Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae.
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.
Sun
Xuesong
X
Institute of Life and Health Engineering and National Engineering Research Center for Genetic Medicine, Jinan University, Guangzhou 510632, China.
Ge
Feng
F
Xiao
Chuan-Le
CL
Yin
Xing-Feng
XF
Ge
Ruiguang
R
Zhang
Liu-Hui
LH
He
Qing-Yu
QY
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
D001426:Bacterial Proteins; D010750:Phosphoproteins; D020543:Proteome; D011494:Protein Kinases