EcoliWiki - User contributions [en]

PMID:6997044

2014-09-07T00:57:39Z

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'''Ferenci, T''' (1980) The recognition of maltodextrins by Escherichia coli. ''Eur. J. Biochem.'' '''108''':631-6
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!align=left |Abstract
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1. Escherichia coli can accumulate 14C-labelled (alpha 1 leads to 4)-linked D-glucose oligomers up to maltoheptaose. Longer maltodextrins are not transported and are not utilized as carbon sources. 2. Maltodextrins too large to be transported are nevertheless bound by the outer envelope of intact E. coli. This binding is saturable (Kd for maltodecaose = 3-4 microM) and the binding sites are inducible by maltose. Each bacterium has approximately 30,000 sites when fully induced. 3. Using mutants devoid of various components of the maltose transport system, the high-affinity binding of maltodextrins by intact bacteria has been shown to be dependent on the presence of both lambda receptor (an outer membrane protein) and periplasmic maltose binding protein. 4. The same binding sites are accessible to both utilizable and non-utilizable maltodextrins. Maltodecapentaose is a competitive inhibitor of maltose transport (Ki 1.5-2.5 microM). 5. These results show that the periplasmic maltose binding protein is readily accessible to substrates of at least 2500 molecular weight. The inability to transport dextrins larger than maltoheptaose is, therefore, due to the inability of E. coli to transfer large substrates from the binding protein to the cytoplasm and not to lack of access through the outer membrane.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6997044 PubMed]

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!align=left |Keywords
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Biological Transport; Carrier Proteins/metabolism; Cell Membrane Permeability; Dextrins/metabolism; Escherichia coli/metabolism; Maltose/analogs & derivatives; Maltose/metabolism; Molecular Weight; Polysaccharides/metabolism

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PMID:6997044

2014-09-07T00:57:38Z

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PMID:1109286

2014-08-28T09:51:00Z

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'''Lozano-Reyes, S''' [Physiological varus of the pelvic extremities in children initiating walking]. ''Bol Med Hosp Infant Mex'' '''32''':157-67
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No abstract in PubMed
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1109286 PubMed]

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!align=left |Keywords
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Child, Preschool; Diagnosis, Differential; Female; Follow-Up Studies; Growth Disorders/radiography; Humans; Infant; Male; Movement; Osteochondritis/radiography; Rickets/radiography; Tibia/radiography

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PMID:1109286

2014-08-28T09:50:59Z

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PMID:22538653

2014-08-28T09:43:45Z

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'''Lee, C and Park, C''' (2012) Development of a suicidal vector-cloning system based on butanal susceptibility due to an expression of YqhD aldehyde reductase. ''J. Microbiol.'' '''50''':249-55
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!align=left |Abstract
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Previously, we observed butanal/propanal sensitivity of Escherichia coli K-12 when cells overexpress YqhD protein, a NADPH dependent aldehyde reductase, possibly due to an accumulation of butanol/propanol in vivo as the reaction products. Based on this finding, we developed a suicidal vector-cloning system derived from pUC19, in which lacZ was substituted with the yqhD gene. As a result, when foreign DNA was inserted into its multiple cloning sites by disrupting an expression of YqhD, the recombinants survived on butanal/propanal containing plate, whereas cells containing the YqhD vector died because of the alcohol production by YqhD. The cloning efficiency, estimated based on colony PCR and enzyme digestion, was achieved more than 90% when the suicidal vector system was used. Moreover, the plasmid vector itself was stably maintained in the cell, presumably due to its ability to remove toxic aldehydes being accumulated in E. coli cell by metabolic stress.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22538653 PubMed]
Online version:[http://dx.doi.org/10.1007/s12275-012-1438-5 10.1007/s12275-012-1438-5]
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!align=left |Keywords
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Aldehyde Reductase/genetics; Aldehyde Reductase/metabolism; Butanols/metabolism; Cloning, Molecular/methods; Escherichia coli K12/enzymology; Escherichia coli K12/genetics; Escherichia coli K12/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression; Genetic Vectors/genetics; Genetic Vectors/metabolism; Plasmids/genetics; Plasmids/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/metabolism

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PMID:22538653

2014-08-28T09:43:44Z

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PMID:625764

2014-08-16T19:13:06Z

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'''Wagner, SR and Greene, FE''' (1978) Dieldrin-induced alterations in biogenic amine content of rat brain. ''Toxicol. Appl. Pharmacol.'' '''43''':45-55
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No abstract in PubMed
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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=625764 PubMed]

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!align=left |Keywords
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Animals; Biogenic Amines/analysis; Brain Chemistry/drug effects; Dieldrin/pharmacology; Female; Male; Nervous System Diseases/chemically induced; Rats; Sex Factors; Time Factors

