Spectral Library Based Analysis of Arginine Phosphorylations in Staphylococcus aureus.

ABSTRACT: Reversible protein phosphorylation is one of the major mechanisms in the regulation of protein expression and protein activity, controlling physiological functions of the important human pathogen Staphylococcus aureus Phosphorylations at serine, threonine and tyrosine are known to influence for example protein activity in central metabolic pathways and the more energy-rich phosphorylations at histidine, aspartate or cysteine can be found as part of two component system sensor domains or mediating bacterial virulence. In addition to these well-known phosphorylations, the phosphorylation at arginine residues plays an essential role. Hence, the deletion mutant S. aureus COL ΔptpB (protein tyrosine phosphatase B) was studied because the protein PtpB is assumed to be an arg

SUBMITTER: Junker S 

PROVIDER: S-EPMC5795395 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature