Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Sequence
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Cysteine / metabolism
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DNA-Binding Proteins*
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Disulfides / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins
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Gene Expression Regulation, Bacterial
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Glutaredoxins
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Glutathione / metabolism
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Glutathione Disulfide / metabolism
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Glutathione Reductase / metabolism
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Hydrogen Peroxide / metabolism*
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Hydrogen Peroxide / pharmacology
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Molecular Sequence Data
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Oxidation-Reduction
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Oxidative Stress
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Oxidoreductases*
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Proteins / genetics
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Proteins / metabolism
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Signal Transduction
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Thioredoxins / metabolism
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Transcription Factors / genetics
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Transcription Factors / metabolism*
Substances
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Bacterial Proteins
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DNA-Binding Proteins
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Disulfides
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Escherichia coli Proteins
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Glutaredoxins
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Proteins
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Repressor Proteins
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Transcription Factors
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oxyR protein, E coli
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Thioredoxins
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Hydrogen Peroxide
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Oxidoreductases
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Glutathione Reductase
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Glutathione
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Cysteine
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Glutathione Disulfide