Chasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase Trap.

ABSTRACT: Arginine phosphorylation is an emerging post-translational protein modification implicated in the bacterial stress response. Although early reports suggested that arginine phosphorylation also occurs in higher eukaryotes, its overall prevalence was never studied using modern mass spectrometry methods, owing to technical difficulties arising from the acid lability of phosphoarginine. As shown recently, the McsB and YwlE proteins from Bacillus subtilis function as a highly specific protein arginine kinase and phosphatase couple, shaping the phosphoarginine proteome. Using a B. subtilis ΔywlE strain as a source for arginine-phosphorylated proteins, we were able to adapt mass spectrometry (MS) protocols to the special chemical properties of the arginine modification. Despite this progress, the

SUBMITTER: Trentini DB 

PROVIDER: S-EPMC4125729 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature