https://ecoliwiki.org/colipedia/api.php?action=feedcontributions&feedformat=atom&user=176.9.118.209EcoliWiki - User contributions [en]2026-11-06T00:43:39ZUser contributionsMediaWiki 1.43.11https://ecoliwiki.org/colipedia/index.php?title=User:TestUser3&diff=1491721User:TestUser32014-08-18T10:23:54Z<p>176.9.118.209: Fill User: Page!</p>
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<div>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. <br />
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jh, jh<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=User:TestUser3&diff=1491720User:TestUser32014-08-18T10:23:54Z<p>176.9.118.209: New User: Page!</p>
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<div></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4332555&diff=1491717PMID:43325552014-08-16T11:25:00Z<p>176.9.118.209: Fill PMID: Page!</p>
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{| id="Y53ef3f8b6bafa" class=" tableEdit PMID_info_table" <br />
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|-<br />
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'''Joseph, DR and Muench, KH''' (1971) Tryptophanyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification of the enzyme and of tryptrophan transfer ribonucleic acid. ''J. Biol. Chem.'' '''246''':7602-9<br />
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!align=left |Abstract<br />
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No abstract in PubMed<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4332555 PubMed]<br />
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!align=left |Keywords<br />
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Adenosine Triphosphate; Amino Acids/analysis; Amino Acyl-tRNA Synthetases/analysis; Amino Acyl-tRNA Synthetases/isolation & purification; Benzoates; Carbon Isotopes; Catalysis; Chemical Precipitation; Chromatography; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Diphosphates; Electrophoresis, Disc; Escherichia coli/analysis; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Hydroxyapatites; Isoelectric Focusing; Kinetics; Manganese; Molecular Weight; RNA, Bacterial/isolation & purification; RNA, Transfer/isolation & purification; Tryptophan<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br />
{{LitMaterials}}<br />
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==Annotations {{HelpIcon|Help:Literature}}==<br />
<annotationlinks/><br />
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br />
{{LitLinks}}<br />
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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4332555&diff=1491716PMID:43325552014-08-16T11:24:59Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:19383770&diff=1491710PMID:193837702014-08-13T14:26:22Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Golovina, AY, Sergiev, PV, Golovin, AV, Serebryakova, MV, Demina, I, Govorun, VM and Dontsova, OA''' (2009) The yfiC gene of E. coli encodes an adenine-N6 methyltransferase that specifically modifies A37 of tRNA1Val(cmo5UAC). ''RNA'' '''15''':1134-41<br />
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Transfer RNA is highly modified. Nucleotide 37 of the anticodon loop is represented by various modified nucleotides. In Escherichia coli, the valine-specific tRNA (cmo(5)UAC) contains a unique modification, N(6)-methyladenosine, at position 37; however, the enzyme responsible for this modification is unknown. Here we demonstrate that the yfiC gene of E. coli encodes an enzyme responsible for the methylation of A37 in tRNA(1)(Val). Inactivation of yfiC gene abolishes m(6)A formation in tRNA(1)(Val), while expression of the yfiC gene from a plasmid restores the modification. Additionally, unmodified tRNA(1)(Val) can be methylated by recombinant YfiC protein in vitro. Although the methylation of m(6)A in tRNA(1)(Val) by YfiC has little influence on the cell growth under standard conditions, the yfiC gene confers a growth advantage under conditions of osmotic and oxidative stress.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19383770 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2685529 PMC2685529]<br />
Online version:[http://dx.doi.org/10.1261/rna.1494409 10.1261/rna.1494409]<br />
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Adenosine/analogs & derivatives; Adenosine/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial; Methylation; Methyltransferases/genetics; Methyltransferases/metabolism; Oxidative Stress; RNA, Transfer, Val/genetics; RNA, Transfer, Val/metabolism; tRNA Methyltransferases/genetics; tRNA Methyltransferases/metabolism<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:19383770&diff=1491709PMID:193837702014-08-13T14:26:22Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:10521257&diff=1491664PMID:105212572014-08-08T03:52:54Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Williams, NL and Maxwell, A''' (1999) Probing the two-gate mechanism of DNA gyrase using cysteine cross-linking. ''Biochemistry'' '''38''':13502-11<br />
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!align=left |Abstract<br />
||<br />
