title: Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae.
abstract: Recent phosphoproteomic characterizations of Bacillus subtilis, Escherichia coli, Lactococcus lactis, Pseudomonas putida, and Pseudomonas aeruginosa have suggested that protein phosphorylation on serine, threonine, and tyrosine residues is a major regulatory post-translational modification in bacteria. In this study, we carried out a global and site-specific phosphoproteomic analysis on the Gram-positive pathogenic bacterium Streptococcus pneumoniae. One hundred and two unique phosphopeptides and 163 phosphorylation sites with distributions of 47%/44%/9% for Ser/Thr/Tyr phosphorylations from 84 S. pneumoniae proteins were identified through the combined use of TiO(2) enrichment and LC-MS/MS determination. The identified phosphoproteins were found to be involved in various biological processes including carbon/protein/nucleotide metabolisms, cell cycle and division regulation. A striking characteristic of S. pneumoniae phosphoproteome is the large number of multiple species-specific phosphorylated sites, indicating that high level of protein phosphorylation may play important roles in regulating many metabolic pathways and bacterial virulence.
authors.affiliation: Institute of Life and Health Engineering and National Engineering Research Center for Genetic Medicine, Jinan University, Guangzhou 510632, China.
authors.forename: Xuesong
authors.initials: X
authors.lastname: Sun
authors.forename: Feng
authors.initials: F
authors.lastname: Ge
authors.forename: Chuan-Le
authors.initials: CL
authors.lastname: Xiao
authors.forename: Xing-Feng
authors.initials: XF
authors.lastname: Yin
authors.forename: Ruiguang
authors.initials: R
authors.lastname: Ge
authors.forename: Liu-Hui
authors.initials: LH
authors.lastname: Zhang
authors.forename: Qing-Yu
authors.initials: QY
authors.lastname: He
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000378:metabolism; D001665:Binding Sites; D010750:Phosphoproteins / Q000032:analysis* / Q000378:metabolism; D010766:Phosphorylation; D025941:Protein Interaction Mapping; D011494:Protein Kinases / Q000378:metabolism; D020543:Proteome / Q000032:analysis* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D013045:Species Specificity; D013296:Streptococcus pneumoniae / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D010750:Phosphoproteins; D020543:Proteome; D011494:Protein Kinases