Evolutionary constraints of phosphorylation in eukaryotes, prokaryotes, and mitochondria.

ABSTRACT: High accuracy mass spectrometry has proven to be a powerful technology for the large scale identification of serine/threonine/tyrosine phosphorylation in the living cell. However, despite many described phosphoproteomes, there has been no comparative study of the extent of phosphorylation and its evolutionary conservation in all domains of life. Here we analyze the results of phosphoproteomics studies performed with the same technology in a diverse set of organisms. For the most ancient organisms, the prokaryotes, only a few hundred proteins have been found to be phosphorylated. Applying the same technology to eukaryotic species resulted in the detection of thousands of phosphorylation events. Evolutionary analysis shows that prokaryotic phosphoproteins are preferentially conserved in all

SUBMITTER: Gnad F 

PROVIDER: S-EPMC3101853 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature