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Methionine oxidation in bacteria: A reversible post‐translational modification
Author(s) -
Vincent Maxence S.,
Ezraty Benjamin
Publication year - 2023
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.15000
Subject(s) - methionine , biology , biochemistry , bacteria , enzyme , protein function , residue (chemistry) , sulfur , antioxidant , amino acid , chemistry , genetics , gene , organic chemistry
Methionine is a sulfur‐containing residue found in most proteins which are particularly susceptible to oxidation. Although methionine oxidation causes protein damage, it can in some cases activate protein function. Enzymatic systems reducing oxidized methionine have evolved in most bacterial species and methionine oxidation proves to be a reversible post‐translational modification regulating protein activity. In this review, we inspect recent examples of methionine oxidation provoking protein loss and gain of function. We further speculate on the role of methionine oxidation as a multilayer endogenous antioxidant system and consider its potential consequences for bacterial virulence.