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• W1989261134 endingPage "12364" @default.
• W1989261134 startingPage "12356" @default.
• W1989261134 abstract "We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the l-arabinose-binding protein AraF. This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-linked homodimer under oxidative stress conditions, preventing l-arabinose binding. DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties. Thus, our results reveal a new link between oxidative protein folding and the defense mechanisms against oxidative stress. We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the l-arabinose-binding protein AraF. This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-linked homodimer under oxidative stress conditions, preventing l-arabinose binding. DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties. Thus, our results reveal a new link between oxidative protein folding and the defense mechanisms against oxidative stress." @default.
• W1989261134 created "2016-06-24" @default.
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• W1989261134 date "2014-05-01" @default.
• W1989261134 modified "2023-10-15" @default.
• W1989261134 title "A New Role for Escherichia coli DsbC Protein in Protection against Oxidative Stress" @default.
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• W1989261134 doi "https://doi.org/10.1074/jbc.m114.554055" @default.
• W1989261134 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4007432" @default.
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