Activation of the OxyR transcription factor by reversible disulfide bond formation
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 …
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 …
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.
AAAS