine Triphosphate/metabolism; Escherichia coli/metabolism; Phosphates/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182879.I50f13dfd83eba&page=182879&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="P50f13dfd98073" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182879.P50f13dfd98073&page=182879&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:13499364

2013-01-12T10:42:05Z

66.249.73.133: New PMID: Page!

PMID:4921664

2013-01-12T10:29:08Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="P50f13af4321c5" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Knippers, R ''' (1970) DNA polymerase II. ''Nature'' '''228''':1050-3
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4921664 PubMed]

|-
!align=left |Keywords
||
Cell-Free System; Centrifugation, Density Gradient; Chromatography, Gel; DNA Nucleotidyltransferases/isolation & purification; Escherichia coli/enzymology; Membranes/enzymology; Molecular Weight; Solubility

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182878.P50f13af4321c5&page=182878&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="P50f13af44adc9" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182878.P50f13af44adc9&page=182878&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4921664

2013-01-12T10:29:08Z

66.249.73.133: New PMID: Page!

PMID:20639336

2013-01-12T10:03:55Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="J50f1350b8b1d2" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Frisch, RL , Su, Y , Thornton, PC , Gibson, JL , Rosenberg, SM and Hastings, PJ ''' (2010) Separate DNA Pol II- and Pol IV-dependent pathways of stress-induced mutation during double-strand-break repair in Escherichia coli are controlled by RpoS. ''J. Bacteriol.'' '''192''':4694-700
|-
!align=left |Abstract
||
Previous work showed that about 85% of stress-induced mutations associated with DNA double-strand break repair in carbon-starved Escherichia coli result from error-prone DNA polymerase IV (Pol IV) (DinB) and that the mutagenesis is controlled by the RpoS stress response, which upregulates dinB. We report that the remaining mutagenesis requires high-fidelity Pol II, and that this component also requires RpoS. The results identify a second DNA polymerase contributing to stress-induced mutagenesis and show that RpoS promotes mutagenesis by more than the simple upregulation of dinB.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20639336 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2937414 PMC2937414]
Online version:[http://dx.doi.org/10.1128/JB.00570-10 10.1128/JB.00570-10]
|-
!align=left |Keywords
||
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; DNA Polymerase II/genetics; DNA Polymerase II/metabolism; DNA Polymerase beta/genetics; DNA Polymerase beta/metabolism; DNA Repair/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mutagenesis; Mutation/genetics; Sigma Factor/genetics; Sigma Factor/metabolism; Signal Transduction/genetics; Signal Transduction/physiology

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182877.J50f1350b8b1d2&page=182877&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="L50f1350bbcff5" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182877.L50f1350bbcff5&page=182877&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:20639336

2013-01-12T10:03:55Z

66.249.73.133: New PMID: Page!

PMID:8

2013-01-12T09:41:15Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="B50f12fbb6921a" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Moroi, K and Sato, T ''' (1975) Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase. ''Biochem. Pharmacol.'' '''24''':1517-21
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8 PubMed]

|-
!align=left |Keywords
||
Amidohydrolases/metabolism; Animals; Esterases/metabolism; Hydrogen-Ion Concentration; Isocarboxazid/metabolism; Kinetics; Male; Metals/pharmacology; Microsomes, Liver/enzymology; Phospholipids/metabolism; Procaine/metabolism; Proteins/metabolism; Rats; Subcellular Fractions/enzymology; Temperature

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182876.B50f12fbb6921a&page=182876&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="Q50f12fbb8e897" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182876.Q50f12fbb8e897&page=182876&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:8

2013-01-12T09:41:15Z

66.249.73.133: New PMID: Page!

PMID:3052268

2013-01-12T09:05:40Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="V50f12764c38fc" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Anraku, Y ''' (1988) Bacterial electron transport chains. ''Annu. Rev. Biochem.'' '''57''':101-32
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3052268 PubMed]
Online version:[http://dx.doi.org/10.1146/annurev.bi.57.070188.000533 10.1146/annurev.bi.57.070188.000533]
|-
!align=left |Keywords
||
Bacteria, Aerobic/metabolism; Electron Transport

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182875.V50f12764c38fc&page=182875&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="T50f12764d8b82" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182875.T50f12764d8b82&page=182875&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:3052268

2013-01-12T09:05:40Z

66.249.73.133: New PMID: Page!

