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

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dc.contributor.authorJ C Lim-
dc.contributor.authorH I Choi-
dc.contributor.authorY S Park-
dc.contributor.authorH W Nam-
dc.contributor.authorH A Woo-
dc.contributor.authorKi Sun Kwon-
dc.contributor.authorY S Kim-
dc.contributor.authorS G Rhee-
dc.contributor.authorK Kim-
dc.contributor.authorH Z Chae-
dc.date.accessioned2017-04-19T09:12:10Z-
dc.date.available2017-04-19T09:12:10Z-
dc.date.issued2008-
dc.identifier.issn0021-9258-
dc.identifier.uri10.1074/jbc.M804087200ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8703-
dc.description.abstractThe 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.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleIrreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity-
dc.title.alternativeIrreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number43-
dc.citation.endPage28880-
dc.citation.startPage28873-
dc.citation.volume283-
dc.contributor.affiliatedAuthorKi Sun Kwon-
dc.contributor.alternativeName임정채-
dc.contributor.alternativeName최훈인-
dc.contributor.alternativeName박유선-
dc.contributor.alternativeName남형욱-
dc.contributor.alternativeName우현애-
dc.contributor.alternativeName권기선-
dc.contributor.alternativeName김유삼-
dc.contributor.alternativeName이서구-
dc.contributor.alternativeName김광화-
dc.contributor.alternativeName채호준-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 283, no. 43, pp. 28873-28880-
dc.identifier.doi10.1074/jbc.M804087200-
dc.description.journalClassY-
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