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Originally published In Press as doi:10.1074/jbc.M200559200 on March 6, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16853-16859, May 10, 2002
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Regulation of Protein S-Thiolation by Glutaredoxin 5 in the Yeast Saccharomyces cerevisiae*

Daniel Shenton, Gabriel PerroneDagger , Kathryn A. Quinn, Ian W. DawesDagger , and Chris M. Grant§

From the Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD, United Kingdom and the Dagger  School of Biochemistry and Molecular Genetics, University of New South Wales, Sydney, New South Wales 2052, Australia

The irreversible oxidation of cysteine residues can be prevented by protein S-thiolation, a process by which protein -SH groups form mixed disulfides with low molecular weight thiols such as glutathione. We report here that this protein modification is not a simple response to the cellular redox state, since different oxidants lead to different patterns of protein S-thiolation. SDS-polyacrylamide gel electrophoresis shows that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the major target for modification following treatment with hydroperoxides (hydrogen peroxide or tert-butylhydroperoxide), whereas this enzyme is unaffected following cellular exposure to the thiol oxidant diamide. Further evidence that protein S-thiolation is tightly regulated in response to oxidative stress is provided by the finding that the Tdh3 GAPDH isoenzyme, and not the Tdh2 isoenzyme, is S-thiolated following exposure to H2O2 in vivo, whereas both GAPDH isoenzymes are S-thiolated when H2O2 is added to cell-free extracts. This indicates that cellular factors are likely to be responsible for the difference in GAPDH S-thiolation observed in vivo rather than intrinsic structural differences between the GAPDH isoenzymes. To begin to search for factors that can regulate the S-thiolation process, we investigated the role of the glutaredoxin family of oxidoreductases. We provide the first evidence that protein dethiolation in vivo is regulated by a monothiol-glutaredoxin rather than the classical glutaredoxins, which contain two active site cysteine residues. In particular, glutaredoxin 5 is required for efficient dethiolation of the Tdh3 GAPDH isoenzyme.

* This work was supported by Biotechnology and Biological Sciences Research Council Grant 36/C13319.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Biomolecular Sciences, UMIST, PO Box 88, Manchester M60 1QD, UK. Tel.: 161-200-4192; Fax: 161-236-0409; E-mail: chris.grant@umist.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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