The global acetylome of the human pathogen Vibrio cholerae V52 reveals lysine acetylation of major transcriptional regulators

ABSTRACT: Protein lysine acetylation is recognized as an important reversible post translational modification in all domains of life. While its primary roles appear to reside in metabolic processes, lysine acetylation has also been implicated in regulating pathogenesis in bacteria. By now, several global lysine acetylome analyses have been carried out in various bacteria, but thus far there have been no reports of lysine acetylation taking place in the important human pathogen Vibrio cholerae. In this study, we analyzed the lysine acetylproteome of the human pathogen V. cholerae V52. By applying a combination of immuno-enrichment of acetylated peptides and high resolution mass spectrometry, we identified 3402 acetylation sites on 1240 proteins. Of the acetylated proteins, more than half were acetylated on two or more sites. As reported for other bacteria, we observed that many of the acetylated proteins were involved in metabolic and cellular processes and there was an over-representation of acetylated proteins involved in protein synthesis. Of interest, we demonstrated that many global transcription factors such as CRP, H-NS, IHF, Lrp and RpoN as well as transcription factors AphB, TcpP, PhoB, and ToxR, involved in direct regulation of virulence in V. cholerae were acetylated. In addition VAS effector proteins involved in type VI secretion were acetylated. The overall level of acetylation increased during growth and was higher in stationary phase. In conclusion, this is the first global protein lysine acetylome analysis of V. cholerae and should constitute a valuable resource for in-depth studies of the impact of lysine acetylation in pathogenesis and other cellular processes.

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Vibrio Cholerae V52

DISEASE(S): Cholera

SUBMITTER: Vaishnavi Ravikumar  

LAB HEAD: Ivan Mijakovic

PROVIDER: PXD008055 | Pride | 2018-01-02

REPOSITORIES: Pride