https://ecoliwiki.org/colipedia/api.php?action=feedcontributions&feedformat=atom&user=54.224.27.110EcoliWiki - User contributions [en]2026-11-04T23:46:38ZUser contributionsMediaWiki 1.43.11https://ecoliwiki.org/colipedia/index.php?title=PMID:1794243&diff=1491770PMID:17942432014-09-28T05:15:45Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Deng, GH and Wang, AX''' (1991) [Bacterial sepsis and nosocomial infection: a study of 70 patients]. ''Zhonghua Nei Ke Za Zhi'' '''30''':484-6, 521<br />
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!align=left |Abstract<br />
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74 episodes of bacterial sepsis in 70 patients were analysed from July 1988 to June 1989. The incidence of sepsis is 0.7% of the whole admitted patients. Compared to a similar previous study from April 1982 to March 1983, the incidence of sepsis decreased (P less than 0.01), and the incidence of nosocomial sepsis remained unchanged, whereas its mortality decreased (P less than 0.05). The host defenses are important in predisposing to sepsis and determining prognosis. Antibiotic sensitivity test revealed that some bacterial strains were resistant to new beta-lactam antibiotics.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1794243 PubMed]<br />
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Adolescent; Adult; Aged; Anti-Bacterial Agents/pharmacology; Child; Child, Preschool; Cross Infection/epidemiology; Cross Infection/microbiology; Cross Infection/mortality; Drug Resistance, Microbial; Female; Gram-Negative Bacterial Infections; Humans; Incidence; Infant; Infant, Newborn; Lactams; Male; Middle Aged; Sepsis/epidemiology; Sepsis/microbiology; Sepsis/mortality<br />
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{{LitSignificance}}<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:1794243&diff=1491769PMID:17942432014-09-28T05:15:44Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:1116701&diff=1491759PMID:11167012014-09-23T02:29:23Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Harrison, R''' (1975) Glaucoma in the elderly. ''Geriatrics'' '''30''':55-62, 65<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=1116701 PubMed]<br />
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Age Factors; Aged; Fundus Oculi; Glaucoma/diagnosis; Glaucoma/drug therapy; Glaucoma/surgery; Humans; Ophthalmoscopy; Tonometry, Ocular; Visual Field Tests; Water<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:1116701&diff=1491758PMID:11167012014-09-23T02:29:23Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:21708137&diff=1491743PMID:217081372014-09-03T09:50:55Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Blencowe, DK, Al Jubori, S and Morby, AP''' (2011) Identification of a novel function for the FtsL cell division protein from Escherichia coli K12. ''Biochem. Biophys. Res. Commun.'' '''411''':44-9<br />
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Analysis of the essential cell division protein FtsL demonstrates the partial conservation of a cysteine-pair within the trans-membrane region which itself is flanked by histidine-pairs in the cytosol and periplasm. Similar arrangements of such amino acids are seen in proteins known to transport/bind metal ions in biological systems. Heterologous expression of ftsL in Escherichia coli K12 confers a Zn(II)-sensitive phenotype and alteration of the candidate metal-ion binding residues cysteine or histidine substantially alters this phenotype. Whilst the cysteine/histidine replacement derivatives of ftsL were able to complement an otherwise ftsL-null strain, the derivative carrying ftsL lacking the cysteine pair was sensitive to raised metal-ion concentrations in the media. We show that ftsL can confer a metal-ion sensitive phenotype and that trans-membrane cysteine residues play a role in FtsL function in elevated metal-ion concentrations.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21708137 PubMed]<br />
Online version:[http://dx.doi.org/10.1016/j.bbrc.2011.06.083 10.1016/j.bbrc.2011.06.083]<br />
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Amino Acid Sequence; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Consensus Sequence; Cysteine/chemistry; Cysteine/genetics; Drug Resistance, Bacterial; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Histidine/chemistry; Histidine/genetics; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Zinc/metabolism; Zinc/pharmacology<br />
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{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:21708137&diff=1491742PMID:217081372014-09-03T09:50:54Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:10613870&diff=1491730PMID:106138702014-08-27T04:26:37Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Ghigo, JM and Beckwith, J''' (2000) Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization. ''J. Bacteriol.'' '''182''':116-29<br />
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In Escherichia coli, nine essential cell division proteins are known to localize to the division septum. FtsL is a 13-kDa bitopic membrane protein with a short cytoplasmic N-terminal domain, a membrane-spanning segment, and a periplasmic domain that has a repeated heptad motif characteristic of leucine zippers. Here, we identify the requirements for FtsL septal localization and function. We used green fluorescent protein fusions to FtsL proteins where domains of FtsL had been exchanged with analogous domains from either its Haemophilus influenzae homologue or the unrelated MalF protein to show that both the membrane-spanning segment and the periplasmic domain of FtsL are required for localization to the division site. Mutagenesis of the periplasmic heptad repeat motif severely impaired both localization and function as well as the ability of FtsL to drive the formation of sodium dodecyl sulfate-resistant multimers in vitro. These results are consistent with the predicted propensity of the FtsL periplasmic domain to adopt a coiled-coiled structure. This coiled-coil motif is conserved in all gram-negative and gram-positive FtsL homologues identified so far. Our data suggest that most of the FtsL molecule is a helical coiled coil involved in FtsL multimerization.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10613870 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC94247 PMC94247]<br />
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ATP-Binding Cassette Transporters; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/drug effects; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cell Cycle Proteins; Cell Division/drug effects; Cell Division/physiology; Cell Membrane/metabolism; Cytoplasm/metabolism; Escherichia coli/cytology; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli Proteins; Haemophilus influenzae/genetics; Maltose-Binding Proteins; Membrane Proteins/drug effects; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Monosaccharide Transport Proteins; Periplasm/metabolism; Periplasmic Binding Proteins; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate/pharmacology<br />
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==Significance {{HelpIcon|Help:Literature}} ==<br />
{{LitSignificance}}<br />
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{{LitMaterials}}<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:10613870&diff=1491729PMID:106138702014-08-27T04:26:36Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2829831&diff=1491728PMID:28298312014-08-27T00:42:46Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Bradley, SA, Tinsley, CR, Muiry, JA and Henderson, PJ''' (1987) Proton-linked L-fucose transport in Escherichia coli. ''Biochem. J.'' '''248''':495-500<br />
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!align=left |Abstract<br />
||<br />
1. Addition of L-fucose to energy-depleted anaerobic suspensions of Escherichia coli elicited an uncoupler-sensitive alkaline pH change diagnostic of L-fucose/H+ symport activity. 2. L-Galactose or D-arabinose were also substrates, but not inducers, for the L-fucose/H+ symporter. 3. L-Fucose transport into subcellular vesicles was dependent upon respiration, displayed a pH optimum of about 5.5, and was inhibited by protonophores and ionophores. 4. These results showed that L-fucose transport into E. coli was energized by the transmembrane electrochemical gradient of protons. 5. Neither steady state kinetic measurements nor assays of L-fucose binding to periplasmic proteins revealed the existence of a second L-fucose transport system.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2829831 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1148569 PMC1148569]<br />
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Antimetabolites/pharmacology; Biological Transport/drug effects; Carbohydrate Metabolism; Escherichia coli/drug effects; Escherichia coli/metabolism; Fucose/metabolism; Hydrogen-Ion Concentration; Kinetics; Protons; Subcellular Fractions/metabolism; Substrate Specificity<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/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2829831&diff=1491727PMID:28298312014-08-27T00:42:45Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2963943&diff=1491724PMID:29639432014-08-24T09:41:28Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Hollifield, WC, Kaplan, EN and Huang, HV''' (1987) Efficient RecABC-dependent, homologous recombination between coliphage lambda and plasmids requires a phage ninR region gene. ''Mol. Gen. Genet.'' '''210''':248-55<br />
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A phage lambda gene that gives a 100-fold increase in recombinant frequencies for RecABC pathway-mediated, phage-plasmid homologous recombination (Shen and Huang 1986) maps to ninG (orf 204) of lambda. We call this gene rap, for recombination adept with plasmid. A similar determinant exists in Charon 4A and maps in phi 80-derived sequences, between nin5 and the Rz homology with lambda. The absence of the Rap+ phenotype from certain lambda vectors explains the inefficiency of screening the resulting phage libraries using phage-plasmid homologous recombination. The mapping of rap permits the construction of lambda vectors more suitable for this screening technique.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2963943 PubMed]<br />
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Bacteriophage lambda/genetics; Chromosome Mapping; Escherichia coli/genetics; Exodeoxyribonuclease V; Exodeoxyribonucleases/genetics; Genes, Viral; Plasmids; Rec A Recombinases/genetics; Recombination, Genetic<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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==References==<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2963943&diff=1491723PMID:29639432014-08-24T09:41:27Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0044659_!_cytolysis_by_virus_of_host_cell&diff=1491722Category:GO:0044659 ! cytolysis by virus of host cell2014-08-24T06:57:15Z<p>54.224.27.110: New GO term category page</p>
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==References==<br />
{{RefHelp}}<br />
<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:3791860&diff=1491715PMID:37918602014-08-16T09:31:14Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Gaines, PA and Reidy, JF''' (1986) Percutaneous high brachial aortography: a safe alternative to the translumbar approach. ''Clin Radiol'' '''37''':595-7<br />
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Percutaneous high brachial aortography with a small diameter catheter (5 gauge) was used as an alternative to the translumbar approach in 45 patients in whom access via the femoral route was not considered possible. Only one serious complication occurred: the late development of a bleeding false aneurysm in a patient with renal failure and severe hypertension who was being treated with anticoagulants. The relevant limitations and complications of the translumbar and axillary approaches are discussed. We consider this technique to be a safe and simple alternative to translumbar aortography when femoral access is not possible.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3791860 PubMed]<br />