Cross-linking a pair of novel cysteine residues on either side of the bottom dimer interface of DNA gyrase blocks catalytic supercoiling. Limited strand passage is allowed, but release of the transported DNA segment (T segment) via opening of the bottom dimer interface is prevented. In contrast, ATP-independent relaxation of negatively supercoiled DNA is completely abolished, suggesting that T-segment entry via the bottom gate is blocked. These findings support a two-gate model for supercoiling by DNA gyrase and suggest that relaxation by gyrase is the reverse of supercoiling. Cross-linking a truncated version of gyrase (A64(2)B2), which lacks the DNA wrapping domains, does not block ATP-dependent relaxation. This indicates that passage of DNA through the bottom dimer interface is not essential for this reaction. The mechanistic implications of these results are discussed.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10521257 PubMed]<br />
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!align=left |Keywords<br />
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Adenosine Triphosphate/antagonists & inhibitors; Adenosine Triphosphate/chemistry; Calcium/chemistry; Catalysis; Cross-Linking Reagents/chemistry; Cysteine/chemistry; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/metabolism; DNA, Bacterial/chemistry; DNA, Superhelical/chemistry; Dimerization; Disulfides/chemistry; Escherichia coli/enzymology; Hydrolysis; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments/chemistry; Peptide Fragments/genetics; Protein Engineering; Quinolones/chemistry<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:10521257&diff=1491663PMID:105212572014-08-08T03:52:54Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:11504719&diff=1491506PMID:115047192014-07-20T20:38:00Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Smelkova, N and Marians, KJ''' (2001) Timely release of both replication forks from oriC requires modulation of origin topology. ''J. Biol. Chem.'' '''276''':39186-91<br />
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Initiation of DNA replication at oriC occurs bidirectionally both in vivo and in vitro. Although the proteins involved in establishing the replication forks are known, little is known about the events that ensure that initiation is bidirectional. We show here that in the absence of DNA gyrase, replication fork progression from oriC on a plasmid template in vitro is unidirectional, although both replication forks have formed at the origin. There was no bias in the release of one fork or the other, ruling out protein blockage of one fork as a possible reason for the asymmetric release. Timely release of both forks required the presence of either DNA gyrase or topoisomerase IV, suggesting that modulation of the topology of the origin region is the governing factor.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11504719 PubMed]<br />
Online version:[http://dx.doi.org/10.1074/jbc.M104411200 10.1074/jbc.M104411200]<br />
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Bacterial Proteins; Blotting, Western; Cross-Linking Reagents/pharmacology; DNA Gyrase/metabolism; DNA Helicases/metabolism; DNA Replication/genetics; DNA Replication/physiology; DnaB Helicases; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Models, Genetic; Protein Binding; Time Factors<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:11504719&diff=1491505PMID:115047192014-07-20T20:37:59Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:2150914&diff=1491484PMID:21509142014-07-16T04:32:11Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Xue, MQ and Black, LW''' Role of the major capsid protein of phage T4 in DNA packaging from structure-function and site-directed mutagenesis studies. ''J. Struct. Biol.'' '''104''':75-83<br />
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Heat cleavage of asp-pro peptide bonds was used to probe the primary structures of the Phage T4 major capsid protein precursor, gp23, its mature capsid form gp23*, and a DNA-dependent ATPase, called capsizyme. This analysis suggests that capsizyme is a gp23** resulting from the N-terminal processing found in gp23* as well as shortening at the C-terminus. Photoaffinity labeling with Azido-ATP and BrU-DNA, followed by heat cleavage, suggests binding sites for these compounds toward the C-terminus of gp23**, suggesting localization of functions within the gp23 primary sequence. Site-directed mutagenesis experiments were targeted therefore to the C-terminal end of g23 as well as to its processing sites. N-terminal processing site modification supports the consensus gp21 proteinase cleavage rule, whereas mutagenesis at the C-terminus suggests that the C-terminal alteration is unlikely to result from a gp21-morphogenesis proteinase cleavage. Amino acid replacements in gp23 at newly introduced amber sites reveal a new g23 mutant phenotype, defective partially DNA-filled heads, in support of the hypothesis that gp23 and its products function directly in the DNA packaging mechanism.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2150914 PubMed]<br />
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Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Base Sequence; Binding Sites; Capsid/genetics; Capsid/metabolism; Capsid/ultrastructure; Capsid Proteins; DNA, Viral/genetics; DNA, Viral/metabolism; DNA, Viral/ultrastructure; Escherichia coli/genetics; Escherichia coli/metabolism; Hot Temperature; Microscopy, Electron; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotide Probes; Protein Precursors/genetics; Protein Precursors/metabolism; T-Phages/genetics; T-Phages/metabolism; T-Phages/ultrastructure<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:2150914&diff=1491483PMID:21509142014-07-16T04:32:11Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:8633085&diff=1491450PMID:86330852014-07-12T08:43:54Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Hesterkamp, T, Hauser, S, Lütcke, H and Bukau, B''' (1996) Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. ''Proc. Natl. Acad. Sci. U.S.A.'' '''93''':4437-41<br />
