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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1989-6-28
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pubmed:databankReference |
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pubmed:abstractText |
The oxyR gene is required for the induction of a regulon of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium. The E. coli oxyR gene has been cloned and sequenced, revealing an open reading frame (305 amino acids) that encodes a 34.4-kDa protein, which is produced in maxicells carrying the oxyR clone. The OxyR protein shows homology to a family of positive regulatory proteins including LysR in E. coli and NodD in Rhizobium. Like them, oxyR appears to be negatively autoregulated: an oxyR::lacZ gene fusion produced 5-fold higher levels of beta-galactosidase activity in oxyR null mutants compared to oxyR+ controls, and extracts from an OxyR-overproducing strain were able to protect regions (-27 to +21) of the oxyR promoter from DNase I digestion. DNA sequence analysis of the oxyR2 mutation, which causes overexpression of oxyR-regulated proteins in the absence of oxidative stress, showed that the oxyR2 phenotype is due to a missense mutation (C.G to T.A transition) that changes alanine to valine at amino acid position 234 of OxyR.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-1092200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-16453758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-212715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-2492495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-2884726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-2982793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-2988786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3003115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3030737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3032952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3040668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3045098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3052291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3062177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3288541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3293046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3413113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3534881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3555840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-355890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3596251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-368040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-3703684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-4006668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6236744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6283634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6310323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6348505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6350602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6390428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471187-6411928
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3484-8
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:2471187-Amino Acid Sequence,
pubmed-meshheading:2471187-Bacterial Proteins,
pubmed-meshheading:2471187-Base Sequence,
pubmed-meshheading:2471187-Cloning, Molecular,
pubmed-meshheading:2471187-DNA-Binding Proteins,
pubmed-meshheading:2471187-Escherichia coli,
pubmed-meshheading:2471187-Escherichia coli Proteins,
pubmed-meshheading:2471187-Gene Expression Regulation,
pubmed-meshheading:2471187-Genes, Bacterial,
pubmed-meshheading:2471187-Genes, Regulator,
pubmed-meshheading:2471187-Hydrogen Peroxide,
pubmed-meshheading:2471187-Molecular Sequence Data,
pubmed-meshheading:2471187-Molecular Weight,
pubmed-meshheading:2471187-Phenotype,
pubmed-meshheading:2471187-Promoter Regions, Genetic,
pubmed-meshheading:2471187-RNA, Bacterial,
pubmed-meshheading:2471187-RNA, Messenger,
pubmed-meshheading:2471187-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:2471187-Repressor Proteins,
pubmed-meshheading:2471187-Salmonella typhimurium,
pubmed-meshheading:2471187-Transcription Factors
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pubmed:year |
1989
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pubmed:articleTitle |
OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins.
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pubmed:affiliation |
Department of Biochemistry, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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