EcoliWiki - User contributions [en]

PMID:1632193

2014-09-27T16:17:29Z

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'''Ekstedt, E and Ridderstråle, Y''' (1992) Histochemical localization of carbonic anhydrase in the testis and epididymis of the rabbit. ''Acta Anat (Basel)'' '''143''':258-64
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!align=left |Abstract
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The distribution of carbonic anhydrase (CA) was studied in the testis and epididymis of mature, male rabbits using a cobalt precipitation method. CA was found only in the endothelium of the capillaries in the testis. The epididymal duct was divided into initial, middle and terminal segments. Strong cytoplasmic CA was present in the apical cells in the initial and middle segments. Vacuoles with CA staining in the membranes were found in the principal cells in the middle segment. Intensely stained basal cells were present in the terminal segment. In the last part of the terminal segment and the first of the ductus deferens the basolateral cell membranes were also stained. The function of the enzyme is discussed especially in relation to acidification of the epididymal fluid and facilitation of CO2 diffusion.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1632193 PubMed]

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Animals; Carbonic Anhydrases/analysis; Epididymis/chemistry; Epididymis/enzymology; Histocytochemistry; Male; Rabbits; Testis/chemistry; Testis/enzymology

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PMID:1632193

2014-09-27T16:17:28Z

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PMID on Demand placeholder

Category:GO:0046729 ! viral procapsid

2014-09-21T23:52:53Z

176.9.129.84: New GO term category page

{{GO term stub|GO:0046729_!_viral_procapsid}}

==References==
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PMID:2010260

2014-09-14T20:46:49Z

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'''Carmelli, D, McElroy, MR and Rosenman, RH''' (1991) Longitudinal changes in fat distribution in the Western Collaborative Group Study: a 23-year follow-up. ''Int J Obes'' '''15''':67-74
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!align=left |Abstract
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Anthropometric measurements for a total of 1,150 surviving subjects aged 65-86 and examined twice 23 years apart were analyzed with the following objectives: (1) to determine longitudinal changes on a large battery of anthropometric measures, (2) to examine the persistence of individual differences in the distribution of fat and relative weight, and (3) to investigate the relationship between changes in weight and changes in fat distribution. Significant changes toward an increase in size with age were observed in younger subjects below the age of 50 when first examined. In older subjects, age greater than or equal to 50, we observed a decrease in stature of 1.2 cm per decade, an overall decrease in weight of 1.6 kg, and no significant changes in trunk skinfold thickness. Longitudinal changes were most pronounced in the redistribution of fat and were also independent of weight changes. The relationships between measures of abdominal fat and overall obesity were stronger at follow-up than 23 years earlier.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2010260 PubMed]

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!align=left |Keywords
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Adipose Tissue/anatomy & histology; Adult; Age Factors; Aged; Aged, 80 and over; Anthropometry; Body Mass Index; Body Weight; Cross-Sectional Studies; Humans; Longitudinal Studies; Male; Middle Aged; Skinfold Thickness; Statistics as Topic

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PMID:2010260

2014-09-14T20:46:49Z

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PMID:17329260

2014-08-31T14:41:45Z

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'''Li, J, Machius, M, Chuang, JL, Wynn, RM and Chuang, DT''' (2007) The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism. ''J. Biol. Chem.'' '''282''':11904-13
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!align=left |Abstract
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A long standing controversy is whether an alternating activesite mechanism occurs during catalysis in thiamine diphosphate (ThDP)-dependent enzymes. We address this question by investigating the ThDP-dependent decarboxylase/dehydrogenase (E1b) component of the mitochondrial branched-chain alpha-keto acid dehydrogenase complex (BCKDC). Our crystal structure reveals that conformations of the two active sites in the human E1b heterotetramer harboring the reaction intermediate are identical. Acidic residues in the core of the E1b heterotetramer, which align with the proton-wire residues proposed to participate in active-site communication in the related pyruvate dehydrogenase from Bacillus stearothermophilus, are mutated. Enzyme kinetic data show that, except in a few cases because of protein misfolding, these alterations are largely without effect on overall activity of BCKDC, ruling out the requirement of a proton-relay mechanism in E1b. BCKDC overall activity is nullified at 50% phosphorylation of E1b, but it is restored to nearly half of the pre-phosphorylation level after dissociation and reconstitution of BCKDC with the same phosphorylated E1b. The results suggest that the abolition of overall activity likely results from the specific geometry of the half-phosphorylated E1b in the BCKDC assembly and not due to a disruption of the alternating active-site mechanism. Finally, we show that a mutant E1b containing only one functional active site exhibits half of the wild-type BCKDC activity, which directly argues against the obligatory communication between active sites. The above results provide evidence that the two active sites in the E1b heterotetramer operate independently during the ThDP-dependent decarboxylation reaction.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17329260 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M610843200 10.1074/jbc.M610843200]
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!align=left |Keywords
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3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/chemistry; 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/physiology; Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Geobacillus stearothermophilus/metabolism; Humans; Kinetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutation; Phosphorylation; Protons; Sequence Homology, Amino Acid

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PMID:17329260

2014-08-31T14:41:43Z

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PMID:10411889

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'''Kampranis, SC, Bates, AD and Maxwell, A''' (1999) A model for the mechanism of strand passage by DNA gyrase. ''Proc. Natl. Acad. Sci. U.S.A.'' '''96''':8414-9
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!align=left |Abstract
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The mechanism of type II DNA topoisomerases involves the formation of an enzyme-operated gate in one double-stranded DNA segment and the passage of another segment through this gate. DNA gyrase is the only type II topoisomerase able to introduce negative supercoils into DNA, a feature that requires the enzyme to dictate the directionality of strand passage. Although it is known that this is a consequence of the characteristic wrapping of DNA by gyrase, the detailed mechanism by which the transported DNA segment is captured and directed through the DNA gate is largely unknown. We have addressed this mechanism by probing the topology of the bound DNA segment at distinct steps of the catalytic cycle. We propose a model in which gyrase captures a contiguous DNA segment with high probability, irrespective of the superhelical density of the DNA substrate, setting up an equilibrium of the transported segment across the DNA gate. The overall efficiency of strand passage is determined by the position of this equilibrium, which depends on the superhelical density of the DNA substrate. This mechanism is concerted, in that capture of the transported segment by the ATP-operated clamp induces opening of the DNA gate, which in turn stimulates ATP hydrolysis.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10411889 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC17530 PMC17530]

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!align=left |Keywords
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Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Binding Sites; DNA/chemistry; DNA Topoisomerases, Type I/metabolism; DNA Topoisomerases, Type II/chemistry; DNA, Superhelical/chemistry; Escherichia coli/enzymology; Models, Molecular; Mutation; Nucleic Acid Conformation; Protein Conformation

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PMID:10411889

2014-08-04T14:20:14Z

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PMID on Demand placeholder

Category:GO:0043069 ! negative regulation of programmed cell death

2014-08-03T11:41:54Z

176.9.129.84: New GO term category page

{{GO term stub|GO:0043069_!_negative_regulation_of_programmed_cell_death}}

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PMID:12354604

2014-07-14T20:48:22Z

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'''Dougan, DA, Mogk, A, Zeth, K, Turgay, K and Bukau, B''' (2002) AAA+ proteins and substrate recognition, it all depends on their partner in crime. ''FEBS Lett.'' '''529''':6-10
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Members of the AAA+ superfamily have been identified in all organisms studied to date. They are involved in a wide range of cellular events. In bacteria, representatives of this superfamily are involved in functions as diverse as transcription and protein degradation and play an important role in the protein quality control network. Often they employ a common mechanism to mediate an ATP-dependent unfolding/disassembly of protein-protein or DNA-protein complexes. In an increasing number of examples it appears that the activities of these AAA+ proteins may be modulated by a group of otherwise unrelated proteins, called adaptor proteins. These usually small proteins specifically modify the substrate recognition of their AAA+ partner protein. The occurrence of such adaptor proteins are widespread; representatives have been identified not only in Escherichia coli but also in Bacillus subtilis, not to mention yeast and other eukaryotic organisms. Interestingly, from the currently known examples, it appears that the N domain of AAA+ proteins (the most divergent region of the protein within the family) provides a common platform for the recognition of these diverse adaptor proteins. Finally, the use of adaptor proteins to modulate AAA+ activity is, in some cases, an elegant way to redirect the activity of an AAA+ protein towards a particular substrate without necessarily affecting other activities of that AAA+ protein while, in other cases, the adaptor protein triggers a complete switch in AAA+ activity.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12354604 PubMed]