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Correct folding of newly synthesized proteins is proposed to be assisted by molecular chaperones and folding catalysts. To identify cellular factors involved in the initial stages of this process we searched for proteins associated with nascent polypeptide chains. In an Escherichia coli transcription/translation system synthesizing beta-galactosidase we identified a 58-kDa protein which associated with translating ribosomes but dissociated from these ribosomes upon release of nascent beta-galactosidase. N-terminal sequencing identified it as trigger factor, previously implicated in protein secretion. Direct evidence for association of trigger factor with nascent polypeptide chains was obtained by crosslinking. In a wheat germ translation system complemented with E. coli lysates, epsilon-4-(3-trifluoromethyldiazirino)benzoic acid-lysine residues were incorporated into nascent secretory preprolactin and a nonsecretory preprolactin mutant. Trigger factor crosslinked to both types of nascent chains, provided they were ribosome bound. Trigger factor contains key residues of the substrate-binding pocket of FK506-binding protein-type peptidyl-prolyl-cis/trans-isomerases and has prolyl isomerase activity in vitro. We propose that trigger factor is a folding catalyst acting cotranslationally.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8633085 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC39556 PMC39556]<br />
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Amino Acid Isomerases/chemistry; Amino Acid Isomerases/isolation & purification; Amino Acid Isomerases/metabolism; Amino Acid Sequence; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Carrier Proteins/chemistry; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism; Chaperonins/metabolism; Cross-Linking Reagents; DNA-Binding Proteins/chemistry; Escherichia coli/metabolism; Heat-Shock Proteins/chemistry; Humans; Kinetics; Molecular Sequence Data; Mutagenesis; Peptidylprolyl Isomerase; Prolactin/biosynthesis; Protein Biosynthesis; Protein Folding; Protein Precursors/biosynthesis; Puromycin/pharmacology; Ribosomes/drug effects; Ribosomes/metabolism; Sequence Homology, Amino Acid; Tacrolimus Binding Proteins; Transcription, Genetic; Triticum; beta-Galactosidase/biosynthesis<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:8633085&diff=1491449PMID:86330852014-07-12T08:43:53Z<p>176.9.118.209: New PMID: Page!</p>
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'''Harrison, JJ, Wade, WD, Akierman, S, Vacchi-Suzzi, C, Stremick, CA, Turner, RJ and Ceri, H''' (2009) The chromosomal toxin gene yafQ is a determinant of multidrug tolerance for Escherichia coli growing in a biofilm. ''Antimicrob. Agents Chemother.'' '''53''':2253-8<br />
|-<br />
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||<br />
Escherichia coli is refractory to elevated doses of antibiotics when it is growing in a biofilm, and this is potentially due to high numbers of multidrug-tolerant persister cells in the surface-adherent population. Previously, the chromosomal toxin-antitoxin loci hipBA and relBE have been linked to the frequency at which persister cells occur in E. coli populations. In the present study, we focused on the dinJ-yafQ-encoded toxin-antitoxin system and hypothesized that deletion of the toxin gene yafQ might influence cell survival in antibiotic-exposed biofilms. By using confocal laser scanning microscopy and viable cell counting, it was determined that a Delta yafQ mutant produced biofilms with a structure and a cell density equivalent to those of the parental strain. In-depth susceptibility testing identified that relative to wild-type E. coli, the Delta yafQ strain had up to a approximately 2,400-fold decrease in cell survival after the biofilms were exposed to bactericidal concentrations of cefazolin or tobramycin. Corresponding to these data, controlled overexpression of yafQ from a high-copy-number plasmid resulted in up to a approximately 10,000-fold increase in the number of biofilm cells surviving exposure to these bactericidal drugs. In contrast, neither the inactivation nor the overexpression of yafQ affected the tolerance of biofilms to doxycycline or rifampin (rifampicin). Furthermore, deletion of yafQ did not affect the tolerance of stationary-phase planktonic cells to any of the antibacterials tested. These results suggest that yafQ mediates the tolerance of E. coli biofilms to multiple but specific antibiotics; moreover, our data imply that this cellular pathway for persistence is likely different from that of multidrug-tolerant cells in stationary-phase planktonic cell cultures.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19307375 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2687228 PMC2687228]<br />
Online version:[http://dx.doi.org/10.1128/AAC.00043-09 10.1128/AAC.00043-09]<br />
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||<br />
