Journal article
The Global Acetylome of the Human Pathogen Vibrio cholerae V52 Reveals Lysine Acetylation of Major Transcriptional Regulators
Department of Biotechnology and Biomedicine, Technical University of Denmark1
Research Groups, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark2
Bacterial Signal Transduction, Research Groups, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark3
Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark4
Department of Chemical and Biochemical Engineering, Technical University of Denmark5
Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark6
Karolinska Institutet7
Umeå University8
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. 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 3,402 acetylation sites on 1,240 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, and PhoB involved in direct regulation of virulence in V. cholerae were acetylated.
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.
Language: | English |
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Publisher: | Frontiers Media S.A. |
Year: | 2018 |
Pages: | 537 |
ISSN: | 22352988 |
Types: | Journal article |
DOI: | 10.3389/fcimb.2017.00537 |
ORCIDs: | Jers, Carsten , Sultan, Abida and Mijakovic, Ivan |
Acetylome Bacteria Lysine acetylation Mass spectrometry Pathogen Proteomics Vibrio cholerae Virulence
Acetylation Bacterial Proteins Computational Biology Gene Expression Regulation, Bacterial Humans Microbiology Models, Molecular Molecular Sequence Annotation Protein Conformation Protein Processing, Post-Translational Proteome QR1-502 Transcription, Genetic Virulence Factors acetylome bacteria lysine acetylation mass spectrometry pathogen proteomics virulence