Journal
PROTEOMICS
Volume 11, Issue 8, Pages 1449-1461Publisher
WILEY-BLACKWELL
DOI: 10.1002/pmic.201000649
Keywords
Helicobacter pylori; Membrane; Microbiology; Phosphoproteome; Tyrosine phosphorylation
Funding
- Chang-Jiang Scholars Program
- National Natural Science Foundation of China [20871057, 20801061]
- Guangdong Natural Science Foundation [8451027501001233]
- Talents Start-up Foundation of Jinan University [JNU 51208047]
- SRF for ROCS, SEM
- Fundamental Research Funds for the Central Universities
Ask authors/readers for more resources
Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr) and tyrosine (Tyr) residues is a major regulatory post-translational modification in the bacteria. To reveal the phosphorylation state in the Gram-negative pathogenic bacterium Helicobacter pylori, we carried out a global and site-specific phosphoproteomic analysis based on TiO(2)-phosphopeptide enrichment and high-accuracy LC-MS/MS determination. Eighty-two phosphopeptides from 67 proteins were identified with 126 phosphorylation sites, among which 79 class I sites were determined to have a distribution of 42.8:38.7:18.5% for the Ser/Thr/Tyr phosphorylation, respectively. The H. pylori phosphoproteome is characterized by comparably big size, high ratio of Tyr phosphorylation, high abundance of multiple phosphorylation sites in individual phosphopeptides and over-representation of membrane proteins. An interaction network covering 28 phosphoproteins was constructed with a total of 163 proteins centering on the major H. pylori virulence factor VacA, indicating that protein phosphorylation in H. pylori may be delicately controlled to regulate many aspects of the metabolic pathways and bacterial virulence.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available