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Papers In Press, published online ahead of print March 6, 2002
Department of Biomolecular Sciences, UMIST, Manchester M60 1QD
Corresponding Author: chris.grant{at}umist.ac.uk
The irreversible oxidation of cysteine residues can be prevented by protein S-thiolation, a process by which protein -SH groups form mixed disulphides 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-butyl hydroperoxide), 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 hydrogen peroxide in vivo, whereas, both GAPDH isoenzymes are S-thiolated when hydrogen peroxide 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.
J. Biol. Chem, 10.1074/jbc.M200559200
Submitted on January 18, 2002
Revised on March 6, 2002
Accepted on March 6, 2002
Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae
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