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Aortography/adverse effects; Aortography/methods; Arterial Occlusive Diseases/radiography; Brachial Artery; Catheterization; Female; Humans; Male; Middle Aged<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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==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>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:3791860&diff=1491714PMID:37918602014-08-16T09:31:13Z<p>54.224.27.110: New PMID: Page!</p>
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'''Piskarev, VE, Navrátil, J, Karásková, H, Bezouska, K and Kocourek, J''' (1990) Interaction of egg-white glycoproteins and their oligosaccharides with the monomer and the hexamer of chicken liver lectin. A multivalent oligosaccharide-combining site exists within the carbohydrate-recognition domain. ''Biochem. J.'' '''270''':755-60<br />
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!align=left |Abstract<br />
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Binding of egg-white glycoproteins and their oligosaccharides to hexameric solubilized form of the chicken hepatic lectin and the monomeric soluble fragment containing the carbohydrate-recognition domain has been investigated by several techniques. Ligand blotting revealed significant differences in binding to two forms of the lectin only for glycoproteins bearing multiple N-linked oligosaccharide moieties in their molecule (riboflavin-binding glycoprotein, avidin or ovomucoid). Inhibition studies indicated that inhibitory potency in a series of linear and branched N-acetyl-D-glucosamine-terminated oligosaccharides is critically dependent on the number and spatial arrangement of the terminal monosaccharide residues for both forms of the lectin. Direct binding of 4-hydroxyphenyl-derivatized radioiodinated oligosaccharides measured by equilibrium dialysis and frontal affinity chromatography points to the existence of two N-acetyl-D-glucosamine-combining sites per one subunit of the lectin, as has been recently reported for the rabbit and rat liver lectin [Lee & Lee (1988) Biochem. Biophys. Res. Commun. 155, 1444-1452]. Highly branch (penta-antennary) oligosaccharides interact with more than one subunit of the hexameric form of the lectin and thus resemble the more complex interaction of the whole glycoprotein.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2241907 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1131796 PMC1131796]<br />
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Animals; Binding Sites; Binding, Competitive; Carbohydrate Sequence; Chickens; Egg Proteins/metabolism; Glycoproteins/metabolism; Lectins/metabolism; Liver/metabolism; Molecular Sequence Data; Oligosaccharides/metabolism; Protein Binding<br />
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{{LitSignificance}}<br />
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br />
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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2241907&diff=1491690PMID:22419072014-08-11T12:08:46Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:10543963&diff=1491687PMID:105439632014-08-10T16:25:07Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Kampranis, SC, Howells, AJ and Maxwell, A''' (1999) The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes. ''J. Mol. Biol.'' '''293''':733-44<br />
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CcdB is a bacterial toxin that targets DNA gyrase. Analysis of the interaction of CcdB with gyrase reveals two distinct complexes. An initial complex (alpha) is formed by direct interaction between GyrA and CcdB; this complex can be detected by affinity column and gel-shift analysis, and has a proteolytic signature which is characterised by a 49 kDa fragment of GyrA. Surface plasmon resonance shows that CcdB binds to the N-terminal domain of GyrA with high affinity. In this mode of binding, CcdB does not affect the ability of gyrase to hydrolyse ATP or promote supercoiling. Incubation of this initial complex with ATP in the presence of GyrB and DNA slowly converts it to a second complex (beta), which has a lower rate of ATP hydrolysis and is unable to catalyse supercoiling. The efficiency of formation of this inactive complex is dependent on the concentrations of ATP and CcdB. We suggest that the conversion between the two complexes proceeds via an intermediate, whose formation is dependent on the rate of ATP hydrolysis.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10543963 PubMed]<br />
Online version:[http://dx.doi.org/10.1006/jmbi.1999.3182 10.1006/jmbi.1999.3182]<br />
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Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/metabolism; Bacterial Toxins/metabolism; Binding Sites; Chromatography, Affinity; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/metabolism; DNA, Superhelical/genetics; DNA, Superhelical/metabolism; Dimerization; Escherichia coli/enzymology; Hydrolysis; Kinetics; Models, Molecular; Molecular Weight; Mutation; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Binding; Protein Conformation; Structure-Activity Relationship; Surface Plasmon Resonance; Topoisomerase II Inhibitors; Trypsin/metabolism<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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<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>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:10543963&diff=1491686PMID:105439632014-08-10T16:25:07Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2132120&diff=1491679PMID:21321202014-08-09T18:39:31Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Spens, E and Gabriel, R''' (1990) [Radiation risk in dentistry]. ''Dtsch Stomatol'' '''40''':518-22<br />
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Reference is made to recommendation by the International Commission for Radiation Protection No. 26 on determination of the risk potentially caused by low-dosage ionising radiation. Calculations were made on that basis of the stochastic radiation risk for the general public.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2132120 PubMed]<br />
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Humans; Radiation Dosage; Radiation Monitoring; Radiography, Dental/adverse effects; Risk Factors; Stochastic Processes<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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<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>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2132120&diff=1491678PMID:21321202014-08-09T18:39:31Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:12397182&diff=1491662PMID:123971822014-08-06T23:23:14Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Kobiler, O, Koby, S, Teff, D, Court, D and Oppenheim, AB''' (2002) The phage lambda CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis. ''Proc. Natl. Acad. Sci. U.S.A.'' '''99''':14964-9<br />
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ATP-dependent proteases, like FtsH (HflB), recognize specific protein substrates. One of these is the lambda CII protein, which plays a key role in the phage lysis-lysogeny decision. Here we provide evidence that the conserved C-terminal end of CII acts as a necessary and sufficient cis-acting target for rapid proteolysis. Deletions of this conserved tag, or a mutation that confers two aspartic residues at its C terminus do not affect the structure or activity of CII. However, the mutations abrogate CII degradation by FtsH. We have established an in vitro assay for the lambda CIII protein and demonstrated that CIII directly inhibits proteolysis by FtsH to protect CII and CII mutants from degradation. Phage lambda carrying mutations in the C terminus of CII show increased frequency of lysogenization, which indicates that this segment of CII may itself be sensitive to regulation that affects the lysis-lysogeny development. In addition, the region coding for the C-terminal end of CII overlaps with a gene that encodes a small antisense RNA called OOP. We show that deletion of the end of the cII gene can prevent OOP RNA, supplied in trans, interfering with CII activity. These findings provide an example of a gene that carries a region that modulates stability at the level of mRNA and protein.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12397182 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC137528 PMC137528]<br />
Online version:[http://dx.doi.org/10.1073/pnas.222172499 10.1073/pnas.222172499]<br />
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Amino Acid Sequence; Bacteriophage lambda/genetics; Base Sequence; Cloning, Molecular; DNA, Viral/chemistry; DNA, Viral/genetics; Escherichia coli/virology; Lysogeny; Molecular Sequence Data; Plasmids; Polymerase Chain Reaction; RNA, Viral/chemistry; RNA, Viral/genetics; Recombinant Fusion Proteins/metabolism; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription, Genetic; Viral Proteins; Virus Replication<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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==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>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:12397182&diff=1491661PMID:123971822014-08-06T23:23:13Z<p>54.224.27.110: New PMID: Page!</p>
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'''Chu, HM, Yun, M, Anderson, DE, Sage, H, Park, HW and Endow, SA''' (2005) Kar3 interaction with Cik1 alters motor structure and function. ''EMBO J.'' '''24''':3214-23<br />
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Kar3, a kinesin-14 motor of Saccharomyces cerevisiae required for mitosis and karyogamy, reportedly interacts with Cik1, a nonmotor protein, via its central, predicted coiled coil. Despite this, neither Kar3 nor Cik1 homodimers have been observed in vivo. Here we show that Kar3 is a dimer in vitro by analytical ultracentrifugation. The motor domains appear as paired particles by rotary-shadow electron microscopy (EM) and circular dichroism (CD) spectroscopy of the nonmotor region shows characteristics of helical structure, typical of coiled coils. Remarkably, the Kar3/Cik1 nonmotor region shows greater helicity by CD analysis and rotary-shadow EM reveals a stalk joined to one large or two smaller particles. The highly helical Kar3/Cik1 nonmotor region and visible stalk indicate that dimerization with Cik1 causes structural changes in Kar3. The Cik1 and Kar3 stalk regions preferentially associate with one another rather than forming homodimers. Kar3/Cik1 moves on microtubules at 2-2.4 microm min(-1), 2-5-fold faster than Kar3, and destabilizes microtubules at the lagging ends. Thus, structural changes in Kar3 upon dimerization with Cik1 alter the motor velocity and likely regulate Kar3 activity in vivo.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16107877 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1224680 PMC1224680]<br />
Online version:[http://dx.doi.org/10.1038/sj.emboj.7600790 10.1038/sj.emboj.7600790]<br />
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Circular Dichroism; Dimerization; Gene Expression; Microscopy, Electron; Microtubule Proteins/chemistry; Microtubule Proteins/genetics; Microtubule Proteins/isolation & purification; Microtubule Proteins/metabolism; Microtubule-Associated Proteins/chemistry; Microtubule-Associated Proteins/genetics; Microtubule-Associated Proteins/isolation & purification; Microtubule-Associated Proteins/metabolism; Microtubules/genetics; Microtubules/metabolism; Protein Binding; Protein Structure, Secondary; Saccharomyces cerevisiae/chemistry; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae/ultrastructure; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/isolation & purification; Saccharomyces cerevisiae Proteins/metabolism; Structure-Activity Relationship<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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==See also==<br />
