EcoliWiki - User contributions [en]

PMID:4590170

2017-07-31T14:14:44Z

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'''Steinman, HM and Hill, RL''' (1973) Sequence homologies among bacterial and mitochondrial superoxide dismutases. ''Proc. Natl. Acad. Sci. U.S.A.'' '''70''':3725-9
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!align=left |Abstract
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Superoxide dismutase from chicken-liver mitochondria (manganese enzyme) and the two dismutases from Escherichia coli (manganese and iron enzymes) were analyzed through 29 cycles of automated Edman degradations. The high degree of homology among the amino-terminal sequences of these three dismutases corroborates their known similarity of structural and functional properties, and serves as further evidence for the endosymbiotic origin of mitochondria. In contrast, these three sequences exhibit no significant homology with the amino-terminal sequence of bovine-erythrocyte superoxide dismutase, which is consistent with the classification of eukaryotic copper-zinc dismutases as a family distinct from the manganese enzymes in stability and catalytic properties.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4590170 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC427315 PMC427315]

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Amino Acid Sequence; Animals; Autoanalysis; Biological Evolution; Cattle; Chickens; Erythrocytes/enzymology; Escherichia coli/enzymology; Iron; Manganese; Mitochondria, Liver/enzymology; Superoxide Dismutase/analysis; Superoxide Dismutase/blood; Superoxide Dismutase/isolation & purification

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PMID:4590170

2017-07-31T14:14:44Z

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PMID:1310503

2017-07-31T12:48:38Z

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'''Mendiola, MV, Jubete, Y and de la Cruz, F''' (1992) DNA sequence of IS91 and identification of the transposase gene. ''J. Bacteriol.'' '''174''':1345-51
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!align=left |Abstract
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IS91 is a 1,830-bp insertion sequence that inserts specifically at the sequence CAAG or GAAC of the target and does not duplicate any sequence upon insertion (23). By transposon mutagenesis, we have identified open reading frame 426 (ORF426; bp 454 to 1731) as the putative ORF for the transposase. It displays a cysteine-rich, potential metal-binding domain in its N-terminal region. Adjacent to ORF426, there is an ORF (ORF121) which precedes and terminally overlaps ORF426 by one amino acid. Tn1732 insertions in ORF121 do not affect the transposition frequency. IS91 has sequence similarities to IS801 from Pseudomonas syringae. Their putative transposases are 36% identical, including conservation of the cysteine-rich cluster. The information concerning IS801 insertion specificity and target duplication has been reevaluated in the light of our results.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1310503 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC206431 PMC206431]

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Amino Acid Sequence; Base Sequence; DNA Transposable Elements/genetics; Escherichia coli/genetics; Molecular Sequence Data; Mutagenesis, Insertional; Nucleotidyltransferases/genetics; Open Reading Frames/genetics; Pseudomonas/genetics; Sequence Alignment; Transposases

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==Significance {{HelpIcon|Help:Literature}} ==
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PMID:1310503

2017-07-31T12:48:37Z

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PMID:3305505

2017-07-29T14:03:46Z

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{| id="A597c95c154891" class=" tableEdit PMID_info_table"

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'''Fontecave, M, Eliasson, R and Reichard, P''' (1987) NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. ''J. Biol. Chem.'' '''262''':12325-31
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The active form of one subunit of Escherichia coli ribonucleotide reductase (protein B2) contains an organic free radical localized to tyrosine 122 of its polypeptide chain. When this radical is scavenged, e.g. by treatment with hydroxyurea, the enzyme is inactivated (protein B2/HU). E. coli contains an enzyme system consisting of at least three proteins that in the presence of NADPH, FMN, dithiothreitol, and oxygen introduce the tyrosyl radical into B2/HU (Eliasson, R., Jörnvall, H., and Reichard, P. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 2373-2377). One of the three proteins was identified as superoxide dismutase. We now identify a second protein, previously provisionally named Fraction c, as an NAD(P)H:flavin oxidoreductase (flavin reductase). After 4,000-fold purification the protein moved as a single band on sodium dodecyl sulfate gel electrophoresis with a molecular weight of 28,000-29,000. The enzyme contained no flavin but reduced riboflavin, FMN, and FAD by NADH, or riboflavin and FMN by NADPH. It is a powerful ferric iron reductase. We propose that its complementing activity during radical generation involves participation in the reduction of the ferric iron center of protein B2/HU. Radical formation is then linked to the reoxidation of iron by oxygen. The flavin reductase may also participate in other aspects of iron metabolism of E. coli.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3305505 PubMed]

