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Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity

Title
Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity
Authors
Jung C.L.Choi H.-I.Yu S.P.Hyung W.N.Hyun A.W.Kwon K.-S.Yu S.K.Sue G.R.Kim K.Ho Z.C.T.
Ewha Authors
이서구
SCOPUS Author ID
이서구scopusscopus
Issue Date
2008
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 283, no. 43, pp. 28873 - 28880
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The thiol (-SH) of the active cysteine residue in peroxiredoxin (Prx) is known to be reversibly hyperoxidized to cysteine sulfinic acid (-SO 2H), which can be reduced back to thiol by sulfiredoxin/sestrin. However, hyperoxidized Prx of an irreversible nature has not been reported yet. Using an antibody developed against the sulfonylated (-SO3H) yeast Prx (Tsa1p) active-site peptide (AFTFVCPTEI), we observed an increase in the immunoblot intensity in proportion to the H2O2 concentrations administered to the yeast cells. We identified two species of hyperoxidized Tsa1p: one can be reduced back (reversible) with sulfiredoxin, and the other cannot (irreversible). Irreversibly hyperoxidized Tsa1p was identified as containing the active-site cysteine sulfonic acid (Tsa1p-SO 3H) by mass spectrometry. Tsa1p-SO3H was not an autoxidation product of Tsa1p-SO2H and was maintained in yeast cells even after two doubling cycles. Tsa1p-SO3H self-assembled into a ring-shaped multimeric form was shown by electron microscopy. Although the Tsa1p-SO3H multimer lost its peroxidase activity, it gained ∼4-fold higher chaperone activity compared with Tsa1p-SH. In this study, we identify an irreversibly hyperoxidized Prx, Tsa1p-SO3H, with enhanced molecular chaperone activity and suggest that Tsa1p-SO3H is a marker of cumulative oxidative stress in cells. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI
10.1074/jbc.M804087200
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일반대학원 > 생명·약학부 > Journal papers
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