Methionine oxidation under anaerobic conditions in Escherichia coli.

ABSTRACT: Repairing oxidative-targeted macromolecules is a central mechanism necessary for living organisms to adapt to oxidative stress. Reactive oxygen and chlorine species preferentially oxidize sulfur-containing amino acids in proteins. Among these amino acids, methionine can be converted into methionine sulfoxide. This post-translational oxidation can be reversed by methionine sulfoxide reductases, Msr enzymes. In Gram-negative bacteria, the antioxidant MsrPQ system is involved in the repair of periplasmic oxidized proteins. Surprisingly, in this study, we observed in Escherichia coli that msrPQ was highly expressed in the absence of oxygen. We have demonstrated that the anaerobic induction of msrPQ was due to chlorate (ClO₃ ^- ) contamination of the Casamino Acids. Molecul

SUBMITTER: Loiseau L 

PROVIDER: S-EPMC9805139 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature