Abstract:
:Since the modern evolutionary synthesis was first proposed early in the twentieth century, attention has focused on assessing the relative contribution of mutation versus natural selection on protein evolution. Here we test a model that yields general quantitative predictions on rates of protein evolution by combining principles of individual energetics with Kimura's neutral theory. The model successfully predicts much of the heterogeneity in rates of protein evolution for diverse eukaryotes (i.e. fishes, amphibians, reptiles, birds, mammals) from different thermal environments. Data also show that the ratio of non-synonymous to synonymous nucleotide substitution is independent of body size, and thus presumably of effective population size. These findings indicate that rates of protein evolution are largely controlled by mutation rates, which in turn are strongly influenced by individual metabolic rate.
journal_name
Biol Lettjournal_title
Biology lettersauthors
Gillooly JF,McCoy MW,Allen APdoi
10.1098/rsbl.2007.0403subject
Has Abstractpub_date
2007-12-22 00:00:00pages
655-9issue
6eissn
1744-9561issn
1744-957Xpii
Q7283GJ033VM1051journal_volume
3pub_type
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