Structural Mapping of Protein Interactions Reveals Differences in Evolutionary Pressures Correlated to MRNA Level and Protein Abundance

Overview

Journal Structure

Publisher Cell Press

Specialties Biochemistry
Biotechnology
Cell Biology
Molecular Biology

Date 2007 Nov 14

PMID 17997970

Citations 12

Authors

Matt Eames

Tanja Kortemme

Affiliations

Soon will be listed here.

Abstract

Genome-wide studies in Saccharomyces cerevisiae concluded that the dominant determinant of protein evolutionary rates is expression level: highly expressed proteins generally evolve most slowly. To determine how this constraint affects the evolution of protein interactions, we directly measure evolutionary rates of protein interface, surface, and core residues by structurally mapping domain interactions to yeast genomes. We find that mRNA level and protein abundance, though correlated, report on pressures affecting regions of proteins differently. Pressures proportional to mRNA level slow evolutionary rates of all structural regions and reduce the variability in rate differences between interfaces and other surfaces. In contrast, the evolutionary rate variation within a domain is much less correlated to protein abundance. Distinct pressures may be associated primarily with the cost (mRNA level) and functional (protein abundance) benefit of protein production. Interfaces of proteins with low mRNA levels may have higher evolutionary flexibility and could constitute the raw material for new functions.

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