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PMID:625764

2014-08-16T19:13:05Z

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PMID:17007877

2014-08-04T19:21:28Z

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'''Madl, T, Van Melderen, L, Mine, N, Respondek, M, Oberer, M, Keller, W, Khatai, L and Zangger, K''' (2006) Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. ''J. Mol. Biol.'' '''364''':170-85
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!align=left |Abstract
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Toxin-antitoxin systems are highly abundant in plasmids and bacterial chromosomes. They ensure plasmid maintenance by killing bacteria that have lost the plasmid. Their expression is autoregulated at the level of transcription. Here, we present the solution structure of CcdA, the antitoxin of the ccd system, as a free protein (16.7 kDa) and in complex with its cognate DNA (25.3 kDa). CcdA is composed of two distinct and independent domains: the N-terminal domain, responsible for DNA binding, which establishes a new family of the ribbon-helix-helix fold and the C-terminal region, which is responsible for the interaction with the toxin CcdB. The C-terminal domain is intrinsically unstructured and forms a tight complex with the toxin. We show that CcdA specifically recognizes a 6 bp palindromic DNA sequence within the operator-promoter (OP) region of the ccd operon and binds to DNA by insertion of the positively charged N-terminal beta-sheet into the major groove. The binding of up to three CcdA dimers to a 33mer DNA of its operator-promoter region was studied by NMR spectroscopy, isothermal titration calorimetry and single point mutation. The highly flexible C-terminal region of free CcdA explains its susceptibility to proteolysis by the Lon ATP-dependent protease.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17007877 PubMed]
Online version:[http://dx.doi.org/10.1016/j.jmb.2006.08.082 10.1016/j.jmb.2006.08.082]
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!align=left |Keywords
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Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Toxins/chemistry; Calorimetry; Crystallography, X-Ray; DNA, Bacterial/chemistry; Dimerization; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Nucleic Acids/chemistry; Oligonucleotides/chemistry; Point Mutation; Promoter Regions, Genetic; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Solutions

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PMID:17007877

2014-08-04T19:21:28Z

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PMID:344065

2014-07-29T09:19:03Z

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'''Yaguchi, M and Wittmann, HG''' (1978) The primary structure of protein S17 from the small ribosomal subunit of Escherichia coli. ''FEBS Lett.'' '''87''':37-40
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No abstract in PubMed
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=344065 PubMed]

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

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PMID:344065

2014-07-29T09:19:03Z

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PMID:15066428

2014-07-29T05:59:57Z

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'''Sam, MD, Cascio, D, Johnson, RC and Clubb, RT''' (2004) Crystal structure of the excisionase-DNA complex from bacteriophage lambda. ''J. Mol. Biol.'' '''338''':229-40
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!align=left |Abstract
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The excisionase (Xis) protein from bacteriophage lambda is the best characterized member of a large family of recombination directionality factors that control integrase-mediated DNA rearrangements. It triggers phage excision by cooperatively binding to sites X1 and X2 within the phage, bending DNA significantly and recruiting the phage-encoded integrase (Int) protein to site P2. We have determined the co-crystal structure of Xis with its X2 DNA-binding site at 1.7A resolution. Xis forms a unique winged-helix motif that interacts with the major and minor grooves of its binding site using an alpha-helix and an ordered beta-hairpin (wing), respectively. Recognition is achieved through an elaborate water-mediated hydrogen-bonding network at the major groove interface, while the preformed hairpin forms largely non-specific interactions with the minor groove. The structure of the complex provides insights into how Xis recruits Int cooperatively, and suggests a plausible mechanism by which it may distort longer DNA fragments significantly. It reveals a surface on the protein that is likely to mediate Xis-Xis interactions required for its cooperative binding to DNA.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15066428 PubMed]
Online version:[http://dx.doi.org/10.1016/j.jmb.2004.02.053 10.1016/j.jmb.2004.02.053]
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!align=left |Keywords
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Amino Acid Sequence; Bacteriophage lambda/enzymology; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA/chemistry; DNA/metabolism; DNA Nucleotidyltransferases/chemistry; DNA Nucleotidyltransferases/metabolism; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nucleic Acid Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Viral Proteins

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PMID:15066428

2014-07-29T05:59:56Z

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PMID:16272399

2014-07-28T14:12:09Z

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'''Görke, B, Foulquier, E and Galinier, A''' (2005) YvcK of Bacillus subtilis is required for a normal cell shape and for growth on Krebs cycle intermediates and substrates of the pentose phosphate pathway. ''Microbiology (Reading, Engl.)'' '''151''':3777-91
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The HPr-like protein Crh has so far been detected only in the bacillus group of bacteria. In Bacillus subtilis, its gene is part of an operon composed of six ORFs, three of which exhibit strong similarity to genes of unknown function present in many bacteria. The promoter of the operon was determined and found to be constitutively active. A deletion analysis revealed that gene yvcK, encoded by this operon, is essential for growth on Krebs cycle intermediates and on carbon sources metabolized via the pentose phosphate pathway. In addition, cells lacking YvcK acquired media-dependent filamentous or L-shape-like aberrant morphologies. The presence of high magnesium concentrations restored normal growth and cell morphology. Furthermore, suppressor mutants cured from these growth defects appeared spontaneously with a high frequency. Such suppressing mutations were identified in a transposon mutagenesis screen and found to reside in seven different loci. Two of them mapped in genes of central carbon metabolism, including zwf, which encodes glucose-6-phosphate dehydrogenase and cggR, the product of which regulates the synthesis of glyceraldehyde-3-phosphate dehydrogenase. All these results suggest that YvcK has an important role in carbon metabolism, probably in gluconeogenesis required for the synthesis of cell wall precursor molecules. Interestingly, the Escherichia coli homologous protein, YbhK, can substitute for YvcK in B. subtilis, suggesting that the two proteins have been functionally conserved in these different bacteria.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16272399 PubMed]
Online version:[http://dx.doi.org/10.1099/mic.0.28172-0 10.1099/mic.0.28172-0]
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!align=left |Keywords
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Bacillus subtilis/genetics; Bacillus subtilis/growth & development; Bacillus subtilis/physiology; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Citric Acid Cycle; Culture Media; DNA Transposable Elements; Gene Expression Regulation, Bacterial; Mutagenesis, Insertional; Mutation; Operon; Pentose Phosphate Pathway; Phosphoproteins/genetics; Phosphoproteins/metabolism; Promoter Regions, Genetic

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PMID:16272399

2014-07-28T14:12:08Z

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PMID:1107801

2014-07-26T20:37:34Z

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'''Lo, TC and Sanwal, BD''' (1975) Genetic analysis of mutants of Escherichia coli defective in dicarboxylate transport. ''Mol. Gen. Genet.'' '''140''':303-7
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!align=left |Abstract
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Mutants of E.coli deficient in dicarboxylate transport can be mapped at three different loci. The dctA locus is linked to xyl and the dctB and cbt loci are linked to gal. Transduction tests reveal that the likely order of genes in the gal region is dctB-cbt-nadA-galK.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1107801 PubMed]

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!align=left |Keywords
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Biological Transport; Chromosome Mapping; Chromosomes, Bacterial; Dicarboxylic Acids/metabolism; Escherichia coli; Genetic Linkage; Mutation; Transduction, Genetic

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PMID:1107801

2014-07-26T20:37:34Z

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PMID:16798730

2014-07-22T03:05:07Z

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'''Belotserkovskii, BP, Arimondo, PB and Cozzarelli, NR''' (2006) Topoisomerase action on short DNA duplexes reveals requirements for gate and transfer DNA segments. ''J. Biol. Chem.'' '''281''':25407-15
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!align=left |Abstract
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Type II topoisomerases change DNA topology by passage of one DNA duplex (the transfer, T-segment) through a transient double-stranded break in another (the gate, G-segment). Here we monitor the passage between short double-stranded DNA segments within long single-stranded DNA circles that leads to catenation of the circles. To facilitate catenation, the circles were brought into close proximity using a tethering oligonucleotide, which was removed after the reaction was complete. We varied the length and the composition of the reacting DNA segments. The minimal DNA duplex length at which we detected catenation was 50-60 bp for DNA gyrase and 40 bp for topoisomerase IV (Topo IV). For Topo IV, catenation was observed when one, but not both, of the DNA-DNA duplexes was replaced by a DNA-RNA duplex. Topo IV cleaved the DNA-DNA duplex, but not the DNA-RNA duplex implying that the DNA-RNA duplex can be a T-segment but not a G-segment.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16798730 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M603977200 10.1074/jbc.M603977200]
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!align=left |Keywords
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Adenosine Triphosphate/chemistry; DNA/chemistry; DNA Gyrase/chemistry; DNA Topoisomerases, Type I/physiology; DNA, Single-Stranded/chemistry; Escherichia coli/enzymology; Models, Biological; Nucleic Acid Hybridization; Oligonucleotides/chemistry; RNA/chemistry

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PMID:16798730

2014-07-22T03:05:06Z

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PMID:9179852

2014-07-18T19:55:11Z

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'''Green, J and Baldwin, ML''' (1997) HlyX, the FNR homologue of Actinobacillus pleuropneumoniae, is a [4Fe-4S]-containing oxygen-responsive transcription regulator that anaerobically activates FNR-dependent class I promoters via an enhanced AR1 contact. ''Mol. Microbiol.'' '''24''':593-605
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!align=left |Abstract
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The hlyX gene of the pig pathogen Actinobacillus pleuropneumoniae encodes HlyX, a homologue of FNR, the anaerobic transcription regulator of Escherichia coli. The hlyX gone complements the anaerobic respiratory deficiencies of E. coli fnr mutants but also induces the expression of an otherwise latent haemolysin. Therefore, FNR and HlyX have distinct but overlapping regulons. The hlyX gene has been overexpressed as a gst::hlyX fusion and the HlyX protein purified. Similar to FNR, HlyX can acquire a [4Fe-4S] cluster, which promotes binding to the FNR box (Kd of 20-30 nM) under anaerobic conditions. Expression of hlyX in E. coli induced the anaerobic production of at least five polypeptides, including the yfiD gene product, which were not induced by fnr. Analysis of the yfiD promoter region revealed the presence of two FNR boxes situated at -61.5 and -114.5. Consistent with this observation, expression from the semi-synthetic Class I promoter FF + 20pmelR was efficiently activated by HlyX but not by FNR. The weaker level of FNR-mediated activation of Class I promoters suggests that there is a poorer activating contact (activating region 1 (AR1) equivalent) between FNR and RNA polymerase at these promoters and that HlyX possesses an additional or improved AR1. The AR1 of HlyX is partially characterized by a surface-exposed region around amino acid A187, which confers the altered specificity and provides an explanation for the existence of distinct but overlapping HlyX and FNR regulons.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9179852 PubMed]

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!align=left |Keywords
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Actinobacillus pleuropneumoniae/genetics; Actinobacillus pleuropneumoniae/metabolism; Actinobacillus pleuropneumoniae/pathogenicity; Amino Acid Sequence; Anaerobiosis; Animals; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites/genetics; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; DNA-Binding Proteins; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Bacterial; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Promoter Regions, Genetic; Protein Conformation; Regulon; Swine; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/metabolism; Transcriptional Activation

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183686.R53c97b9e986d7&page=183686&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:9179852

2014-07-18T19:55:10Z

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PMID:11591347

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{| id="C53c401ed4d645" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Martín, CS, Burnett, RM, de Haas, F, Heinkel, R, Rutten, T, Fuller, SD, Butcher, SJ and Bamford, DH''' (2001) Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions. ''Structure'' '''9''':917-30
|-
!align=left |Abstract
||
The dsDNA bacteriophage PRD1 has a membrane inside its icosahedral capsid. While its large size (66 MDa) hinders the study of the complete virion at atomic resolution, a 1.65-A crystallographic structure of its major coat protein, P3, is available. Cryo-electron microscopy (cryo-EM) and three-dimensional reconstruction have shown the capsid at 20-28 A resolution. Striking architectural similarities between PRD1 and the mammalian adenovirus indicate a common ancestor.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11591347 PubMed]

|-
!align=left |Keywords
||
Adenoviruses, Human/chemistry; Bacteriophage PRD1/chemistry; Bacteriophage PRD1/ultrastructure; Capsid/chemistry; Capsid/ultrastructure; Computer Simulation; Cryoelectron Microscopy/methods; Crystallography, X-Ray/methods; DNA, Viral/chemistry; DNA, Viral/ultrastructure; Image Enhancement/methods; Models, Molecular; Protein Conformation; Viral Envelope Proteins/chemistry; Viral Envelope Proteins/ultrastructure; Virion/chemistry; Virion/ultrastructure

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183680.C53c401ed4d645&page=183680&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:11591347

2014-07-14T16:14:37Z

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PMID:17158458

2014-07-08T08:19:39Z

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{| id="U53bba99a3d29a" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Weitz, D, Harder, D, Casagrande, F, Fotiadis, D, Obrdlik, P, Kelety, B and Daniel, H''' (2007) Functional and structural characterization of a prokaryotic peptide transporter with features similar to mammalian PEPT1. ''J. Biol. Chem.'' '''282''':2832-9
|-
!align=left |Abstract
||
The ydgR gene of Escherichia coli encodes a protein of the proton-dependent oligopeptide transporter (POT) family. We cloned YdgR and overexpressed the His-tagged fusion protein in E. coli BL21 cells. Bacterial growth inhibition in the presence of the toxic phosphonopeptide alafosfalin established YgdR functionality. Transport was abolished in the presence of the proton ionophore carbonyl cyanide p-chlorophenylhydrazone, suggesting a proton-coupled transport mechanism. YdgR transports selectively only di- and tripeptides and structurally related peptidomimetics (such as aminocephalosporins) with a substrate recognition pattern almost identical to the mammalian peptide transporter PEPT1. The YdgR protein was purified to homogeneity from E. coli membranes. Blue native-polyacrylamide gel electrophoresis and transmission electron microscopy of detergent-solubilized YdgR suggest that it exists in monomeric form. Transmission electron microscopy revealed a crown-like structure with a diameter of approximately 8 nm and a central density. These are the first structural data obtained from a proton-dependent peptide transporter, and the YgdR protein seems an excellent model for studies on substrate and inhibitor interactions as well as on the molecular architecture of cell membrane peptide transporters.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17158458 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M604866200 10.1074/jbc.M604866200]
|-
!align=left |Keywords
||
Animals; Biological Transport; Cell Membrane/metabolism; DNA Primers; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Mammals; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/genetics; Polymerase Chain Reaction; Proteolipids/metabolism; Symporters/chemistry; Symporters/genetics; Symporters/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183665.U53bba99a3d29a&page=183665&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:17158458

2014-07-08T08:19:38Z

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PMID:4923012

2014-07-03T09:48:28Z

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{| id="N53b526ec2ae56" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Buchwald, M, Murialdo, H and Siminovitch, L''' (1970) The morphogenesis of bacteriophage lambda. II. Identification of the principal structural proteins. ''Virology'' '''42''':390-400
|-
!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=4923012 PubMed]

|-
!align=left |Keywords
||
Acrylates; Amino Acids/metabolism; Autoradiography; Carbon Isotopes; Centrifugation, Density Gradient; Cesium; Chlorides; Chromosome Mapping; Coliphages/analysis; Culture Media; Electrophoresis; Escherichia coli/growth & development; Escherichia coli/radiation effects; Gels; Genes; Genetics, Microbial; Molecular Weight; Mutation; Sodium; Sulfates; Ultraviolet Rays; Viral Proteins/analysis

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|}


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

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

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

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

==See also==

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

PMID:4923012

2014-07-03T09:48:28Z

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PMID:17269935

2014-07-03T09:44:40Z

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{| id="X53b52607867b4" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Ang, EL, Obbard, JP and Zhao, H''' (2007) Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis. ''FEBS J.'' '''274''':928-39
|-
!align=left |Abstract
||
Aniline dioxygenase is a multicomponent Rieske nonheme-iron dioxygenase enzyme isolated from Acinetobacter sp. strain YAA. Saturation mutagenesis of the substrate-binding pocket residues, which were identified using a homology model of the alpha subunit of the terminal dioxygenase (AtdA3), was used to probe the molecular determinants of AtdA substrate specificity. The V205A mutation widened the substrate specificity of aniline dioxygenase to include 2-isopropylaniline, for which the wild-type enzyme has no activity. The V205A mutation also made 2-isopropylaniline a better substrate for the enzyme than 2,4-dimethylaniline, a native substrate of the wild-type enzyme. The I248L mutation improved the activity of aniline dioxygenase against aniline and 2,4-dimethylaniline approximately 1.7-fold and 2.1-fold, respectively. Thus, it is shown that the alpha subunit of the terminal dioxygenase indeed plays a part in the substrate specificity as well as the activity of aniline dioxygenase. Interestingly, the equivalent residues of V205 and I248 have not been previously reported to influence the substrate specificity of other Rieske dioxygenases. These results should facilitate future engineering of the enzyme for bioremediation and industrial applications.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17269935 PubMed]
Online version:[http://dx.doi.org/10.1111/j.1742-4658.2007.05638.x 10.1111/j.1742-4658.2007.05638.x]
|-
!align=left |Keywords
||
Acinetobacter/enzymology; Acinetobacter/metabolism; Aniline Compounds/chemistry; Aniline Compounds/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Carcinogens/chemistry; Carcinogens/metabolism; Dioxygenases/chemistry; Dioxygenases/genetics; Dioxygenases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Models, Molecular; Mutagenesis; Protein Subunits/chemistry; Protein Subunits/metabolism; Structure-Activity Relationship; Substrate Specificity

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183654.X53b52607867b4&page=183654&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:17269935