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!align=left |Keywords
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ATP-Dependent Proteases; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Bacillus subtilis/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Endopeptidase Clp; Endopeptidases/chemistry; Endopeptidases/metabolism; Escherichia coli Proteins/metabolism; Eukaryotic Cells/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Chaperones; Serine Endopeptidases/chemistry; Serine Endopeptidases/metabolism; Substrate Specificity

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PMID:12354604

2014-07-14T20:48:22Z

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PMID:4555420

2014-07-03T18:10:50Z

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'''Lambert, MP and Neuhaus, FC''' (1972) Mechanism of D-cycloserine action: alanine racemase from Escherichia coli W. ''J. Bacteriol.'' '''110''':978-87
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!align=left |Abstract
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The antibiotic d-cycloserine is an effective inhibitor of alanine racemase. The lack of inhibition by l-cycloserine of alanine racemase from Staphylococcus aureus led Roze and Strominger to formulate the cycloserine hypothesis. This hypothesis states that d-cycloserine has the conformation required of the substrates on the enzyme surface and that l-cycloserine cannot have this conformation. Alanine racemase from Escherichia coli W has been examined to establish whether these observations are a general feature of all alanine racemases. The enzyme (molecular weight = 95,000) has Michaelis-Menten constants of 4.6 x 10(-4)m and 9.7 x 10(-4)m for d- and l-alanine, respectively. The ratio of V(max) in the d- to l-direction is 2.3. The equilibrium constant calculated from the Haldane relationship is 1.11 +/- 0.15. Both d- and l-cycloserine are competitive inhibitors with constants (K(i)) of 6.5 x 10(-4)m and 2.1 x 10(-3)m, respectively. The ratio of K(m)d-alanine to K(i)d-cycloserine is 0.71, and the ratio of K(m)l-alanine to K(i)l-cycloserine is 0.46. Since l-cycloserine is an effective inhibitor, it is concluded that the cycloserine hypothesis does not apply to the enzyme from E. coli W.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4555420 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC247518 PMC247518]

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!align=left |Keywords
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Alanine/metabolism; Ammonium Sulfate; Butanols; Carbon Isotopes; Cell Fractionation; Cell-Free System; Centrifugation, Density Gradient; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; Cycloserine/pharmacology; Electrophoresis, Disc; Escherichia coli/enzymology; Escherichia coli/growth & development; Hydrogen-Ion Concentration; Isomerases/antagonists & inhibitors; Isomerases/isolation & purification; Isomerases/metabolism; Molecular Weight; Protamines; Stereoisomerism; Sucrose; Sulfates

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PMID:4555420

2014-07-03T18:10:50Z

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PMID on Demand placeholder

Category:GO:0019013 ! viral nucleocapsid

2014-07-02T20:00:42Z

176.9.129.84: New GO term category page

{{GO term stub|GO:0019013_!_viral_nucleocapsid}}

==References==
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PMID:6350296

2014-07-01T19:08:22Z

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'''Green, PR, Vanaman, TC, Modrich, P and Bell, RM''' (1983) Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase. ''J. Biol. Chem.'' '''258''':10862-6
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!align=left |Abstract
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The sn-glycerol-3-phosphate acyltransferase from Escherichia coli, an integral membrane protein whose activity is dependent on phospholipids, was purified to near homogeneity (Green, P. R., Merrill, A. H., Jr., and Bell, R. M., (1981) J. Biol. Chem. 256, 11151-11159). Determination of a partial NH2-terminal sequence and the COOH terminus permitted alignment of the polypeptide on the sequenced sn-glycerol-3-phosphate acyltransferase structural gene (Lightner, V. A., Bell, R. M., and Modrich, P. (1983) J. Biol. Chem. 258, 10856-10861). Processing of the sn-glycerol-3-phosphate acyltransferase is apparently limited to the removal of the NH2-terminal formylmethionine. Thirteen of 27 possible cyanogen bromide peptides predicted from the DNA sequence were purified, characterized, and assigned to their location in the primary structure. Three peptides located at positions throughout the sequence were partially sequenced by automated Edman degradation. The partial sequence analysis of the homogeneous sn-glycerol-3-phosphate acyltransferase is fully in accord with the primary structure inferred from the DNA sequence.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6350296 PubMed]

