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Protein lysine acetylation in bacteria: Current state of the art
Author(s) -
Ouidir Tassadit,
Kentache Takfarinas,
Hardouin Julie
Publication year - 2016
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201500258
Subject(s) - lysine , acetylation , proteomics , bacteria , biology , adaptation (eye) , computational biology , posttranslational modification , biochemistry , genetics , amino acid , enzyme , gene , neuroscience
Post‐translational modifications of proteins are key events in cellular metabolism and physiology regulation. Lysine acetylation is one of the best studied protein modifications in eukaryotes, but, until recently, ignored in bacteria. However, proteomic advances have highlighted the diversity of bacterial lysine‐acetylated proteins. The current data support the implication of lysine acetylation in various metabolic pathways, adaptation and virulence. In this review, we present a broad overview of the current knowledge of lysine acetylation in bacteria. We emphasize particularly the significant contribution of proteomics in this field.