2014-07-03T09:44:39Z

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PMID:2123958

2014-06-29T12:46:25Z

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{| id="X53b00aa13feff" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Jackson, GE, Wynchank, S and Woudenberg, M''' (1990) Gadolinium(III) complex equilibria: the implications for Gd(III) MRI contrast agents. ''Magn Reson Med'' '''16''':57-66
|-
!align=left |Abstract
||
A computer model of blood plasma which has allowed the effect of Gd(III) contrast agents to be simulated has been developed. Initial binding of Gd(III) is to transferrin. At high concentration the metal ion binds to citrate and salicylate. At a concentrate of 10(-3) M, GdCl3 is predicted to effect a redistribution of the in vivo Zn(II), Ca(II), and Fe(II) complexes present in blood plasma. There is little effect on the Cu(II) distribution. At a concentration below 10(-5) M EDTA and DTPA have little effect on the free Gd(III) metal ion concentration. Above this concentration though, the metal ion is bound almost exclusively to the EDTA or DTPA. An attempt is made to relate the toxicity of GdCl3, [Gd(EDTA)]-, and [Gd(DTPA)]2- to the thermodynamic stability of these complexes. The effect of substitution kinetics is also discussed.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2123958 PubMed]

|-
!align=left |Keywords
||
Computer Simulation; Contrast Media; Edetic Acid/pharmacology; Gadolinium/blood; Gadolinium/pharmacokinetics; Gadolinium/toxicity; Humans; Iron/blood; Lethal Dose 50; Magnetic Resonance Imaging/methods; Metals/blood; Models, Biological; Models, Chemical; Molecular Weight; Pentetic Acid/pharmacology

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|}


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

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

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

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

==See also==

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

PMID:2123958

2014-06-29T12:46:25Z

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PMID on Demand placeholder

Category:GO:0003909 ! DNA ligase activity

2014-06-20T11:11:41Z

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{{GO term stub|GO:0003909_!_DNA_ligase_activity}}

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

PMID:2570061

2014-06-16T11:16:15Z

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{| id="P539ed1ff3d58a" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Suzuki, H, Kumagai, H, Echigo, T and Tochikura, T''' (1989) DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt. ''J. Bacteriol.'' '''171''':5169-72
|-
!align=left |Abstract
||
The DNA sequence of ggt, the gene that codes for gamma-glutamyltranspeptidase (EC 2.3.2.2) of Escherichia coli K-12, has been determined. The sequence contains a single open reading frame encoding the signal peptide and large and small subunits, in that order. This result suggests that E. coli gamma-glutamyltranspeptidase is processed posttranslationally.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2570061 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC210333 PMC210333]

|-
!align=left |Keywords
||
Amino Acid Sequence; Animals; Base Sequence; DNA, Bacterial/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Humans; Kidney/enzymology; Liver/enzymology; Molecular Sequence Data; Rats; Sequence Homology, Nucleic Acid; gamma-Glutamyltransferase/genetics

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183573.P539ed1ff3d58a&page=183573&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:2570061

2014-06-16T11:16:15Z

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PMID:164855

2014-06-15T15:21:30Z

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{| id="F539db9fa09916" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Sakamoto, S, Sakamoto, M, Goldhaber, P and Glimcher, M''' (1975) Collagenase and bone resorption: isolation of collagenase from culture medium containing serum after stimulation of bone resorption by addition of parathyroid hormone extract. ''Biochem. Biophys. Res. Commun.'' '''63''':172-8
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=164855 PubMed]

|-
!align=left |Keywords
||
Animals; Bone Resorption/drug effects; Bone and Bones/enzymology; Chromatography, Affinity; Collagen; Culture Media; Embryo, Mammalian; Heparin/pharmacology; Kinetics; Methods; Mice; Microbial Collagenase/isolation & purification; Microbial Collagenase/metabolism; Organ Culture Techniques; Parathyroid Hormone/pharmacology; Rats; Skin

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183570.F539db9fa09916&page=183570&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:164855

2014-06-15T15:21:29Z

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PMID:11087118

2014-06-14T03:39:22Z

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{| id="S539bc3e9cd593" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Wrzesinski, J, Bakin, A, Ofengand, J and Lane, BG''' (2000) Isolation and properties of Escherichia coli 23S-RNA pseudouridine 1911, 1915, 1917 synthase (RluD). ''IUBMB Life'' '''50''':33-7
|-
!align=left |Abstract
||
All nine pseudouridine (psi) residues in Escherichia coli 23S RNA are in or very near the peptidyl transfer centre (PTC) of the ribosome. Five psi synthases catalyze synthesis of these nine psi's. Deletion of the gene for one psi synthase, RluD, which directs synthesis of three closely clustered psi's in the decoding site of the PTC, has a profound negative impact on cell growth. We describe the isolation, without amplification from a cloned coding element, of the triple-site modifying enzyme, RluD, the N-terminal sequence of which has been used to clone and express the corresponding gene, rluD. Unlike "expressed" RluD, which so far has not been shown to modify one (1911) of the three closely clustered sites (1911, 1915, 1917), "natural" RluD modifies all three sites; and unlike another pai synthase, RluA, natural RluD has greatly expanded modifying activity at low Mg concentrations. These properties of the expressed and natural forms of RluD are discussed.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11087118 PubMed]
Online version:[http://dx.doi.org/10.1080/15216540050176566 10.1080/15216540050176566]
|-
!align=left |Keywords
||
Amino Acid Sequence; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli Proteins; Hydro-Lyases; Intramolecular Transferases/chemistry; Intramolecular Transferases/isolation & purification; Intramolecular Transferases/metabolism; Magnesium/metabolism; Molecular Sequence Data; Pseudouridine/biosynthesis; RNA, Ribosomal, 23S/metabolism

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183558.S539bc3e9cd593&page=183558&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:11087118

2014-06-14T03:39:21Z

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PMID:18284581

2014-06-13T18:41:48Z

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{| id="Z539b45ebe2346" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Chodavarapu, S, Gomez, R, Vicente, M and Kaguni, JM''' (2008) Escherichia coli Dps interacts with DnaA protein to impede initiation: a model of adaptive mutation. ''Mol. Microbiol.'' '''67''':1331-46
|-
!align=left |Abstract
||
During exponential growth, the level of Dps transiently increases in response to oxidative stress to sequester and oxidize Fe2+, which would otherwise lead to hydroxyl radicals that damage the bacterial chromosome. We report that Dps specifically interacts with DnaA protein by affinity chromatography and a solid phase binding assay, requiring the N-terminal region of DnaA to interact. In vitro, Dps inhibits DnaA function in initiation by interfering with strand opening of the replication origin. Comparing isogenic dps+ and dps::kan strains by flow cytometry and by quantitative polymerase chain reaction assays at either the chromosomally encoded level, or at an elevated level encoded by an inducible plasmid, we show that Dps causes less frequent initiations. Results from genetic experiments support this conclusion. We suggest that Dps acts as a checkpoint during oxidative stress to reduce initiations, providing an opportunity for mechanisms to repair oxidative DNA damage. Because Dps does not block initiations absolutely, duplication of the damaged DNA is expected to increase the genetic variation of a population, and the probability that genetic adaptation leads to survival under conditions of oxidative stress.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18284581 PubMed]
Online version:[http://dx.doi.org/10.1111/j.1365-2958.2008.06127.x 10.1111/j.1365-2958.2008.06127.x]
|-
!align=left |Keywords
||
Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Bacterial Outer Membrane Proteins/physiology; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; DNA Replication/genetics; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; DNA-Binding Proteins/physiology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/physiology; Gene Expression Regulation, Bacterial; Magnesium/pharmacology; Mutation; Protein Binding/drug effects; Replication Origin/genetics; Transcription, Genetic

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183554.Z539b45ebe2346&page=183554&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


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

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

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

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

==See also==

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

PMID:18284581

2014-06-13T18:41:47Z

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PMID on Demand placeholder

Category:GO:0098003 ! viral tail assembly

2014-06-13T09:47:49Z

54.204.166.135: New GO term category page

{{GO term stub|GO:0098003_!_viral_tail_assembly}}

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

Category:GO:0098015 ! virus tail

2014-06-12T03:43:26Z

54.204.166.135: New GO term category page

{{GO term stub|GO:0098015_!_virus_tail}}

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

PMID:16531068

2014-06-11T20:38:04Z

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|-
!align=left |Citation
||
'''Schumacher, J, Joly, N, Rappas, M, Zhang, X and Buck, M''' (2006) Structures and organisation of AAA+ enhancer binding proteins in transcriptional activation. ''J. Struct. Biol.'' '''156''':190-9
|-
!align=left |Abstract
||
Initiation of transcription is a major point of transcriptional regulation and invariably involves the transition from a closed to an open RNA polymerase (RNAP) promoter complex. In the case of the sigma(54)-RNAP, this multi step process requires energy, provided by ATP hydrolysis occurring within the AAA+ domain of enhancer binding proteins (EBPs). Typically, EBPs have an N-terminal regulatory domain, a central AAA+ domain that directly contacts sigma(54) and a C-terminal DNA binding domain. The following AAA+ EBP crystal structures have recently become available: heptameric AAA+ domains of NtrC1 and dimeric NtrC1 with its regulatory domain, hexameric AAA+ domains of ZraR with DNA binding domains, apo and nucleotide bound forms of the AAA+ domain of PspF as well as a cryo-EM structure of the AAA+ domain of PspF complexed with sigma(54). These AAA+ domains reveal the structural conservation between EBPs and other AAA+ domains. EBP specific structural features involved in substrate remodelling are located proximal to the pore of the hexameric ring. Parallels with the substrate binding elements near the central pore of other AAA+ members are drawn. We propose a structural model of EBPs in complex with a sigma(54)-RNAP-promoter complex.
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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=16531068 PubMed]
Online version:[http://dx.doi.org/10.1016/j.jsb.2006.01.006 10.1016/j.jsb.2006.01.006]
|-
!align=left |Keywords
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Adenosine Triphosphate/metabolism; Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Catalytic Domain; Consensus Sequence; Conserved Sequence; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Enhancer Elements, Genetic; Hydrolysis; Models, Chemical; Molecular Sequence Data; Nucleotides/metabolism; Promoter Regions, Genetic; Protein Binding; Protein Structure, Tertiary; RNA Polymerase Sigma 54/metabolism; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Transcriptional Activation