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!align=left |Keywords
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Acyltransferases/analysis; Amino Acid Sequence; Cyanogen Bromide; Escherichia coli/enzymology; Glycerol-3-Phosphate O-Acyltransferase/analysis; Peptide Fragments/analysis

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PMID:6350296

2014-07-01T19:08:21Z

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PMID:1656859

2014-06-26T16:04:48Z

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'''Hancock, RE, Farmer, SW, Li, ZS and Poole, K''' (1991) Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli. ''Antimicrob. Agents Chemother.'' '''35''':1309-14
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!align=left |Abstract
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The mechanism of uptake of aminoglycosides across the outer membrane of Escherichia coli was reevaluated. Porin-deficient mutants showed no alteration in gentamicin or kanamycin susceptibility. Furthermore, the influence of kanamycin on intrinsic tryptophan fluorescence of porin OmpF (Y. Kobayashi, and T. Nakae, Eur. J. Biochem. 151:231-236, 1985) was shown to be strongly influenced by protein concentration and EDTA. This led to the hypothesis that aminoglycoside-mediated increases and decreases in intrinsic tryptophan fluorescence were due to aggregation-disaggregation of OmpF mediated by interaction at a divalent cation binding site on OmpF. Gentamicin, kanamycin, and polymyxin B increased E. coli outer membrane permeability to the hydrophobic fluorescent compound 1-N-phenyl-naphthylamine (NPN) and the peptidoglycan-degrading enzyme lysozyme. Addition of Mg2+ blocked these permeabilizing activities. Furthermore, gentamicin and polymyxin B bound to Mg(2+)-binding sites on E. coli lipopolysaccharide, as determined in dansyl polymyxin displacement experiments. A polymyxin-resistant, lipopolysaccharide-altered pmr mutant of E. coli had a fourfold-lower MIC of gentamicin and kanamycin and was more poorly permeabilized to 1-N-phenylnaphthylamine than was its parent strain. These data were consistent with uptake of aminoglycosides across the E. coli outer membrane by the self-promoted uptake mechanism.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1656859 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC245163 PMC245163]

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!align=left |Keywords
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Anti-Bacterial Agents/metabolism; Anti-Bacterial Agents/pharmacology; Bacterial Outer Membrane Proteins/drug effects; Bacterial Outer Membrane Proteins/metabolism; Culture Media; Escherichia coli/drug effects; Escherichia coli/metabolism; Gentamicins/pharmacology; Kanamycin/pharmacology; Lipopolysaccharides/metabolism; Polymyxin B/pharmacology; Porins

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PMID:1656859

2014-06-26T16:04:47Z

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PMID:6756915

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'''Barker, DG, Ebel, JP, Jakes, R and Bruton, CJ''' (1982) Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. ''Eur. J. Biochem.'' '''127''':449-57
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!align=left |Abstract
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A 3300-base segment of Escherichia coli chromosomal DNA, cloned into pBR322, will complement a methionine auxotroph in which the lesion is a defective methionyl-tRNA synthetase with a much reduced affinity for methionine. Crude extracts of these transformants contain elevated levels of a protein which has a subunit molecular weight of 66 000, methionyl-tRNA synthetase aminoacylation activity in vitro and which cross-reacts with anti-(methionyl-tRNA synthetase) antibodies. This polypeptide is very slightly larger than the well-characterised and crystallised tryptic fragment of methionyl-tRNA synthetase. A DNA sequence of 1750 residues at one end of the cloned insert codes for a non-terminated open reading frame in which we can locate a large number of methionyl-tRNA synthetase tryptic and chymotryptic peptides. We have also sequenced 300 nucleotides upstream of this coding segment where we find a large invert repeat in the putative methionyl-tRNA synthetase promoter region.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6756915 PubMed]

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!align=left |Keywords
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Amino Acid Sequence; Amino Acyl-tRNA Synthetases/isolation & purification; Bacterial Proteins/isolation & purification; Chemical Phenomena; Chemistry; Chymotrypsin; Cloning, Molecular; Crystallization; DNA, Bacterial/isolation & purification; Escherichia coli/enzymology; Methionine-tRNA Ligase/genetics; Methionine-tRNA Ligase/isolation & purification; Peptide Fragments/isolation & purification; Trypsin

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PMID:6756915

2014-06-14T17:31:12Z

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PMID:2555351

2014-06-14T17:10:51Z

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||
'''Padan, E, Maisler, N, Taglicht, D, Karpel, R and Schuldiner, S''' (1989) Deletion of ant in Escherichia coli reveals its function in adaptation to high salinity and an alternative Na+/H+ antiporter system(s). ''J. Biol. Chem.'' '''264''':20297-302
|-
!align=left |Abstract
||
We have deleted the chromosomal ant gene from Escherichia coli by substitution with the kan gene, which encodes kanamycin resistance. The delta ant strains obtained cannot adapt to high sodium concentrations (700 mM, pH 6.8), which do not affect the wild type. The Na+ sensitivity of delta ant is pH dependent, increasing at alkaline pH. Thus at pH 8.5, 100 mM NaCl retard growth of delta ant with no effect on the wild type. The delta ant strains also cannot challenge the toxic effects of Li+ ions, a substrate of the Na+/H+ antiporter system. However, growth of these strains is normal on carbon sources which require Na+ ions for transport and growth. Moreover, antiporter activity, as measured in everted membrane vesicles, is not significantly impaired. A detailed analysis of the remaining antiporter activity in a delta ant strain reveals kinetic properties which differ from those displayed by the ant protein: (a) Km for transport of Li+ ions is about 15 times higher and (b) the activity is practically independent of intracellular pH. Our results demonstrate the presence of an alternative Na+/H+ antiporter(s) in E. coli, additional to ant system.
|-
!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2555351 PubMed]

|-
!align=left |Keywords
||
Blotting, Southern; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cell Membrane/metabolism; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/physiology; Genes, Bacterial; Hydrogen-Ion Concentration; Kinetics; Lithium/pharmacology; Osmolar Concentration; Plasmids; Potassium/pharmacology; Restriction Mapping; Sodium/pharmacology; Sodium-Hydrogen Antiporter; Transduction, Genetic

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==Significance {{HelpIcon|Help:Literature}} ==
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==References==
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2014-06-14T17:10:50Z

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'''Heermann, R, Weber, A, Mayer, B, Ott, M, Hauser, E, Gabriel, G, Pirch, T and Jung, K''' (2009) The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress. ''J. Mol. Biol.'' '''386''':134-48
|-
!align=left |Abstract
||
The sensor kinase KdpD and the response regulator KdpE control induction of the kdpFABC operon encoding the high-affinity K(+)-transport system KdpFABC in response to K(+) limitation or salt stress. Under K(+) limiting conditions the Kdp system restores the intracellular K(+) concentration, while in response to salt stress K(+) is accumulated far above the normal content. The kinase activity of KdpD is inhibited at high concentrations of K(+), so it has been puzzling how the sensor can be activated in response to salt stress. Here, we demonstrate that the universal stress protein UspC acts as a scaffolding protein of the KdpD/KdpE signaling cascade by interacting with a Usp domain in KdpD of the UspA subfamily under salt stress. Escherichia coli encodes three single domain proteins of this subfamily, UspA, UspC, and UspD, whose expression is up-regulated under various stress conditions. Among these proteins only UspC stimulated the in vitro reconstructed signaling cascade (KdpD-->KdpE-->DNA) resulting in phosphorylation of KdpE at a K(+) concentration that would otherwise almost prevent phosphorylation. In agreement, in a DeltauspC mutant KdpFABC production was down-regulated significantly when cells were exposed to salt stress, but unchanged under K(+) limitation. Biochemical studies revealed that UspC interacts specifically with the Usp domain in the stimulus perceiving N-terminal domain of KdpD. Furthermore, UspC stabilized the KdpD/KdpE~P/DNA complex and is therefore believed to act as a scaffolding protein. This study describes the stimulation of a bacterial two-component system under distinct stress conditions by a scaffolding protein, and highlights a new role of the universal stress proteins.
|-
!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19101563 PubMed]
Online version:[http://dx.doi.org/10.1016/j.jmb.2008.12.007 10.1016/j.jmb.2008.12.007]
|-
!align=left |Keywords
||
Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Models, Biological; Models, Molecular; Potassium/metabolism; Protein Conformation; Protein Kinases/metabolism; Protein Structure, Tertiary; Signal Transduction; Sodium Chloride/metabolism; Surface Plasmon Resonance; Trans-Activators/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
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'''Robert-Baudouy, JM and Portalier, RC''' (1974) [Studies of mutations in glucuronate catabolism in Escherichia coli K12 (author's transl)]. ''Mol. Gen. Genet.'' '''131''':31-46
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4603847 PubMed]

