Publication Date:
1998-03-28
Description:
The OxyR transcription factor is sensitive to oxidation and activates the expression of antioxidant genes in response to hydrogen peroxide in Escherichia coli. Genetic and biochemical studies revealed that OxyR is activated through the formation of a disulfide bond and is deactivated by enzymatic reduction with glutaredoxin 1 (Grx1). The gene encoding Grx1 is regulated by OxyR, thus providing a mechanism for autoregulation. The redox potential of OxyR was determined to be -185 millivolts, ensuring that OxyR is reduced in the absence of stress. These results represent an example of redox signaling through disulfide bond formation and reduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, M -- Aslund, F -- Storz, G -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497290" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Bacterial Proteins/genetics/metabolism
;
Base Sequence
;
Cysteine/metabolism
;
*DNA-Binding Proteins
;
Disulfides/*metabolism
;
Escherichia coli/genetics/*metabolism
;
Escherichia coli Proteins
;
Gene Expression Regulation, Bacterial
;
Glutaredoxins
;
Glutathione/metabolism
;
Glutathione Disulfide/metabolism
;
Glutathione Reductase/metabolism
;
Hydrogen Peroxide/*metabolism/pharmacology
;
Molecular Sequence Data
;
Oxidation-Reduction
;
Oxidative Stress
;
*Oxidoreductases
;
Proteins/genetics/metabolism
;
Repressor Proteins/genetics/*metabolism
;
Signal Transduction
;
Thioredoxins/metabolism
;
Transcription Factors/genetics/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