Bacterial Toxins/genetics; Biofilms/drug effects; Drug Resistance, Multiple, Bacterial/genetics; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli Proteins/genetics; Plankton/microbiology<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:19307375&diff=1491435PMID:193073752014-07-09T12:24:47Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:17679694&diff=1491428PMID:176796942014-07-09T01:38:53Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Fujisawa, M, Ito, M and Krulwich, TA''' (2007) Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity. ''Proc. Natl. Acad. Sci. U.S.A.'' '''104''':13289-94<br />
|-<br />
!align=left |Abstract<br />
||<br />
Properties of four two-component bacterial transport systems of the cation/proton antiporter-2 (CPA2) family led to suggestions that this CPA2 subset may use a channel rather than an antiport mechanism [see Booth IR, Edwards MD, Gunasekera B, Li C, Miller S (2005) in Bacterial Ion Channels, eds Kubalski A, Martinac B (Am Soc Microbiol, Washington, DC), pp 21-40]. The transporter subset includes the intensively studied glutathione-gated K(+) efflux systems from Escherichia coli, KefGB, and KefFC. KefG and KefF are ancillary proteins. They are peripheral membrane proteins that are encoded in operons with the respective transporter proteins, KefB and KefC, and are required for optimal efflux activity. The other two-component CPA2 transporters of the subset are AmhMT, an NH(4)(+) (K(+)) efflux system from alkaliphilic Bacillus pseudofirmus OF4; and YhaTU, a K(+) efflux system from Bacillus subtilis. Here a K(+)/H(+) antiport capacity was demonstrated for YhaTU, AmhMT, and KefFC in membrane vesicles from antiporter-deficient E. coli KNabc. The apparent K(m) for K(+) was in the low mM range. The peripheral protein was required for YhaU- and KefC-dependent antiport, whereas both AmhT and AmhMT exhibited antiport. KefFC had the broadest range of substrates, using Rb(+) approximately K(+)>Li(+)>Na(+). Glutathione significantly inhibited KefFC-mediated K(+)/H(+) antiport in vesicles. The inhibition was enhanced by NADH, which presumably binds to the KTN/RCK domain of KefC. The antiport mechanism accounts for the H(+) uptake involved in KefFC-mediated electrophile resistance in vivo. Because the physiological substrate of AmhMT in the alkaliphile is NH(4)(+), the results also imply that AmhMT catalyzes NH(4)(+)/H(+) antiport, which would prevent net cytoplasmic H(+) loss during NH(4)(+) efflux.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17679694 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1948933 PMC1948933]<br />
Online version:[http://dx.doi.org/10.1073/pnas.0703709104 10.1073/pnas.0703709104]<br />
|-<br />
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Cations, Monovalent/metabolism; Cloning, Molecular; Glutathione/physiology; Membrane Transport Proteins/metabolism; NAD/metabolism; Protons<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:17679694&diff=1491427PMID:176796942014-07-09T01:38:52Z<p>176.9.118.209: New PMID: Page!</p>
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'''Horwich, AL, Low, KB, Fenton, WA, Hirshfield, IN and Furtak, K''' (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. ''Cell'' '''74''':909-17<br />
|-<br />
!align=left |Abstract<br />
||<br />
A general role for chaperonin ring structures in mediating folding of newly translated proteins has been suggested. Here we have directly examined the role of the E. coli chaperonin GroEL in the bacterial cytoplasm by production of temperature-sensitive lethal mutations in this essential gene. After shift to nonpermissive temperature, the rate of general translation in the mutant cells was reduced, but, more specifically, a defined group of cytoplasmic proteins--including citrate synthase, ketoglutarate dehydrogenase, and polynucleotide phosphorylase--were translated but failed to reach native form. Similarly, a monomeric test protein, maltose-binding protein, devoid of its signal domain, was translated but failed to fold to its native conformation. We conclude that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8104102 PubMed]<br />
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ATP-Binding Cassette Transporters; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/genetics; Bacteriophage lambda/metabolism; Carrier Proteins/biosynthesis; Carrier Proteins/genetics; Chaperonin 60; Citrate (si)-Synthase/biosynthesis; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Ketoglutarate Dehydrogenase Complex/biosynthesis; Maltose/metabolism; Maltose-Binding Proteins; Methionine; Monosaccharide Transport Proteins; Operon; Ornithine Carbamoyltransferase/biosynthesis; Ornithine Carbamoyltransferase/genetics; Plasmids; Polyribonucleotide Nucleotidyltransferase/biosynthesis; Promoter Regions, Genetic; Protein Biosynthesis; Protein Folding; Protein Sorting Signals/metabolism; Sequence Deletion; Temperature; Transduction, Genetic<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:8104102&diff=1491417PMID:81041022014-07-05T14:38:03Z<p>176.9.118.209: New PMID: Page!</p>
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'''Anderson, A and Cooper, RA''' (1969) The significance of ribokinase for ribose utilization by Escherichia coli. ''Biochim. Biophys. Acta'' '''177''':163-5<br />
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No abstract in PubMed<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4889152 PubMed]<br />
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Culture Media; Enzyme Induction; Escherichia coli/enzymology; Glucose/pharmacology; Mutation; Phosphotransferases/metabolism; Ribose; Spectrophotometry; Succinates/pharmacology; Uridine/pharmacology<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4889152&diff=1491415PMID:48891522014-07-05T11:29:15Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:2215307&diff=1491328PMID:22153072014-06-28T12:11:25Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''McLaws, ML, Brown, AR, Cunningham, PH, Imrie, AA, Wilcken, B and Cooper, DA''' (1990) Prevalence of maternal HIV infection based on anonymous testing of neonates, Sydney 1989. ''Med. J. Aust.'' '''153''':383-6<br />
|-<br />
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||<br />
The presence of antibody to human immunodeficiency virus (HIV) in post-partum women may be inferred by screening the blood of their newborn babies, since maternal IgG antibodies freely cross the placenta. We tested a sample of 10,217 newborns from 10 hospitals covering three areas in Sydney and other metropolitan centres in New South Wales from April to July, 1989. None of the specimens gave a positive test for antibody to HIV. Thus, the prevalence of HIV positive serology in this sample of newborns was found to be zero. It was estimated that the seroprevalence of antibody to HIV among all neonates in the study area was between zero and 0.045% (99% confidence interval). Because newborns are an accessible group for the study of HIV, and can act as surrogates for their mothers, anonymous testing of this sentinel group will remove some of the limitations generalizing the information in the present database of HIV infection in Australia. This study provides baseline data and suggests that there is not a widespread epidemic of HIV infection among heterosexual persons in Australia at the present time and that routine antenatal testing of women for antibody to HIV may not be cost-effective. However, it will be important to repeat this study at regular intervals to detect any increase in HIV seroprevalence.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2215307 PubMed]<br />
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!align=left |Keywords<br />
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Adult; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Female; HIV Antibodies/blood; HIV Infections/epidemiology; HIV Seropositivity/epidemiology; HIV-1; Humans; Infant, Newborn; New South Wales/epidemiology; Prevalence; Urban Population/statistics & numerical data<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:2215307&diff=1491327PMID:22153072014-06-28T12:11:24Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:19233928&diff=1491292PMID:192339282014-06-23T18:18:44Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Gonzalez, MD and Beckwith, J''' (2009) Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. ''J. Bacteriol.'' '''191''':2815-25<br />
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||<br />
Cell division in bacteria requires the coordinated action of a set of proteins, the divisome, for proper constriction of the cell envelope. Multiple protein-protein interactions are required for assembly of a stable divisome. Within the Escherichia coli divisome is a conserved subcomplex of inner membrane proteins, the FtsB/FtsL/FtsQ complex, which is necessary for linking the upstream division proteins, which are predominantly cytoplasmic, with the downstream division proteins, which are predominantly periplasmic. FtsB and FtsL are small bitopic membrane proteins with predicted coiled-coil motifs, which themselves form a stable subcomplex that can recruit downstream division proteins independently of FtsQ; however, the details of how FtsB and FtsL interact together and with other proteins remain to be characterized. Despite the small size of FtsB, we identified separate interaction domains of FtsB that are required for interaction with FtsL and FtsQ. The N-terminal half of FtsB is necessary for interaction with FtsL and sufficient, when in complex with FtsL, for recruitment of downstream division proteins, while a portion of the FtsB C terminus is necessary for interaction with FtsQ. These properties of FtsB support the proposal that its main function is as part of a molecular scaffold to allow for proper formation of the divisome.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19233928 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668415 PMC2668415]<br />
Online version:[http://dx.doi.org/10.1128/JB.01597-08 10.1128/JB.01597-08]<br />
|-<br />
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||<br />
Cell Cycle Proteins/metabolism; Cell Division; Escherichia coli/growth & development; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Membrane Proteins/metabolism; Protein Interaction Domains and Motifs; Protein Interaction Mapping; Sequence Deletion<br />
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:19233928&diff=1491291PMID:192339282014-06-23T18:18:43Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0046797_!_viral_procapsid_maturation&diff=1491225Category:GO:0046797 ! viral procapsid maturation2014-06-22T00:27:25Z<p>176.9.118.209: New GO term category page</p>
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<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:11160901&diff=1491189PMID:111609012014-06-16T12:10:29Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''McCue, L, Thompson, W, Carmack, C, Ryan, MP, Liu, JS, Derbyshire, V and Lawrence, CE''' (2001) Phylogenetic footprinting of transcription factor binding sites in proteobacterial genomes. ''Nucleic Acids Res.'' '''29''':774-82<br />
|-<br />
!align=left |Abstract<br />
||<br />
Toward the goal of identifying complete sets of transcription factor (TF)-binding sites in the genomes of several gamma proteobacteria, and hence describing their transcription regulatory networks, we present a phylogenetic footprinting method for identifying these sites. Probable transcription regulatory sites upstream of Escherichia coli genes were identified by cross-species comparison using an extended Gibbs sampling algorithm. Close examination of a study set of 184 genes with documented transcription regulatory sites revealed that when orthologous data were available from at least two other gamma proteobacterial species, 81% of our predictions corresponded with the documented sites, and 67% corresponded when data from only one other species were available. That the remaining predictions included bona fide TF-binding sites was proven by affinity purification of a putative transcription factor (YijC) bound to such a site upstream of the fabA gene. Predicted regulatory sites for 2097 E.coli genes are available at http://www.wadsworth.org/resnres/bioinfo/.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11160901 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC30389 PMC30389]<br />
<br />
|-<br />
!align=left |Keywords<br />
||<br />
Base Sequence; Binding Sites/genetics; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; Databases, Factual; Escherichia coli/genetics; Gammaproteobacteria/genetics; Genes, Bacterial/genetics; Genome, Bacterial; Phylogeny; Protein Binding; Sequence Alignment; Sequence Homology, Nucleic Acid; Transcription Factors/metabolism<br />
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{{LitSignificance}}<br />
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br />
{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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<br />
==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:11160901&diff=1491188PMID:111609012014-06-16T12:10:29Z<p>176.9.118.209: New PMID: Page!</p>
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'''Ninfa, AJ and Bennett, RL''' (1991) Identification of the site of autophosphorylation of the bacterial protein kinase/phosphatase NRII. ''J. Biol. Chem.'' '''266''':6888-93<br />
|-<br />
!align=left |Abstract<br />
||<br />
Previous studies have established that the Escherichia coli protein kinase/phosphatase nitrogen regulator II (NRII also known as NtrB) becomes autophosphorylated on a histidine residue when incubated with ATP. We show that the major site at which NRII was autophosphorylated was contained within a peptide consisting of amino acid residues 136-142 of NRII, and thus probably corresponds to His-139. A minor site of phosphorylation, accounting for about 2% of the phosphate in NRII-P, was found in a peptide that corresponds to residues 158-169.<br />
|-<br />
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||<br />
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2016302 PubMed]<br />
<br />
|-<br />
!align=left |Keywords<br />
||<br />
Amino Acid Sequence; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Chromatography, High Pressure Liquid; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/metabolism; Escherichia coli/enzymology; Molecular Sequence Data; PII Nitrogen Regulatory Proteins; Peptide Fragments/isolation & purification; Phosphopeptides/isolation & purification; Phosphoprotein Phosphatases; Phosphorylation; Protein Kinases; Trans-Activators; Transcription Factors; Trypsin<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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{{LitLinks}}<br />
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{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:2016302&diff=1491184PMID:20163022014-06-16T11:25:05Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:8466915&diff=1491181PMID:84669152014-06-16T11:11:29Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Hayden, MA, Huang, IY, Iliopoulos, G, Orozco, M and Ashley, GW''' (1993) Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9. ''Biochemistry'' '''32''':3778-82<br />
|-<br />
!align=left |Abstract<br />
||<br />
The abilities of the Escherichia coli lipoic acid auxotrophs W1485-lip2 and JRG33-lip9 to grow on succinate medium in the presence of octanoate, 8-mercaptooctanoate, or 6-mercaptooctanoate have been determined. Both organisms are mutated in lipA. Neither organism can use octanoate or 6-mercaptooctanoate for production of lipoate, but the lip2 allele can use 8-mercaptooctanoate. Chromosomal DNA from the auxotrophs was amplified by PCR using primers derived from the DNA sequence of wild-type lipA and then sequenced. Both mutants contain single G/C to A/T mutations in lipA, resulting in conversion of Ser307 into Phe in W1485-lip2 and Glu195 into Lys in JRG33-lip9. These results support the hypothesis that lipA is involved in the sulfur insertion step(s) of lipoate biosynthesis and indicate that it is possible to selectively block formation of the C8-S bond through suitable mutation in lipA.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8466915 PubMed]<br />
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|-<br />
!align=left |Keywords<br />
||<br />
