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Science 13 March 1998:
Vol. 279. no. 5357, pp. 1718 - 1722
DOI: 10.1126/science.279.5357.1718
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Reports

Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation

Ming Zheng, Fredrik Åslund, Gisela Storz *

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.

M. Zheng and G. Storz, Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
F. Åslund, Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
*   To whom correspondence should be addressed. E-mail: storz{at}helix.nih.gov

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Identification of Albumin Precursor Protein, Phi AP3, and alpha -Smooth Muscle Actin as Novel Components of Redox Sensing Machinery in Vascular Smooth Muscle Cells.
M. T. Holderman, K. P. Miller, L. J. Dangott, and K. S. Ramos (2002)
Mol. Pharmacol. 61, 1174-1183
   Abstract »    Full Text »    PDF »
Regulation of the nfsA Gene in Escherichia coli by SoxS.
E. S. Paterson, S. E. Boucher, and I. B. Lambert (2002)
J. Bacteriol. 184, 51-58
   Abstract »    Full Text »    PDF »
Free Radicals in the Physiological Control of Cell Function.
W. Droge (2002)
Physiol Rev 82, 47-95
   Abstract »    Full Text »    PDF »
Adjacent cysteine residues as a redox switch.
C. Park and R. T. Raines (2001)
Protein Eng. Des. Sel. 14, 939-942
   Abstract »    Full Text »    PDF »
Regulation of the Yeast Yap1p Nuclear Export Signal Is Mediated by Redox Signal-Induced Reversible Disulfide Bond Formation.
S. Kuge, M. Arita, A. Murayama, K. Maeta, S. Izawa, Y. Inoue, and A. Nomoto (2001)
Mol. Cell. Biol. 21, 6139-6150
   Abstract »    Full Text »    PDF »
Complex Regulation of the Organic Hydroperoxide Resistance Gene (ohr) from Xanthomonas Involves OhrR, a Novel Organic Peroxide-Inducible Negative Regulator, and Posttranscriptional Modifications.
R. Sukchawalit, S. Loprasert, S. Atichartpongkul, and S. Mongkolsuk (2001)
J. Bacteriol. 183, 4405-4412
   Abstract »    Full Text »    PDF »
DNA Microarray-Mediated Transcriptional Profiling of the Escherichia coli Response to Hydrogen Peroxide.
M. Zheng, X. Wang, L. J. Templeton, D. R. Smulski, R. A. LaRossa, and G. Storz (2001)
J. Bacteriol. 183, 4562-4570
   Abstract »    Full Text »    PDF »
Computation-Directed Identification of OxyR DNA Binding Sites in Escherichia coli.
M. Zheng, X. Wang, B. Doan, K. A. Lewis, T. D. Schneider, and G. Storz (2001)
J. Bacteriol. 183, 4571-4579
   Abstract »    Full Text »    PDF »


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