PMID:21779320

2013-01-12T08:32:48Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="Q50f11fafed881" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Engelen, K , Fu, Q , Meysman, P , Sánchez-Rodríguez, A , De Smet, R , Lemmens, K , Fierro, AC and Marchal, K ''' (2011) COLOMBOS: access port for cross-platform bacterial expression compendia. ''PLoS ONE'' '''6''':e20938
|-
!align=left |Abstract
||
Microarrays are the main technology for large-scale transcriptional gene expression profiling, but the large bodies of data available in public databases are not useful due to the large heterogeneity. There are several initiatives that attempt to bundle these data into expression compendia, but such resources for bacterial organisms are scarce and limited to integration of experiments from the same platform or to indirect integration of per experiment analysis results.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21779320 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3136457 PMC3136457]
Online version:[http://dx.doi.org/10.1371/journal.pone.0020938 10.1371/journal.pone.0020938]
|-
!align=left |Keywords
||
Bacillus subtilis/genetics; Databases, Genetic; Escherichia coli/genetics; Oligonucleotide Array Sequence Analysis; Salmonella enterica/genetics

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182874.Q50f11fafed881&page=182874&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="F50f11fb03ce11" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182874.F50f11fb03ce11&page=182874&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:21779320

2013-01-12T08:32:47Z

66.249.73.133: New PMID: Page!

PMID:17889824

2013-01-12T05:57:30Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="Q50f0fb4a2c27f" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Gulmezian, M , Hyman, KR , Marbois, BN , Clarke, CF and Javor, GT ''' (2007) The role of UbiX in Escherichia coli coenzyme Q biosynthesis. ''Arch. Biochem. Biophys.'' '''467''':144-53
|-
!align=left |Abstract
||
The reversible redox chemistry of coenzyme Q serves a crucial function in respiratory electron transport. Biosynthesis of Q in Escherichia coli depends on the ubi genes. However, very little is known about UbiX, an enzyme thought to be involved in the decarboxylation step in Q biosynthesis in E. coli and Salmonella enterica. Here we characterize an E. coli ubiX gene deletion strain, LL1, to further elucidate E. coli ubiX function in Q biosynthesis. LLI produces very low levels of Q, grows slowly on succinate as the sole carbon source, accumulates 4-hydroxy-3-octaprenyl-benzoate, and has reduced UbiG O-methyltransferase activity. Expression of either E. coli ubiX or the Saccharomyces cerevisiae ortholog PAD1, rescues the deficient phenotypes of LL1, identifying PAD1 as an ortholog of ubiX. Our results suggest that both UbiX and UbiD are required for the decarboxylation of 4-hydroxy-3-octaprenyl-benzoate in E. coli coenzyme Q biosynthesis, especially during logarithmic growth.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17889824 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2475804 PMC2475804]
Online version:[http://dx.doi.org/10.1016/j.abb.2007.08.009 10.1016/j.abb.2007.08.009]
|-
!align=left |Keywords
||
Carboxy-Lyases/metabolism; Cell Proliferation; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial/physiology; Gene Expression Regulation, Enzymologic/physiology; Ubiquinone/biosynthesis

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182871.Q50f0fb4a2c27f&page=182871&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="R50f0fb4a49bba" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182871.R50f0fb4a49bba&page=182871&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:17889824

2013-01-12T05:57:30Z

66.249.73.133: New PMID: Page!

PMID:16756481

2013-01-12T05:43:17Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="O50f0f7f57014d" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Lee, PA , Tullman-Ercek, D and Georgiou, G ''' (2006) The bacterial twin-arginine translocation pathway. ''Annu. Rev. Microbiol.'' '''60''':373-95
|-
!align=left |Abstract
||
The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16756481 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2654714 PMC2654714]
Online version:[http://dx.doi.org/10.1146/annurev.micro.60.080805.142212 10.1146/annurev.micro.60.080805.142212]
|-
!align=left |Keywords
||
Amino Acid Sequence; Bacterial Proteins/metabolism; Biotechnology; Escherichia coli Proteins/physiology; Membrane Transport Proteins/physiology; Molecular Sequence Data; Protein Folding; Protein Sorting Signals; Protein Transport; Quality Control

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182870.O50f0f7f57014d&page=182870&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="W50f0f7f591b72" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182870.W50f0f7f591b72&page=182870&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:16756481

2013-01-12T05:43:17Z

66.249.73.133: New PMID: Page!

