title: Bacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicity.
abstract: Increasing evidence shows that protein phosphorylation on serine, threonine and tyrosine residues is a major regulatory post-translational modification in the bacteria. This review focuses on the implications of bacterial phosphoproteome in bacterial pathogenicity and highlights recent development of methods in phosphoproteomics and the connectivity of the phosphorylation networks. Recent technical developments in the high accuracy mass spectrometry have dramatically transformed proteomics and made it possible the characterization of a few exhaustive site-specific bacterial phosphoproteomes. The high abundance of tyrosine phosphorylations in a few bacterial phosphoproteomes suggests their roles in the pathogenicity, especially in the case of pathogen-host interactions; the high abundance of multi-phosphorylation sites in bacterial phosphoprotein is a compensation of the relatively small phosphorylation size and an indicator of the delicate regulation of protein functions.
authors.affiliation: Laboratory of Integrative Biosciences, College of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China. gerg@mail.sysu.edu.cn
authors.forename: Ruiguang
authors.initials: R
authors.lastname: Ge
authors.forename: Weiran
authors.initials: W
authors.lastname: Shan
mesh_terms: D001419:Bacteria / Q000378:metabolism* / Q000472:pathogenicity*; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D010750:Phosphoproteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D040901:Proteomics; D014443:Tyrosine / Q000032:analysis / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D010750:Phosphoproteins; D014443:Tyrosine