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Thiol-based Regulatory Switches.

M. Paget, M. Buttner
Published 2003 · Biology, Medicine

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Thiol-based regulatory switches play central roles in cellular responses to oxidative stress, nitrosative stress, and changes in the overall thiol-disulfide redox balance. Protein sulfhydryls offer a great deal of flexibility in the different types of modification they can undergo and the range of chemical signals they can perceive. For example, recent work on OhrR and OxyR has clearly established that disulfide bonds are not the only cysteine oxidation products that are likely to be relevant to redox sensing in vivo. Furthermore, different stresses can result in distinct modifications to the same protein; in OxyR it seems that distinct modifications can occur at the same cysteine, and in Yap1 a partner protein ensures that the disulfide bond induced by peroxide stress is different from the disulfide bond induced by other stresses. These kinds of discoveries have also led to the intriguing suggestion that different modifications to the same protein can create multiple activation states and thus deliver discrete regulatory outcomes. In this review, we highlight these issues, focusing on seven well-characterized microbial proteins controlled by thiol-based switches, each of which exhibits unique regulatory features.
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THIOL-BASED REGULATORY SWITCHES
Colin Kleanthous, and Stephen Spiro for helpful discussion and comments on the manuscript, and Hee-Jeon Hong and Tobias Kieser for help in preparing the diagrams
Acknowledgments We
EMBO J
J. Bacteriol
THIOL-BASED REGULATORY SWITCHES 121 Activation of the OxyR transcription factor by reversible disulfide bond formation



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