PMID:18067539

2013-01-12T04:45:00Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="A50f0ea4c4d58d" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Pennetier, C , Domínguez-Ramírez, L and Plumbridge, J ''' (2008) Different regions of Mlc and NagC, homologous transcriptional repressors controlling expression of the glucose and N-acetylglucosamine phosphotransferase systems in Escherichia coli, are required for inducer signal recognition. ''Mol. Microbiol.'' '''67''':364-77
|-
!align=left |Abstract
||
Mlc and NagC are two homologous transcription factors which bind to similar DNA targets but for which the inducing signals and mechanisms of activation are very different. Displacing Mlc from its DNA binding sites necessitates its sequestration to the inner membrane via an interaction with PtsG (EIICB(Glc)), while NagC is displaced from its DNA targets by interacting with GlcNAc6P. We have isolated mutations in both proteins which prevent the inactivation of the repressors by growth on glucose or GlcNAc. These mutations are located in different and specific regions of each protein. For Mlc changes at the C-terminal make it a constitutive repressor and also prevent it from binding to EIIB(Glc). Mutations in NagC, at positions which form a structural motif resembling a glucose binding site in Mlc, produce permanently repressing forms of NagC, suggesting that this motif forms a GlcNAc6P binding site in NagC. The pattern of repression by chimeric proteins of NagC and Mlc confirms the importance of the C-terminal region of Mlc for both repression and inducer binding and demonstrate that the helix-turn-helix DNA-binding motif is not sufficient to determine the specificity of interaction of the repressor with DNA.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18067539 PubMed]
Online version:[http://dx.doi.org/10.1111/j.1365-2958.2007.06041.x 10.1111/j.1365-2958.2007.06041.x]
|-
!align=left |Keywords
||
Acetylglucosamine/analogs & derivatives; Acetylglucosamine/metabolism; Amino Acid Sequence; Electrophoretic Mobility Shift Assay; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Dosage; Glucose/metabolism; Helix-Turn-Helix Motifs; Models, Molecular; Molecular Sequence Data; Operator Regions, Genetic; Phosphotransferases/genetics; Plasmids; Point Mutation; Protein Structure, Tertiary; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/metabolism; Sequence Alignment; Sequence Deletion; Signal Transduction; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/metabolism; Transcription, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182869.A50f0ea4c4d58d&page=182869&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="Y50f0ea4c7617a" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182869.Y50f0ea4c7617a&page=182869&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:18067539

2013-01-12T04:45:00Z

66.249.73.133: New PMID: Page!

PMID:1916241

2013-01-12T04:44:15Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="T50f0ea1ef2533" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Cairns, J and Foster, PL ''' (1991) Adaptive reversion of a frameshift mutation in Escherichia coli. ''Genetics'' '''128''':695-701
|-
!align=left |Abstract
||
Mutation rates are generally thought not to be influenced by selective forces. This doctrine rests on the results of certain classical studies of the mutations that make bacteria resistant to phages and antibiotics. We have studied a strain of Escherichia coli which constitutively expresses a lacI-lacZ fusion containing a frameshift mutation that renders it Lac-. Reversion to Lac+ is a rare event during exponential growth but occurs in stationary cultures when lactose is the only source of energy. No revertants accumulate in the absence of lactose, or in the presence of lactose if there is another, unfulfilled requirement for growth. The mechanism for such mutation in stationary phase is not known, but it requires some function of RecA which is apparently not required for mutation during exponential growth.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1916241 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1204544 PMC1204544]

|-
!align=left |Keywords
||
Adaptation, Biological/genetics; Adaptation, Biological/physiology; Alleles; Escherichia coli/genetics; Escherichia coli/physiology; Frameshift Mutation/genetics; Frameshift Mutation/physiology; Gene Expression Regulation, Bacterial; Genes, Bacterial/genetics; Genes, Bacterial/physiology; Genetic Variation; Lac Operon/genetics; Lac Operon/physiology; Lactose/metabolism; Lactose/pharmacology; Tryptophan/metabolism; Tryptophan/pharmacology

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182868.T50f0ea1ef2533&page=182868&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="I50f0ea1f1876d" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182868.I50f0ea1f1876d&page=182868&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:1916241

2013-01-12T04:44:14Z

66.249.73.133: New PMID: Page!

PMID:2563997

2013-01-12T04:10:12Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="Q50f0e223df1f5" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Fayet, O , Ziegelhoffer, T and Georgopoulos, C ''' (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. ''J. Bacteriol.'' '''171''':1379-85
|-
!align=left |Abstract
||
The products of the groES and groEL genes of Escherichia coli, constituting the groE operon, are known to be required for growth at high temperature (42 degrees C) and are members of the heat shock regulon. Using a genetic approach, we examined the requirement for these gene products for bacterial growth at low temperature (17 to 30 degrees C). To do this, we constructed various groES groEL heterodiploid derivative strains. By inactivating one of the groE operons by a polar insertion, it was shown by bacteriophage P1 transduction that at least one of the groE genes was essential for growth at low temperature. Further P1 transduction experiments with strains that were heterodiploid for only one of the groE genes demonstrated that both groE gene products were required for growth at low temperature, which suggested a fundamental role for the groE proteins in E. coli growth and physiology.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2563997 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC209756 PMC209756]

|-
!align=left |Keywords
||
Bacterial Proteins/genetics; Blotting, Western; Chaperonin 10; Chaperonin 60; Escherichia coli/genetics; Escherichia coli/growth & development; Genes; Genes, Bacterial; Genes, Regulator; Genotype; Heat-Shock Proteins/genetics; Operon; Phenotype; Temperature; Transduction, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182867.Q50f0e223df1f5&page=182867&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="U50f0e22401e30" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182867.U50f0e22401e30&page=182867&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:2563997

2013-01-12T04:10:11Z

66.249.73.133: New PMID: Page!

PMID:1657895

2013-01-12T04:03:52Z

66.249.73.133: Fill PMID: Page!

{{RightTOC}}


{| id="S50f0e0a857df1" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Sharples, GJ and Lloyd, RG ''' (1991) Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein. ''J. Bacteriol.'' '''173''':7711-5
|-
!align=left |Abstract
||
The ruvC gene of Escherichia coli specifies a nuclease that resolves Holliday junction intermediates in genetic recombination (B. Connolly, C.A. Parsons, F.E. Benson, H.J. Dunderdale, G.J. Sharples, R.G. Lloyd, and S.C. West, Proc. Natl. Acad, Sci. USA 88:6063-6067, 1991). The gene was located between aspS and the ruvAB operon by DNA sequencing and deletion analysis of ruvC plasmids and was shown to encode a protein of 18,747 Da. Analysis of the DNA flanking ruvC indicated that the gene is transcribed independently of the LexA-regulated ruvAB operon and is not under direct SOS control. ruvC lies downstream of an open reading frame, orf-33, for a protein which migrates during sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a 33-kDa polypeptide. These two genes probably form an operon. However, expression of ruvC was found to be very poor relative to that of orf-33. A double ribosomal frameshift between these genes is proposed as a possible reason for the low level of RuvC. Two further open reading frames of unknown function were identified, one on either side of the orf-33-ruvC operon.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1657895 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC212543 PMC212543]

|-
!align=left |Keywords
||
Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Endodeoxyribonucleases; Escherichia coli/genetics; Escherichia coli Proteins; Genes, Bacterial; Molecular Sequence Data; Molecular Weight; Nucleotidyltransferases/genetics; Open Reading Frames; Operon; Plasmids; Recombination, Genetic; Restriction Mapping; Sequence Homology, Nucleic Acid; Transposases

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182866.S50f0e0a857df1&page=182866&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="M50f0e0a87e2e7" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.182866.M50f0e0a87e2e7&page=182866&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:1657895

2013-01-12T04:03:52Z

66.249.73.133: New PMID: Page!