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==References==<br />
{{RefHelp}}<br />
<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:16107877&diff=1491628PMID:161078772014-08-04T00:51:48Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:3312962&diff=1491626PMID:33129622014-08-03T19:43:55Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Fognini-Lefebvre, N, Lazzaroni, JC and Portalier, R''' (1987) tolA, tolB and excC, three cistrons involved in the control of pleiotropic release of periplasmic proteins by Escherichia coli K12. ''Mol. Gen. Genet.'' '''209''':391-5<br />
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!align=left |Abstract<br />
||<br />
Mutants of Escherichia coli K12 carrying exc mutations inducing the release of the plasmid pBR322-encoded beta-lactamase (EC 3.5.2.6) into the extracellular medium were analysed and compared with previously described excretory mutants carrying lky mutations associated with the release of alkaline phosphatase and to tolA and tolB mutants, originally described as tolerant towards various colicins. The exc, lky and tol mutations mapped near the gal operon at min 16.5 of the E. coli linkage map. A genetic analysis presented in this paper showed that some exc and lky mutations belonged to the tolA and tolB complementation groups. Furthermore, we identified a third cistron, excC, involved in the excretion of periplasmic enzymes but distinct from the two others.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3312962 PubMed]<br />
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Alleles; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Genes; Genes, Bacterial; Mutation; Phenotype; Plasmids; Transduction, Genetic; beta-Lactamases/genetics<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>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:3312962&diff=1491625PMID:33129622014-08-03T19:43:54Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:8107146&diff=1491544PMID:81071462014-07-24T09:37:41Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Celia, H, Hoermann, L, Schultz, P, Lebeau, L, Mallouh, V, Wigley, DB, Wang, JC, Mioskowski, C and Oudet, P''' (1994) Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films. ''J. Mol. Biol.'' '''236''':618-28<br />
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!align=left |Abstract<br />
||<br />
Two-dimensional crystals of the Escherichia coli DNA gyrase B subunit were obtained upon specific interactions with novobiocin linked phospholipid films. A three-dimensional surface model of the protein was generated by analysing images of tilted negatively stained crystals. The structure showed, at 2.5 to 3.0 nm resolution, two elongated arms organised as a V-shaped protein: the bottom of the V contains the novobiocin binding site, and the extremities of the arms mediate protein-protein interactions between the two monomers in the unit cell. Image analysis of frozen hydrated two-dimensional crystals resulted in a 1.0 nm resolution projection map that shows structural elements not revealed with negative staining. Electron microscopic structural data were compared with the crystallographic structure of the 43 kDa N-terminal fragment of the B subunit complexed with a non hydrolysable ATP analogue.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8107146 PubMed]<br />
Online version:[http://dx.doi.org/10.1006/jmbi.1994.1171 10.1006/jmbi.1994.1171]<br />
|-<br />
!align=left |Keywords<br />
||<br />
Binding Sites; Crystallography, X-Ray; DNA Gyrase; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/ultrastructure; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Image Processing, Computer-Assisted; Microscopy, Electron; Models, Molecular; Novobiocin/chemistry; Phospholipids/chemistry; Water/chemistry<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:8107146&diff=1491543PMID:81071462014-07-24T09:37:40Z<p>54.224.27.110: New PMID: Page!</p>
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'''Krueger, S, Zaccai, G, Wlodawer, A, Langowski, J, O'Dea, M, Maxwell, A and Gellert, M''' (1990) Neutron and light-scattering studies of DNA gyrase and its complex with DNA. ''J. Mol. Biol.'' '''211''':211-20<br />
|-<br />
!align=left |Abstract<br />
||<br />
The solution structure of Escherichia coli DNA gyrase, an enzyme that catalyzes the ATP-dependent supercoiling of DNA, has been characterized by small-angle neutron scattering (SANS) and dynamic light-scattering (DLS). The enzyme and its complex with a 172 base-pair fragment of duplex DNA, in H2O or 2H2O solvent, were studied by contrast variation and the measurement of hydrodynamic parameters as a function of scattering angle. The complex was also measured in the presence of 5'-adenylyl-beta,gamma-imidodiphosphate (ADPNP), a non-hydrolyzable ATP analog that is known to support limited supercoiling. The values of the radius of gyration, Rg = 67 A, from SANS and the hydrodynamic radius, Rh = 64 A, from DLS predict a larger than expected volume for the enzyme, supporting the notion of channels or cavities within the molecule. In addition, several classes of models were rejected based on SANS data obtained in 2H2O at larger scattering angles. The best fit to both the SANS and DLS data is obtained for oblate, inhomogeneous particles approximately 175 A wide and 52 A thick. Such particles provide a large surface area for DNA interaction. Both Rg and Rh values change very little upon addition of DNA, suggesting that DNA binds in a manner that does not significantly change the shape of the protein. No appreciable change in structure is found with the addition of ADPNP. However, the higher-angle SANS data indicate a slight rearrangement of the enzyme in the presence of nucleotide.<br />
