Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Sci. STKE, 5 November 2002
Vol. 2002, Issue 157, p. pe46
OxyR: A Molecular Code for Redox Sensing?
John D. Helmann*
Department of Microbiology, Cornell University, Ithaca, NY 14853-8101, USA.
Helmann discusses the controversy surrounding the activation of the bacterial redox-regulated transcription factor OxyR. Evidence from different sources, including crystallographic data, has led to opposing models for the chemical changes that activate OxyR. Is it an intramolecular disulfide-linkage? Is it oxidation of a single cysteine residue to a sulfenic acid? Are there different active forms depending on the type of cysteine modification: intramolecular disulfide bond, sulfenic acid, S-nitrosothiol, or mixed disulfide with glutathione? These issues are discussed in the broader context of transcriptional regulation and how particular regulators may activate distinct genetic programs depending on the precise state of the regulator produced in response to environmental cues.
*Contact information. E-mail: email@example.com
Citation: J. D. Helmann, OxyR: A Molecular Code for Redox Sensing? Sci. STKE2002, pe46 (2002).