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Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

Authors
Woo, HA; Jeong, W; Chang, TS; Park, KJ; Park, SJ; Yang, JS; Rhee, SG
Citation
The Journal of biological chemistry, 280(5):3125-3128, 2005
Journal Title
The Journal of biological chemistry
ISSN
0021-92581083-351X
Abstract
Cysteine residues of certain peroxiredoxins (Prxs) undergo reversible oxidation to sulfinic acid (Cys-SO2H) and the reduction reaction is catalyzed by sulfiredoxin (Srx). Specific Cys residues of various other proteins are also oxidized to sulfinic acid, suggesting that formation of Cys-SO2H might be a novel posttranslational modification that contributes to regulation of protein function. To examine the susceptibility of sulfinic forms of proteins to reduction by Srx, we prepared such forms of all six mammalian Prx isoforms and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH. Furthermore, Srx bound specifically to the four 2-Cys Prxs in vitro and in cells. Sulfinic forms of Prx I and Prx II, but not of Prx VI or GAPDH, present in H2O2-treated A549 cells were gradually reduced after removal of H2O2; overexpression of Srx increased the rate of the reduction of Prx I and Prx II but did not induce that of Prx VI or GAPDH. These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage.
MeSH terms
AnimalsCysteine/analogs & derivatives*Cysteine/metabolism*Gene Expression Regulation, EnzymologicGlyceraldehyde-3-Phosphate Dehydrogenases/metabolismHumansIsoenzymes/geneticsIsoenzymes/metabolism*Oxidation-ReductionOxidoreductases/metabolism*Oxidoreductases Acting on Sulfur Group DonorsPeroxidases/geneticsPeroxidases/metabolism*Peroxiredoxin VIPeroxiredoxinsProtein Processing, Post-Translational/physiologyRatsSaccharomyces cerevisiae ProteinsSubstrate Specificity
DOI
10.1074/jbc.C400496200
PMID
15590625
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pulmonary & Critical Care Medicine
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박, 광주
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