期刊
MOLECULAR BIOLOGY AND EVOLUTION
卷 24, 期 4, 页码 1005-1011出版社
OXFORD UNIV PRESS
DOI: 10.1093/molbev/msm019
关键词
evolutionary rate; protein structure; fitness density; functional density; solvent accessibility; disordered
Translational selection, including gene expression, protein abundance, and codon usage bias, has been suggested as the single dominant determinant of protein evolutionary rate in yeast. Here, we show that protein structure is also an important determinant. Buried residues, which are responsible for maintaining protein structure or are located on a stable interaction surface between 2 subunits, are usually under stronger evolutionary constraints than solvent-exposed residues. Our partial correlation analysis shows that, when whole proteins are included, the variance of evolutionary rate explained by the proportion of solvent-exposed residues (P-exposed) can reach two-thirds of that explained by translational selection, indicating that P-exposed is the most important determinant of protein evolutionary rate next only to translational selection. Our result suggests that proteins with many residues under selective constraint (e.g., maintaining structure or intermolecular interaction) tend to evolve slowly, supporting the fitness (functional) density hypothesis.
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