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||<br />
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2153834 PubMed]<br />
Online version:[http://dx.doi.org/10.1016/0022-2836(90)90021-D 10.1016/0022-2836(90)90021-D]<br />
|-<br />
!align=left |Keywords<br />
||<br />
Animals; DNA Topoisomerases, Type II/metabolism; DNA, Ribosomal/metabolism; Escherichia coli/enzymology; Light; Mathematics; Models, Structural; Models, Theoretical; Neutrons; Nucleic Acid Conformation; Protein Binding; Protein Conformation; RNA, Ribosomal, 5S/genetics; Scattering, Radiation; Sea Urchins<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2153834&diff=1491517PMID:21538342014-07-21T17:19:17Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:1970641&diff=1491413PMID:19706412014-07-04T18:58:13Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Quiocho, FA''' (1990) Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. ''Philos. Trans. R. Soc. Lond., B, Biol. Sci.'' '''326''':341-51; discussion 351-2<br />
|-<br />
!align=left |Abstract<br />
||<br />
We have determined and refined the X-ray crystal structures of six periplasmic binding proteins that serve as initial receptors for the osmotic-shock sensitive, active transport of L-arabinose, D-galactose/D-glucose, maltose, sulphate, leucine/isoleucine/valine and leucine. The tertiary structures and atomic interactions between proteins and ligands show common features that are important for understanding the function of the binding proteins. All six structures are ellipsoidal, consisting of two similar, globular domains. The ligand-binding site is located deep in the cleft between the two domains. Irrespective of the nature of the ligand (e.g. saccharide, sulphate dianion or leucine zwitterion), the specificities and affinities of the binding sites are achieved mainly through hydrogen-bonding interactions. Binding of ligands induces a large protein conformational change. Three different structures have been observed among the binding proteins: unliganded 'open cleft', liganded 'open cleft', and liganded 'closed cleft'. Here we discuss the functions of binding proteins in the light of numerous crystallographic and ligand-binding studies and propose a mechanism for the binding protein-dependent, high-affinity active transport.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1970641 PubMed]<br />
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|-<br />
!align=left |Keywords<br />
||<br />
Bacteria/metabolism; Biological Transport, Active; Carrier Proteins/metabolism; Cell Membrane/metabolism; Cell Membrane/ultrastructure; Membrane Proteins/metabolism; Models, Molecular; Protein Conformation<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:1970641&diff=1491412PMID:19706412014-07-04T18:58:12Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0006273_!_lagging_strand_elongation&diff=1491395Category:GO:0006273 ! lagging strand elongation2014-07-02T18:00:18Z<p>54.224.27.110: New GO term category page</p>
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2245670&diff=1491352PMID:22456702014-06-29T13:23:41Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Zion, MM, Balkin, J, Rosenmann, D, Goldbourt, U, Reicher-Reiss, H, Kaplinsky, E and Behar, S''' (1990) Use of pulmonary artery catheters in patients with acute myocardial infarction. Analysis of experience in 5,841 patients in the SPRINT Registry. SPRINT Study Group. ''Chest'' '''98''':1331-5<br />
|-<br />
!align=left |Abstract<br />
||<br />
This study analyzes the use of PAC in a registry comprising 5,841 hospitalized patients with AMI. A total of 371 patients received PAC. In-hospital mortality was higher in patients with CHF who received PAC, while there was no difference in patients with cardiogenic shock or persistent hypotension. Mortality in patients receiving PAC was higher irrespective of the presence or absence of "pump failure." A separate analysis of discharge summaries of 364 patients with CHF showed that PAC was used more frequently in sicker patients and that when severity of CHF was assessed, no difference in mortality was found in patients with mild or moderate CHF. We conclude that while a higher in-hospital mortality is found in patients receiving PAC, this excess is likely related to difference in severity of CHF, which had not been assessed in every individual. It is unlikely that PAC increases mortality.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2245670 PubMed]<br />
<br />
|-<br />
!align=left |Keywords<br />
||<br />
Adult; Aged; Catheterization, Swan-Ganz/adverse effects; Female; Heart Failure/etiology; Humans; Hypotension/etiology; Male; Middle Aged; Myocardial Infarction/complications; Myocardial Infarction/diagnosis; Myocardial Infarction/mortality; Myocardial Infarction/therapy; Retrospective Studies; Shock, Cardiogenic/etiology<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2245670&diff=1491351PMID:22456702014-06-29T13:23:40Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:4345920&diff=1491314PMID:43459202014-06-26T07:56:47Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Siegel, EC''' (1973) Ultraviolet-sensitive mutator strain of Escherichia coli K-12. ''J. Bacteriol.'' '''113''':145-60<br />
|-<br />
!align=left |Abstract<br />
||<br />
An ultraviolet (UV)-sensitive mutator gene, mutU, was identified in Escherichia coli K-12. The mutation mutU4 is very close to uvrD, between metE and ilv, on the E. coli chromosome. It was recessive as a mutator and as a UV-sensitive mutation. The frequency of reversion of trpA46 on an F episome was increased by mutU4 on the chromosome. The mutator gene did not increase mutation frequencies in virulent phages or in lytically grown phage lambda. The mutU4 mutation predominantly induced transitional base changes. Mutator strains were normal for recombination and host-cell reactivation of UV-irradiated phage T1. They were normally resistant to methyl methanesulfonate and were slightly more sensitive to gamma irradiation than Mut(+) strains. UV irradiation induced mutations in a mutU4 strain, and phage lambda was UV-inducible. Double mutants containing mutU4 and recA, B, or C were extremely sensitive to UV irradiation; a mutU4 uvrA6 double mutant was only slightly more sensitive than a uvrA6 strain. The mutU4 uvrA6 and mutU4 recA, B, or C double mutants had mutation rates similar to that of a mutU4 strain. Two UV-sensitive mutators, mut-9 and mut-10, isolated by Liberfarb and Bryson in E. coli B/UV, were found to be co-transducible with ilv in the same general region as mutU4.<br />
|-<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4345920 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC251612 PMC251612]<br />
<br />
|-<br />
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||<br />
Alkanesulfonates; Anti-Bacterial Agents/pharmacology; Cell Survival; Chromosome Mapping; Coliphages/growth & development; Culture Media; DNA Repair; Drug Resistance, Microbial; Escherichia coli/drug effects; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli/radiation effects; Genes, Recessive; Lysogeny; Mutagens; Mutation; Phenotype; Radiation Effects; Recombination, Genetic; Thymine/metabolism; Transduction, Genetic; Ultraviolet Rays<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:4345920&diff=1491313PMID:43459202014-06-26T07:56:46Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:4946852&diff=1491312PMID:49468522014-06-26T07:18:24Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Smirnov, GB and Skavronskaya, AG''' (1971) Location of uvr502 mutation on the chromosome of Escherichia coli K-12. ''Mol. Gen. Genet.'' '''113''':217-21<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=4946852 PubMed]<br />
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|-<br />
!align=left |Keywords<br />
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Chromosome Mapping; Escherichia coli; Genetics, Microbial; Mutation/radiation effects; Radiation Genetics; Transduction, Genetic; Ultraviolet Rays<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:4946852&diff=1491311PMID:49468522014-06-26T07:18:24Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:385062&diff=1491309PMID:3850622014-06-25T01:22:59Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Reinbolt, J, Tritsch, D and Wittmann-Liebold, B''' (1979) The primary structure of ribosomal protein S7 from E. coli strains K and B. ''Biochimie'' '''61''':501-22<br />
|-<br />
!align=left |Abstract<br />
||<br />
Ribosomal proteins S7 from 30S subunits of Escherichia coli strains K and B differ extensively in their aminoacid compositions. The experimental details which led to the determination of the complete primary structures of proteins S7K and S7B are presented. Protein S7K consists of a single polypeptide chain of 177 aminoacids giving a calculated molecular weight of 19, 732, whereas protein S7B has 153 residues which amount to a molecular weight of 17,131. Aminoacid sequences were determined by a combination of automated Edman degradation of the intact proteins in a modified Beckman sequenator and sequencing of peptides obtained by digestion with trypsin. Staphylococcus aureus protease, thermolysin and pepsin, either by solid-phase Edman degradation or by dansyl-Edman degradation. Additional information about the primary structure was derived from peptides resulting from chemical cleavages of the protein by 2-(2-nitrophenyl-sulphenyl)-3-methyl 3' bromoindolenine at its tryptophanyl bonds and by cyanogen bromide at its methionyl bonds leading to large fragments. The mutational event occurring between S7B and S7K was characterized. Protein S7K contains an additional sequence of 24 aminoacids at its C-terminal end. The aminoacid sequence of both proteins S7K and S7B was compared to the published sequences of the other ribosomal proteins of Escherichia coli and predictions for the secondary structure of these proteins were made.<br />
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||<br />
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=385062 PubMed]<br />
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|-<br />
!align=left |Keywords<br />
||<br />
Amino Acid Sequence; Amino Acids/analysis; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Escherichia coli/analysis; Escherichia coli/genetics; Molecular Weight; Mutation; Protein Conformation; Ribosomal Proteins/genetics; Ribosomal Proteins/isolation & purification<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:385062&diff=1491308PMID:3850622014-06-25T01:22:58Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0019069_!_viral_capsid_assembly&diff=1491216Category:GO:0019069 ! viral capsid assembly2014-06-19T12:55:35Z<p>54.224.27.110: New GO term category page</p>
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:6285351&diff=1491173PMID:62853512014-06-15T10:07:00Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Feiss, M and Widner, W''' (1982) Bacteriophage lambda DNA packaging: scanning for the terminal cohesive end site during packaging. ''Proc. Natl. Acad. Sci. U.S.A.'' '''79''':3498-502<br />
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Bacteriophage lambda packages the DNA of the related phage 21 poorly [Hohn, B. (1975) J. Mol. Biol. 98, 93--106]. To understand the nature of the packaging defect, the interaction of the cohesive end site (cos) specific for phage 21 (cos phi 21) with phage lambda terminase has been investigated. The ability of lambda terminase to cleave cos phi 21 was studied in vitro; lambda terminase cleaved cos phi 21 only 1% as well as it cleaved the phage lambda cohesive end site (cos lambda). In vitro packaging experiments showed that the lambda and 21 packaging specificities observed in vivo are also found in vitro. The cos cleavage reaction was modified so that competition experiments could be performed; these experiments showed that cos phi 21 was unable to bind lambda terminase, thus identifying the nature of the defect. Previous work [Feiss, M., Fisher, R. A., Siegele, D. A., Nichols, B. P. & Donelson, J. E. (1979) Virology 92, 56--67] has shown that the base pairs giving lambda or 21 packaging specificity are at the left end of the chromosome, outside the 22-base-pair symmetry region that includes the annealed cohesive ends. Therefore, terminase binding to cos requires interactions with base pairs to the Nu1 side of the cohesive end symmetry segment. The evidence supports the proposition that cos consists of adjacent sites for binding of terminase and for nicking by terminase. Because cos phi 21 can be cut by lambda terminase to terminate DNA packaging, it is proposed that the terminase that binds and nicks at the initial cos site is brought into contact with the terminal cos site by the packaging process. Terminase recognizes and nicks the cohesive end sequence of the terminal cos without requiring the binding site.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6285351 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC346448 PMC346448]<br />
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Bacteriophage lambda/growth & development; Bacteriophage lambda/metabolism; Base Sequence; DNA, Viral/metabolism; Deoxyribonucleases/metabolism; Endodeoxyribonucleases; Endonucleases/metabolism; Genes, Regulator; Substrate Specificity; Virus Replication<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:6285351&diff=1491172PMID:62853512014-06-15T10:06:59Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:17933887&diff=1491147PMID:179338872014-06-14T01:14:00Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Abdallah, J, Caldas, T, Kthiri, F, Kern, R and Richarme, G''' (2007) YhbO protects cells against multiple stresses. ''J. Bacteriol.'' '''189''':9140-4<br />
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YhbO is a member of the DJ-1/ThiJ/Pfp1 superfamily, which includes chaperones, peptidases, and the Parkinson's disease protein DJ-1. A yhbO-disrupted mutant of Escherichia coli is highly sensitive to oxidative, thermal, UV, and pH stresses, and the putative nucleophilic cysteine C104 of YhbO is required for stress resistance. These results suggest that YhbO affects a central process in stress management.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17933887 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2168597 PMC2168597]<br />
Online version:[http://dx.doi.org/10.1128/JB.01208-07 10.1128/JB.01208-07]<br />
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Anti-Bacterial Agents/pharmacology; Cysteine/genetics; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli/radiation effects; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Heat-Shock Proteins/genetics; Heat-Shock Proteins/physiology; Hot Temperature; Hydrogen-Ion Concentration; Mutagenesis, Insertional; Oxidants/pharmacology; Ultraviolet Rays<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:17933887&diff=1491146PMID:179338872014-06-14T01:14:00Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:7007073&diff=1491127PMID:70070732014-06-13T01:22:24Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Yaguchi, M, Roy, C and Wittmann, HG''' (1980) The primary structure of protein S10 from the small ribosomal subunit of Escherichia coli. ''FEBS Lett.'' '''121''':113-6<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=7007073 PubMed]<br />
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Amino Acid Sequence; Bacterial Proteins; Computers; Escherichia coli; Hydrogen Bonding; Protein Conformation; Ribosomal Proteins; Ribosomes/ultrastructure<br />
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<references/></div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:7007073&diff=1491126PMID:70070732014-06-13T01:22:24Z<p>54.224.27.110: New PMID: Page!</p>
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<div>PMID on Demand placeholder</div>54.224.27.110https://ecoliwiki.org/colipedia/index.php?title=PMID:2693216&diff=1491063PMID:26932162014-06-08T02:09:22Z<p>54.224.27.110: Fill PMID: Page!</p>
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'''Anselme, J and Härtlein, M''' (1989) Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase. ''Gene'' '''84''':481-5<br />
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The Escherichia coli asnS gene codes for asparaginyl-tRNA synthetase (NRSEC). We have sequenced the asnS region, including 382 bp of the 5'-untranslated region, 1398 bp of the coding region and 280 bp of the 3'-untranslated region. The DNA-derived NRSEC amino acid (aa) sequence was confirmed by direct aa sequencing of the N-terminal parts of the native protein and of a 28-kDa internal fragment generated by trypsin digestion. The asnS gene product has been purified to homogeneity using three chromatographic steps. Sequence comparison of the deduced NRSEC sequence with all aminoacyl-tRNA synthetase sequences showed significant homologies with the yeast aspartyl-tRNA synthetase and weaker relationships with other aminoacyl-tRNA synthetases for aa with an XAX codon.<br />
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2693216 PubMed]<br />
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Amino Acid Sequence; Amino Acids/analysis; Amino Acyl-tRNA Synthetases/genetics; Aspartate-tRNA Ligase/genetics; Bacillus/enzymology; Bacillus/genetics; Base Sequence; Codon; DNA, Bacterial; DNA, Fungal; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; RNA, Transfer, Amino Acyl; Sequence Homology, Nucleic Acid; Yeasts/enzymology; Yeasts/genetics<br />
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<references/></div>54.224.27.110