Global Analysis of the Serine, Threonine and Tyrosine Phosphorylation Networks in the Model Bacterium Bacillus subtilis

Abstract

Cells constantly have to respond to environmental cues in their natural environment. These responses are mediated by covalent modifications on proteins. Reversible protein phosphorylation on proteins is known to govern discrete functions in a cell.By applying quantitative phosphoproteomics workflow based on SILAC labeling and high accuracy mass spectrometry, the aim was to define potential substrates of B. subtilis STY kinases and phosphatases and understand the global impact of phosphorylation events during growth.