Skip to Main content Skip to Navigation
Journal articles

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.
Document type :
Journal articles
Complete list of metadata

Cited literature [35 references]  Display  Hide  Download

https://hal.univ-lorraine.fr/hal-01452720
Contributor : Imopa Ul <>
Submitted on : Friday, January 12, 2018 - 1:16:55 PM
Last modification on : Tuesday, October 13, 2020 - 10:46:37 AM
Long-term archiving on: : Monday, May 7, 2018 - 6:54:08 AM

File

Denoncin et al. - 2014 - A New...
Publisher files allowed on an open archive

Identifiers

Collections

Citation

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, American Society for Biochemistry and Molecular Biology, 2014, 289 (18), pp.12356-12364. ⟨10.1074/jbc.M114.554055⟩. ⟨hal-01452720⟩

Share

Metrics

Record views

188

Files downloads

174