MassIVE MSV000094842

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Quantitative phosphoproteomic analysis of Streptococcus pneumoniae reveals that competence modulates protein phosphorylation

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Description

Extensive phosphoproteomic studies have revealed that protein phosphorylation on serine, threonine and tyrosine residues is a widespread regulatory post-translational modification in bacteria. In this study, we carried out a biological triplicate of quantitative proteomic and phosphoproteomic analyses on the pathogenic bacterium Streptococcus pneumoniae in the non-competent and the competent states. Competence is a developmental genetic program triggered by a signaling pathway that is key for natural genetic transformation and consequently bacterial horizontal gene transfer. We used dimethyl-tag labeling for the calculation of peptide abundance ratios between non-competent and competent samples, Titanium dioxide (TiO2) beads for phosphopeptide enrichment and LC-MS/MS determination. Our proteome covers 62.7% of the total protein content of the bacteria with 75 proteins having different abundance ratios, including proteins not previously described to be involved in competence. 103 phosphopeptides were identified including 48 having different abundance ratios. Notably, the proteins with a change in phosphorylation in competent cells are different from the proteins with a change in expression, highlighting different pathways induced by competence and regulated by phosphorylation. This is the first report that phosphorylation of some proteins is regulated during competence in Streptococcus pneumoniae, a key pathway for the bacteria to evade vaccines or acquire antibiotic resistance. [doi:10.25345/C5MG7G67F] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Streptococcus pneumoniae ; competence ; phosphorylation ; protein kinase ; phosphoproteomic

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Principal Investigators:
(in alphabetical order) 		Christophe Grangeasse, MMSB-UMR5086-CNRS, France
Submitting User: Adeline
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