| Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity. | |
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MedLine Citation:
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PMID: 18725414 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The thiol (-SH) of the active cysteine residue in peroxiredoxin (Prx) is known to be reversibly hyperoxidized to cysteine sulfinic acid (-SO(2)H), 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 (-SO(3)H) yeast Prx (Tsa1p) active-site peptide (AFTFVCPTEI), we observed an increase in the immunoblot intensity in proportion to the H(2)O(2) 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(3)H) by mass spectrometry. Tsa1p-SO(3)H was not an autoxidation product of Tsa1p-SO(2)H and was maintained in yeast cells even after two doubling cycles. Tsa1p-SO(3)H self-assembled into a ring-shaped multimeric form was shown by electron microscopy. Although the Tsa1p-SO(3)H multimer lost its peroxidase activity, it gained approximately 4-fold higher chaperone activity compared with Tsa1p-SH. In this study, we identify an irreversibly hyperoxidized Prx, Tsa1p-SO(3)H, with enhanced molecular chaperone activity and suggest that Tsa1p-SO(3)H is a marker of cumulative oxidative stress in cells. |
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Authors:
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Jung Chae Lim; Hoon-In Choi; Yu Sun Park; Hyung Wook Nam; Hyun Ae Woo; Ki-Sun Kwon; Yu Sam Kim; Sue Goo Rhee; Kanghwa Kim; Ho Zoon Chae |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-08-25 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 283 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2008 Oct |
Date Detail:
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Created Date: 2008-10-20 Completed Date: 2008-12-11 Revised Date: 2010-09-21 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 28873-80 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, Chonnam National University, Gwangju 500-757, Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Catalytic Domain* Cysteine / analogs & derivatives*, chemistry* Electrophoresis, Gel, Two-Dimensional Gene Expression Regulation, Fungal* Hydrogen Peroxide / chemistry Microscopy, Electron Models, Biological Molecular Chaperones / chemistry* Oxidation-Reduction Oxidative Stress Oxygen / chemistry* Peroxidases / chemistry, physiology* Peroxiredoxins / chemistry, genetics* Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / chemistry, physiology* |
| Chemical | |
Reg. No./Substance:
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0/Molecular Chaperones; 0/Saccharomyces cerevisiae Proteins; 2381-08-0/cysteine sulfinic acid; 52-90-4/Cysteine; 7722-84-1/Hydrogen Peroxide; 7782-44-7/Oxygen; EC 1.11.1.-/Peroxidases; EC 1.11.1.-/Tsa1 protein, S cerevisiae; EC 1.11.1.15/Peroxiredoxins |
| Comments/Corrections | |
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