Amino Acid Sequence; Base Sequence; Caprylates/metabolism; DNA, Bacterial/chemistry; Deoxyribonuclease HindIII/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Molecular Sequence Data; Mutation; Polymerase Chain Reaction; Thioctic Acid/biosynthesis; Thioctic Acid/chemistry; Thioctic Acid/genetics<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br />
{{LitLinks}}<br />
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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:8466915&diff=1491180PMID:84669152014-06-16T11:11:28Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4579702&diff=1491175PMID:45797022014-06-15T13:57:24Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Ferenci, T and Kornberg, HL''' (1973) The utilization of fructose by Escherichia coli. Properties of a mutant defective in fructose 1-phosphate kinase activity. ''Biochem. J.'' '''132''':341-7<br />
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!align=left |Abstract<br />
||<br />
1. The isolation and properties of a mutant of Escherichia coli devoid of fructose 1-phosphate kinase activity are described. 2. This mutant grew in media containing any one of a variety of substances, including hexoses, hexose 6-phosphates, sugar acids and glucogenic substrates, at rates not significantly different from those at which the parent organism grew on these substrates. However, only the parent grew on fructose or fructose 1-phosphate. 3. Fructose and fructose 1-phosphate inhibit the growth of the mutant, but not of its parent, on other carbon sources. 4. Even though not previously exposed to fructose, the mutant took up [(14)C]fructose rapidly but to only a small extent: [(14)C]fructose 1-phosphate was identified as the predominant labelled product. In contrast, the equally rapid but more extensive uptake of [(14)C]fructose by the parent organism required prior growth in the presence of fructose.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4579702 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1177592 PMC1177592]<br />
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||<br />
Autoradiography; Biological Transport; Carbon Isotopes; Cell Count; Cell-Free System; Chromatography, Thin Layer; Escherichia coli/drug effects; Escherichia coli/enzymology; Fructose/metabolism; Fructose/pharmacology; Fructosephosphates/pharmacology; Glycerol/metabolism; Mutation; Phosphotransferases/metabolism; Time Factors; Ultrasonics<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4579702&diff=1491174PMID:45797022014-06-15T13:57:23Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:1937709&diff=1491159PMID:19377092014-06-14T13:59:01Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Thora, S, Singh, SD and Chhaparwal, BC''' (1991) Tuberculosis meningitis--how early can it occur? ''Indian Pediatr'' '''28''':296-8<br />
|-<br />
!align=left |Abstract<br />
||<br />
No abstract in PubMed<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1937709 PubMed]<br />
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||<br />
Age Factors; Humans; Infant; Male; Tuberculosis, Meningeal/etiology; Tuberculosis, Miliary/complications<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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{{LitLinks}}<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:1937709&diff=1491158PMID:19377092014-06-14T13:59:00Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4862193&diff=1491140PMID:48621932014-06-13T18:00:58Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Markovitz, A, Sydiskis, RJ and Lieberman, MM''' (1967) Genetic and biochemical studies on mannose-negative mutants that are deficient in phosphomannose isomerase in Escherichia coli K-12. ''J. Bacteriol.'' '''94''':1492-6<br />
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!align=left |Abstract<br />
||<br />
Two mannose-negative mutants of Escherichia coli K-12 have been isolated. These mutants are deficient in the ability to synthesize phosphomannose isomerase and capsular polysaccharide when grown on glucose-containing media. Interrupted mating experiments to determine the kinetics of genetic transfer show that the two mannose-negative mutations map together between the histidine and tryptophan regions of the E. coli chromosome.<br />
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||<br />
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4862193 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC276853 PMC276853]<br />
<br />
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||<br />
Chromosome Mapping; Chromosomes, Bacterial; Conjugation, Genetic; Escherichia coli/enzymology; Escherichia coli/growth & development; Genetics, Microbial; Glucose/metabolism; Glucose-6-Phosphate Isomerase/metabolism; Glucosephosphate Dehydrogenase/metabolism; Histidine; Isomerases/biosynthesis; Isomerases/metabolism; Mannose/metabolism; Mutation; Polysaccharides, Bacterial/biosynthesis; Recombination, Genetic; Streptomycin/pharmacology; Tryptophan<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<annotationlinks/><br />
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br />
{{LitLinks}}<br />
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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:4862193&diff=1491139PMID:48621932014-06-13T18:00:58Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:3511029&diff=1491135PMID:35110292014-06-13T03:44:00Z<p>176.9.118.209: Fill PMID: Page!</p>
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||<br />
'''Salowe, SP and Stubbe, J''' (1986) Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase. ''J. Bacteriol.'' '''165''':363-6<br />
|-<br />
!align=left |Abstract<br />
||<br />
The nrdB gene, which encodes the B2 subunit of Escherichia coli ribonucleotide reductase (EC 1.17.4.1), was cloned into multicopy plasmid pSPS2. This vector, which contains the pL promoter of bacteriophage lambda and the tetracycline resistance gene of pBR322, was transformed into a lysogenic host with a thermolabile repressor. In the newly constructed strain, subunit B2 constituted approximately 25% of the soluble protein after heat induction, an overproduction of several hundredfold relative to the wild-type strain. Purification to homogeneity of the overproduced protein was accomplished by using DEAE and quaternary aminoethyl ion-exchange resins.<br />
|-<br />
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||<br />
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3511029 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC214425 PMC214425]<br />
<br />
|-<br />
!align=left |Keywords<br />
||<br />
Amino Acid Sequence; Cloning, Molecular; Escherichia coli/enzymology; Gene Expression Regulation; Macromolecular Substances; Ribonucleoside Diphosphate Reductase/biosynthesis; Ribonucleoside Diphosphate Reductase/genetics; Ribonucleoside Diphosphate Reductase/isolation & purification; Ribonucleotide Reductases/genetics<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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{{LitLinks}}<br />
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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:3511029&diff=1491134PMID:35110292014-06-13T03:43:59Z<p>176.9.118.209: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>176.9.118.209https://ecoliwiki.org/colipedia/index.php?title=PMID:18515344&diff=1491129PMID:185153442014-06-13T01:56:56Z<p>176.9.118.209: Fill PMID: Page!</p>
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'''Shimada, T, Ishihama, A, Busby, SJ and Grainger, DC''' (2008) The Escherichia coli RutR transcription factor binds at targets within genes as well as intergenic regions. ''Nucleic Acids Res.'' '''36''':3950-5<br />
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The Escherichia coli RutR protein is the master regulator of genes involved in pyrimidine catabolism. Here we have used chromatin immunoprecipitation in combination with DNA microarrays to measure the binding of RutR across the chromosome of exponentially growing E. coli cells. Twenty RutR-binding targets were identified and analysis of these targets generated a DNA consensus logo for RutR binding. Complementary in vitro binding assays showed high-affinity RutR binding to 16 of the 20 targets, with the four low-affinity RutR targets lacking predicted key binding determinants. Surprisingly, most of the DNA targets for RutR are located within coding segments of the genome and appear to have little or no effect on transcript levels in the conditions tested. This contrasts sharply with other E. coli transcription factors whose binding sites are primarily located in intergenic regions. We suggest that either RutR has yet undiscovered function or that evolution has been slow to eliminate non-functional DNA sites for RutR because they do not have an adverse effect on cell fitness.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18515344 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2475637 PMC2475637]<br />
Online version:[http://dx.doi.org/10.1093/nar/gkn339 10.1093/nar/gkn339]<br />
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Base Sequence; Binding Sites; Chromatin Immunoprecipitation; Consensus Sequence; DNA, Bacterial/metabolism; DNA, Intergenic/metabolism; DNA-Binding Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins/metabolism; Genes, Bacterial; Genome, Bacterial; Oligonucleotide Array Sequence Analysis; Sequence Analysis, DNA; Transcription Factors/metabolism<br />
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'''Kaidow, A, Kataoka, T, Wachi, M, Takada, A, Yamasaki, M and Nagai, K''' (1992) The 55-kilodalton protein in an oriC complex fraction is glycogen synthase. ''J. Bacteriol.'' '''174''':5454-6<br />
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!align=left |Abstract<br />
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Three proteins with molecular masses of 35, 55, and 75 kDa were found in an oriC complex fraction after purification through CsCl density gradient centrifugation (W. G. Hendrickson, T. Kusano, H. Yamaki, R. Balakrishnan, M. King, J. Murchie, and M. Schaechter, Cell 30:915-923, 1982). Of these three proteins, the 55-kDa protein was determined to be glycogen synthase on the basis of the N-terminal amino acid sequence and the molecular weight. The oriC complex was formed in glgA mutant cells, which produce no detectable glycogen, as well as in wild-type cells. None of the 35-, 55-, and 75-kDa proteins were detected in the fraction from this mutant. The results indicate that these proteins were not constituents of the oriC complex.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1644773 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC206386 PMC206386]<br />
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Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Centrifugation; Chromosomes, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Glycogen/analysis; Glycogen Synthase/isolation & purification; Glycogen Synthase/metabolism<br />
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