|-
!align=left |Keywords
||
Alcohol Oxidoreductases/analysis; Chromosome Mapping; Conjugation, Genetic; Escherichia coli/enzymology; Escherichia coli/metabolism; Genes; Genetics, Microbial; Glucuronates/metabolism; Mutation; Operon

|- class="tableEdit_footer"
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==Significance {{HelpIcon|Help:Literature}} ==
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'''Chernyaeva, NS, Murgola, EJ and Mankin, AS''' (1999) Suppression of nonsense mutations induced by expression of an RNA complementary to a conserved segment of 23S rRNA. ''J. Bacteriol.'' '''181''':5257-62
|-
!align=left |Abstract
||
We identified a short RNA fragment, complementary to the Escherichia coli 23S rRNA segment comprising nucleotides 735 to 766 (in domain II), which when expressed in vivo results in the suppression of UGA nonsense mutations in two reporter genes. Neither UAA nor UAG mutations, examined at the same codon positions, were suppressed by the expression of this antisense rRNA fragment. Our results suggest that a stable phylogenetically conserved hairpin at nucleotides 736 to 760 in 23S rRNA, which is situated close to the peptidyl transferase center, may participate in one or more specific interactions during peptide chain termination.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10464195 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC94030 PMC94030]

|-
!align=left |Keywords
||
Base Sequence; Chloramphenicol O-Acetyltransferase/biosynthesis; Chloramphenicol O-Acetyltransferase/genetics; Codon, Terminator; Conserved Sequence; Escherichia coli/genetics; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; RNA, Bacterial; RNA, Ribosomal, 23S; Suppression, Genetic

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

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{{LitMaterials}}

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<annotationlinks/>

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||
'''Wittmann-Liebold, B and Greuer, B''' (1980) Amino acid sequence of protein L22 from the large subunit of the Escherichia coli ribosome. ''FEBS Lett.'' '''121''':105-12
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7007072 PubMed]

|-
!align=left |Keywords
||
Amino Acid Sequence; Bacterial Proteins; Computers; Escherichia coli; Protein Conformation; Ribosomal Proteins; Ribosomes/ultrastructure

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==Significance {{HelpIcon|Help:Literature}} ==
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User:Wikiadmin

2014-06-09T07:22:15Z

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==References==
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2014-06-08T07:37:51Z

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'''Eyer, L, Pantůcek, R, Růzicková, V and Doskar, J''' (2007) [New perspectives of the phage therapy]. ''Klin. Mikrobiol. Infekc. Lek.'' '''13''':231-5
|-
!align=left |Abstract
||
A solution to the problem of the increasing number of antibiotic-resistant bacterial strains can be the use of rational phage therapy. In the past, bacteriophages (phages) were often used for the treatment and prevention of infections and unlike antibiotic therapy, phage therapy caused almost no serious side effects. While previously several preparations containing whole phage particles were available for phage therapy, currently, the isolation of well characterised and purified phage components with antibacterial properties opens up new options for the management of intractable infections caused primarily by the bacterial genera Enterococcus, Escherichia, Klebsiella, Listeria, Proteus, Pseudomonas, Salmonella, Shigella, Staphylococcus and Streptococcus. In addition to human and veterinary medicine, the phage therapy principles also find use in the agriculture and food industry. Recent and former clinical studies as well as numerous animal model experiments have supported that phage therapy is an effective and safe alternative of antibiotic treatment of bacterial infections.
|-
!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18320502 PubMed]

|-
!align=left |Keywords
||
Animals; Bacterial Infections/therapy; Bacteriophages; Drug Resistance, Microbial; Humans

