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Nat Rev Microbiol. 2017 Jul;15(7):385-396. doi: 10.1038/nrmicro.2017.26. Epub 2017 Apr 19.

Oxidative stress, protein damage and repair in bacteria.

Author information

1
Aix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne, UMR 7283, Institut de Microbiologie de la Méditerranée, 31 Chemin Joseph Aiguier, 13009 Marseille, France.
2
WELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium.
3
de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
4
Brussels Center for Redox Biology, Avenue Hippocrate 75, 1200 Brussels, Belgium.

Abstract

Oxidative damage can have a devastating effect on the structure and activity of proteins, and may even lead to cell death. The sulfur-containing amino acids cysteine and methionine are particularly susceptible to reactive oxygen species (ROS) and reactive chlorine species (RCS), which can damage proteins. In this Review, we discuss our current understanding of the reducing systems that enable bacteria to repair oxidatively damaged cysteine and methionine residues in the cytoplasm and in the bacterial cell envelope. We highlight the importance of these repair systems in bacterial physiology and virulence, and we discuss several examples of proteins that become activated by oxidation and help bacteria to respond to oxidative stress.

PMID:
28420885
DOI:
10.1038/nrmicro.2017.26
[Indexed for MEDLINE]

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