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Journal Articles Journal of Biological Chemistry Year : 2014

A New Role for Escherichia coli DsbC Protein in Protection against Oxidative Stress

Abstract

Background: DsbC is a protein-disulfide isomerase present in the periplasm of Gram-negative bacteria. Results: We discovered that DsbC also regulates the redox state of the single cysteine residue of the l-arabinose-binding protein AraF. Conclusion: DsbC is involved in the protection of single cysteine residues against oxidative stress. Significance: This finding reveals a new link between oxidative stress protection and oxidative protein folding. 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.
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Dates and versions

hal-01452720 , version 1 (12-01-2018)

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Katleen Denoncin, Didier Vertommen, Isabelle S. Arts, Camille V. Goemans, Sophie Rahuel-Clermont, et al.. A New Role for Escherichia coli DsbC Protein in Protection against Oxidative Stress. Journal of Biological Chemistry, 2014, 289 (18), pp.12356-12364. ⟨10.1074/jbc.M114.554055⟩. ⟨hal-01452720⟩
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