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==Significance {{HelpIcon|Help:Literature}} ==
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PMID:18320502

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{| id="S5393f285e08d9" class=" tableEdit PMID_info_table"

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!align=left |Citation
||
'''Beckman, D and Cooper, S''' (1973) Temperature-sensitive nonsense mutations in essential genes of Escherichia coli. ''J. Bacteriol.'' '''116''':1336-42
|-
!align=left |Abstract
||
Cells containing nonsense mutations in essential genes have been isolated in a strain of Escherichia coli that carried the su4(ts) gene which specifies a temperature-sensitive tyrosine transfer ribonucleic acid. Such cells are unable to form colonies at temperatures which inactivate this suppressor transfer ribonucleic acid. A screening procedure for the identification of mutants that carry temperature-sensitive nonsense mutations in essential genes is described, and certain properties of two such mutants are reported.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4127628 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC246492 PMC246492]

|-
!align=left |Keywords
||
Chromosome Mapping; Escherichia coli/enzymology; Escherichia coli/isolation & purification; Escherichia coli/metabolism; Mutation; Nitrosoguanidines; Peptide Biosynthesis; Phenotype; RNA, Bacterial/biosynthesis; RNA, Transfer/biosynthesis; Staining and Labeling; Suppression, Genetic; Temperature; Transduction, Genetic

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

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<annotationlinks/>

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2014-06-08T05:20:05Z

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PMID:1953774

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{| id="V5392a5717364d" class=" tableEdit PMID_info_table"

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!align=left |Citation
||
'''Pontis, E, Sun, XY, Jörnvall, H, Krook, M and Reichard, P''' (1991) ClpB proteins copurify with the anaerobic Escherichia coli reductase. ''Biochem. Biophys. Res. Commun.'' '''180''':1222-6
|-
!align=left |Abstract
||
Two proteins, called alpha and beta 3, copurify with the anaerobic ribonucleotide reductase from Escherichia coli (Eliasson et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 3314-3318). Both are now identified as products of the clpB gene that is presumed to code for a subunit of an ATP dependent protease. The tight associations suggest the possibility that the ClpB proteins are involved in the regulation of the anaerobic reductase.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1953774 PubMed]

|-
!align=left |Keywords
||
ATP-Dependent Proteases; Amino Acid Sequence; Anaerobiosis; Antibodies, Monoclonal; Escherichia coli/enzymology; Escherichia coli/growth & development; Heat-Shock Proteins; Macromolecular Substances; Molecular Sequence Data; Ribonucleotide Reductases/isolation & purification; Sequence Homology, Nucleic Acid; Serine Endopeptidases/isolation & purification

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==Significance {{HelpIcon|Help:Literature}} ==
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<annotationlinks/>

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<references/>

PMID:1953774

2014-06-07T05:38:57Z

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{| id="G53923b94029ac" class=" tableEdit PMID_info_table"

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!align=left |Citation
||
'''Brosius, J, Schiltz, E and Chen, R''' (1975) The primary structure of the 5S RNA binding protein L18 from Escherichia coli ribosomes. ''FEBS Lett.'' '''56''':359-61
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1098937 PubMed]

|-
!align=left |Keywords
||
Amino Acid Sequence; Binding Sites; Escherichia coli/analysis; Macromolecular Substances; Protein Binding; RNA, Bacterial/metabolism; RNA, Ribosomal/metabolism; Ribosomal Proteins/metabolism; Ribosomes/analysis

|- class="tableEdit_footer"
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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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PMID:1098937

2014-06-06T22:07:15Z

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