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Proteomics. 2016 Jan;16(2):301-9. doi: 10.1002/pmic.201500258. Epub 2015 Dec 14.

Protein lysine acetylation in bacteria: Current state of the art.

Ouidir T1,2,3, Kentache T1,2,3, Hardouin J1,2,3.

Author information

1
CNRS, UMR 6270, Polymères, Biopolymères, Surfaces Laboratory, Mont-Saint-Aignan, France.
2
Normandie University, UR, France.
3
PISSARO proteomic facility, IRIB, Mont-Saint-Aignan, France.

Abstract

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.

KEYWORDS:

Bacteria; Lysine acetylation; Microbiology

PMID:
26390373
DOI:
10.1002/pmic.201500258
[Indexed for MEDLINE]

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