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 and yeast orthologous proteins. 3) Selection should be stronger against mutations that create tyrosine versus remove tyrosine. We tested this prediction using human population genomic variation data. We found that all three predicted effects are modest for tyrosine when compared with the other amino acids, suggesting that selection against deleterious phosphorylation was not dominant in driving metazoan tyrosine loss.
journal_name
Mol Biol Evoljournal_title
Molecular biology and evolutionauthors
Pandya S,Struck TJ,Mannakee BK,Paniscus M,Gutenkunst RNdoi
10.1093/molbev/msu284subject
Has Abstractpub_date
2015-01-01 00:00:00pages
144-52issue
1eissn
0737-4038issn
1537-1719pii
msu284journal_volume
32pub_type
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