Testing whether metazoan tyrosine loss was driven by selection against promiscuous phosphorylation.

ABSTRACT: Protein tyrosine phosphorylation is a key regulatory modification in metazoans, and the corresponding kinase enzymes have diversified dramatically. This diversification is correlated with a genome-wide reduction in protein tyrosine content, and it was recently suggested that this reduction was driven by selection to avoid promiscuous phosphorylation that might be deleterious. We tested three predictions of this intriguing hypothesis. 1) Selection should be stronger on residues that are more likely to be phosphorylated due to local solvent accessibility or structural disorder. 2) Selection should be stronger on proteins that are more likely to be promiscuously phosphorylated because they are abundant. We tested these predictions by comparing distributions of tyrosine within and among human

SUBMITTER: Pandya S 

PROVIDER: S-EPMC4271526 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature