Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 이서구 | * |
dc.date.accessioned | 2016-12-06T02:12:19Z | - |
dc.date.available | 2016-12-06T02:12:19Z | - |
dc.date.issued | 2008 | * |
dc.identifier.issn | 0021-9258 | * |
dc.identifier.other | OAK-5138 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/232957 | - |
dc.description.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. | * |
dc.language | English | * |
dc.title | Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity | * |
dc.type | Article | * |
dc.relation.issue | 43 | * |
dc.relation.volume | 283 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 28873 | * |
dc.relation.lastpage | 28880 | * |
dc.relation.journaltitle | Journal of Biological Chemistry | * |
dc.identifier.doi | 10.1074/jbc.M804087200 | * |
dc.identifier.wosid | WOS:000260179900012 | * |
dc.identifier.scopusid | 2-s2.0-57649213405 | * |
dc.author.google | Jung C.L. | * |
dc.author.google | Choi H.-I. | * |
dc.author.google | Yu S.P. | * |
dc.author.google | Hyung W.N. | * |
dc.author.google | Hyun A.W. | * |
dc.author.google | Kwon K.-S. | * |
dc.author.google | Yu S.K. | * |
dc.author.google | Sue G.R. | * |
dc.author.google | Kim K. | * |
dc.author.google | Ho Z.C.T. | * |
dc.contributor.scopusid | 이서구(7401852092) | * |
dc.date.modifydate | 20240423081003 | * |