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


ABSTRACT: 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.

SUBMITTER: Sun CC 

PROVIDER: S-EPMC4528153 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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

Sun Cen-Cen CC   Dong Wei-Ren WR   Zhao Jing J   Nie Li L   Xiang Li-Xin LX   Zhu Guan G   Shao Jian-Zhong JZ  

The Journal of biological chemistry 20150618 32


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  ...[more]

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