Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance.

ABSTRACT:

Background

Phosphorylation of amino acid residues on proteins is an important and common post-translational modification in both eukaryotes and prokaryotes. Most research work has been focused on phosphorylation of serine, threonine or tyrosine residues, whereas phosphorylation of other amino acids are significantly less clear due to the controversy on their stability under standard bioanalytical conditions.

Results

Here we applied a shotgun strategy to analyze the histidine and aspartate phosphorylations in different microbes. Our results collectively indicate that histidine and aspartate phosphorylations frequently occur also in proteins that are not part of the two-component systems. Noticeably, a number of the modified proteins are pathogenesis-related or essential for s

SUBMITTER: Lai SJ 

PROVIDER: S-EPMC5445275 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature