Proteomic profiling of lysine acetylation in Pseudomonas aeruginosa reveals the diversity of acetylated proteins
| Autor: | Thierry Jouenne, Tassadit Ouidir, Pascal Cosette, Julie Hardouin |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences 030306 microbiology Proteomic Profiling Pseudomonas aeruginosa Lysine Biology medicine.disease_cause Proteomics Biochemistry 03 medical and health sciences Metabolic pathway chemistry.chemical_compound Enzyme chemistry Biosynthesis Acetylation medicine Molecular Biology 030304 developmental biology |
| Zdroj: | PROTEOMICS. 15:2152-2157 |
| ISSN: | 1615-9853 |
| DOI: | 10.1002/pmic.201500056 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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