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Recently, it was demonstrated that purified OxyR has one intramolecular disulfide bond, which led to the proposal that the reversible disulfide bond formation regulates the activity of OxyR as a transcription factor in response to peroxide stress. In this study, I demonstrated by SDS\u2010PAGE under non\u2010reducing conditions that an intramolecular disulfide bond is formed in OxyR upon exposure of the cells to hydrogen peroxide in vivo. Experiments using strains expressing mutant OxyR proteins with Cys to Ser single amino acid substitutions confirmed that the disulfide bond is formed between the Cys\u2010199 and \u2010208. Kinetic analyses indicated that the formation of the disulfide bond is rapid and transient, oxidized within 30 s and re\u2010reduced within 5 min after the addition of hydrogen peroxide in the wild\u2010type strain. These results provide evidence for the regulatory role of the reversible oxidation of dithiol to disulfide in sensing peroxide stress in vivo and signal transduction to the transcription apparatus by OxyR.<\/jats:p>","DOI":"10.1016\/s0014-5793(99)01013-3","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T17:52:28Z","timestamp":1027619548000},"page":"90-92","source":"Crossref","is-referenced-by-count":43,"title":["In vivo oxidation\u2010reduction kinetics of OxyR, the transcriptional activator for an oxidative stress\u2010inducible regulon in <i>Escherichia coli<\/i>"],"prefix":"10.1002","volume":"457","author":[{"given":"Kazuyuki","family":"Tao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[1999,8,30]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"crossref","unstructured":"Hidalgo E. and Demple B. 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