Activation of the OxyR transcription factor by reversible disulfide bond formation

被引：979

作者：

Zheng, M

Åslund, F

Storz, G ^{[1
]}

机构：

[1] NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA

[2] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA

来源：

SCIENCE | 1998年 / 279卷 / 5357期

关键词：

D O I：

10.1126/science.279.5357.1718

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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, th us 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.

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页码：1718 / 1721

页数：4

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