Journal
PROTEOMICS
Volume 15, Issue 13, Pages 2152-2157Publisher
WILEY
DOI: 10.1002/pmic.201500056
Keywords
Lysine acetylation; Mass spectrometry; Microbiology; Pseudomonas aeruginosa
Funding
- European Regional Development Fund (FEDER program) [33267]
- Haute-Normandie region
- France (Manche/Channel) England Interreg program
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Protein lysine acetylation is a reversible and highly regulated post-translational modification with the well demonstrated physiological relevance in eukaryotes. Recently, its important role in the regulation of metabolic processes in bacteria was highlighted. Here, we reported the lysine acetylproteome of Pseudomonas aeruginosa using a proteomic approach. We identified 430 unique peptides corresponding to 320 acetylated proteins. In addition to the proteins involved in various metabolic pathways, several enzymes contributing to the lipopolysaccharides biosynthesis were characterized as acetylated. This data set illustrated the abundance and the diversity of acetylated lysine proteins in P. aeruginosa and opens opportunities to explore the role of the acetylation in the bacterial physiology.
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