Hannes Luz1, Martin Vingron. 1. Max Planck Institute for Molecular Genetics Ihnestrasse 73, 14195 Berlin, Germany. luz@molgen.mpg.de
Abstract
MOTIVATION: Amino acid changing mutations in proteins are contstrained by purifying selection and accumulate at different rates. We estimate evolutionary rates on multiple alignments of eukaryotic protein families in a maximum likelihood framework and spot sets of slow and fast evolving proteins. RESULTS: We find that the evolution of indispensable proteins is constrained by selection and that protein secretion is coupled to an increased evolutionary rate.
MOTIVATION: Amino acid changing mutations in proteins are contstrained by purifying selection and accumulate at different rates. We estimate evolutionary rates on multiple alignments of eukaryotic protein families in a maximum likelihood framework and spot sets of slow and fast evolving proteins. RESULTS: We find that the evolution of indispensable proteins is constrained by selection and that protein secretion is coupled to an increased evolutionary rate.
Authors: Matthew N Benedict; James R Henriksen; William W Metcalf; Rachel J Whitaker; Nathan D Price Journal: BMC Genomics Date: 2014-01-03 Impact factor: 3.969
Authors: David Alvarez-Ponce; Beatriz Sabater-Muñoz; Christina Toft; Mario X Ruiz-González; Mario A Fares Journal: Genome Biol Evol Date: 2016-09-26 Impact factor: 3.416