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==Significance {{HelpIcon|Help:Literature}} ==
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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==References==
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PMID:16531068

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'''Colbourne, JK, Singan, VR and Gilbert, DG''' (2005) wFleaBase: the Daphnia genome database. ''BMC Bioinformatics'' '''6''':45
|-
!align=left |Abstract
||
wFleaBase is a database with the necessary infrastructure to curate, archive and share genetic, molecular and functional genomic data and protocols for an emerging model organism, the microcrustacean Daphnia. Commonly known as the water-flea, Daphnia's ecological merit is unequaled among metazoans, largely because of its sentinel role within freshwater ecosystems and over 200 years of biological investigations. By consequence, the Daphnia Genomics Consortium (DGC) has launched an interdisciplinary research program to create the resources needed to study genes that affect ecological and evolutionary success in natural environments.
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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=15752432 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC555599 PMC555599]
Online version:[http://dx.doi.org/10.1186/1471-2105-6-45 10.1186/1471-2105-6-45]
|-
!align=left |Keywords
||
Animals; Chromosome Mapping; Computational Biology/methods; Computer Graphics; Daphnia/genetics; Database Management Systems; Databases, Factual; Databases, Genetic; Ecology; Ecosystem; Evolution, Molecular; Genetics, Population; Genome; Genomics; Information Services; Information Storage and Retrieval; Internet; Software

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

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

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

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

==See also==

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

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'''Smith, JD, Barnett, L, Brenner, S and Russell, RL''' (1970) More mutant tyrosine transfer ribonucleic acids. ''J. Mol. Biol.'' '''54''':1-14
|-
!align=left |Abstract
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No abstract in PubMed
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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=4923867 PubMed]

|-
!align=left |Keywords
||
Coliphages; Electrophoresis; Escherichia coli/analysis; Gels; Genetic Code; Ligases; Mutation; Phosphorus Isotopes; RNA, Transfer/biosynthesis; RNA, Transfer/isolation & purification; Suppression, Genetic; Temperature; Tyrosine

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

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

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

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

==See also==

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

PMID:4923867

2014-06-08T02:32:44Z

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'''Bader, M, Muse, W, Ballou, DP, Gassner, C and Bardwell, JC''' (1999) Oxidative protein folding is driven by the electron transport system. ''Cell'' '''98''':217-27
|-
!align=left |Abstract
||
Disulfide bond formation is catalyzed in vivo by DsbA and DsbB. Here we reconstitute this oxidative folding system using purified components. We have found the sources of oxidative power for protein folding and show how disulfide bond formation is linked to cellular metabolism. We find that disulfide bond formation and the electron transport chain are directly coupled. DsbB uses quinones as electron acceptors, allowing various choices for electron transport to support disulfide bond formation. Electrons flow via cytochrome bo oxidase to oxygen under aerobic conditions or via cytochrome bd oxidase under partially anaerobic conditions. Under truly anaerobic conditions, menaquinone shuttles electrons to alternate final electron acceptors such as fumarate. This flexibility reflects the vital nature of the disulfide catalytic system.
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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=10428033 PubMed]

|-
!align=left |Keywords
||
Anaerobiosis; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Catalytic Domain; Cytochromes/metabolism; DNA Primers; Disulfides/metabolism; Electron Transport/physiology; Electron Transport Chain Complex Proteins; Electron Transport Complex IV/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutagenesis/physiology; Oxidation-Reduction; Oxidoreductases/metabolism; Oxygen/analysis; Protein Disulfide-Isomerases/chemistry; Protein Disulfide-Isomerases/genetics; Protein Disulfide-Isomerases/metabolism; Protein Folding; Ubiquinone/metabolism

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

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

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

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

==See also==

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