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A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.

ABSTRACT: Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI). In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation. We also found that PDI can inhibit this reaction by exerting its reductase and chaperone activities. This discovery discloses an off-pathway reaction in the Prx4-mediated oxidative protein folding and the quality control role of PDI.

SUBMITTER: Zhu L

PROVIDER: S-EPMC4138195 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.

Zhu Li L Yang Kai K Wang Xi'e X Wang Xi X Wang Chih-chen CC

PloS one 20140819 8

Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI). In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation. We also found that PDI can inhibit this reaction by ...[more]

PMID: 25137134

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