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Chromatography, High Pressure Liquid; Escherichia coli/enzymology; FMN Reductase; Free Radicals; Isoelectric Focusing; Kinetics; NADH, NADPH Oxidoreductases/metabolism; Ribonucleotide Reductases/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
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PMID:3305505

2017-07-29T14:03:45Z

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PMID:11274125

2017-07-29T14:03:16Z

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'''Kobayashi, K, Tsukagoshi, N and Aono, R''' (2001) Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element. ''J. Bacteriol.'' '''183''':2646-53
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The AcrAB-TolC efflux pump plays an intrinsic role in resistance to hydrophobic solvents in Escherichia coli. E. coli OST5500 is hypersensitive to solvents due to inactivation of the acrB gene by insertion of IS30. Suppressor mutants showing high solvent resistance were isolated from OST5500. These mutants produced high levels of AcrE and AcrF proteins, which were not produced in OST5500, and in each mutant an insertion sequence (IS1 or IS2) was found integrated upstream of the acrEF operon, coding for the two proteins. The suppressor mutants lost solvent resistance on inactivation of the acrEF operon. The solvent hypersensitivity of OST5500 was suppressed by introduction of the acrEF operon with IS1 or IS2 integrated upstream but not by introduction of the operon lacking the integrated IS. It was concluded that IS integration activated acrEF, resulting in functional complementation of the acrB mutation. The acrB mutation was also complemented by a plasmid containing acrF or acrEF under the control of Plac. The wild-type tolC gene was found to be essential for complementation of the acrB mutation by acrEF. Thus, it is concluded that in these cells a combination of the proteins AcrA, AcrF, and TolC or the proteins AcrE, AcrF, and TolC is functional in solvent efflux instead of the AcrAB-TolC efflux pump.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11274125 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95182 PMC95182]
Online version:[http://dx.doi.org/10.1128/JB.183.8.2646-2653.2001 10.1128/JB.183.8.2646-2653.2001]
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Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins; DNA Transposable Elements; Drug Resistance, Microbial/genetics; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genetic Complementation Test; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Membrane Transport Proteins; Multidrug Resistance-Associated Proteins; Mutagenesis, Insertional; Mutation; Operon; Organic Chemicals/pharmacology; Plasmids/genetics; Solvents/pharmacology

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==Significance {{HelpIcon|Help:Literature}} ==
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PMID:11274125

2017-07-29T14:03:15Z

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Category:GO:0035312 ! 5'-3' exodeoxyribonuclease activity

2015-09-16T02:30:03Z

185.53.44.189: New GO term category page

{{GO term stub|GO:0035312_!_5'-3'_exodeoxyribonuclease_activity}}

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Category:GO:0000731 ! DNA synthesis during DNA repair

2015-09-12T03:20:40Z

185.53.44.189: New GO term category page

{{GO term stub|GO:0000731_!_DNA_synthesis_during_DNA_repair}}

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Category:GO:0046086 ! adenosine biosynthetic process

2015-07-19T17:18:58Z

185.53.44.189: New GO term category page

{{GO term stub|GO:0046086_!_adenosine_biosynthetic_process}}

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Category:GO:0032968 ! positive regulation of RNA elongation from RNA polymerase II promoter

2015-06-10T05:21:59Z

185.53.44.189: New GO term category page

{{GO term stub|GO:0032968_!_positive_regulation_of_RNA_elongation_from_RNA_polymerase_II_promoter}}

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