Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1)

Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins that are known as thioredoxin peroxidases. Here we report that Prx1 proteins from Tetraodon nigroviridis and humans also possess a previously unknown catalase-like activity that is independent of Cys residues and reductants but de...

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Published inThe Journal of biological chemistry Vol. 290; no. 32; pp. 19942 - 19955
Main Authors Sun, Cen-Cen, Dong, Wei-Ren, Zhao, Jing, Nie, Li, Xiang, Li-Xin, Zhu, Guan, Shao, Jian-Zhong
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 07.08.2015
American Society for Biochemistry and Molecular Biology
Subjects
catalase
Enzymology
hydrogen peroxide
peroxidase
peroxiredoxin
signaling
peroxiredoxin
signaling
peroxidase
catalase
hydrogen peroxide
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Summary:Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins that are known as thioredoxin peroxidases. Here we report that Prx1 proteins from Tetraodon nigroviridis and humans also possess a previously unknown catalase-like activity that is independent of Cys residues and reductants but dependent on iron. We identified that the GVL motif was essential to the catalase (CAT)-like activity of Prx1 but not to the Cys-dependent thioredoxin peroxidase (POX) activity, and we generated mutants lacking POX and/or CAT activities for individually delineating their functional features. We discovered that the TnPrx1 POX and CAT activities possessed different kinetic features in reducing H2O2. The overexpression of wild-type TnPrx1 and mutants differentially regulated the intracellular levels of reactive oxygen species and p38 phosphorylation in HEK-293T cells treated with H2O2. These observations suggest that the dual antioxidant activities of Prx1 may be crucial for organisms to mediate intracellular redox homeostasis. Background: Peroxiredoxin (Prx) was previously known only as a Cys-dependent thioredoxin. Results: Cys-independent catalase-like activity was observed in two vertebrate Prx1 proteins. Conclusion: Prx1 possesses dual antioxidant activities with varied affinities toward H2O2. Significance: This discovery extends our knowledge on Prx1 and provides new opportunities to further study the biological roles of this family of antioxidants.
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Both authors contributed equally to this work.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M115.659011