Journal
SCIENCE
Volume 306, Issue 5701, Pages 1553-1554Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1100522
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- NHGRI NIH HHS [P41-HG00739] Funding Source: Medline
- NIGMS NIH HHS [GM068465] Funding Source: Medline
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Relatively little is known about the importance of amino acid interactions in protein and phenotypic evolution. Here we examine whether mutations that are pathogenic in Drosophila melanogaster become fixed via epistasis in other Dipteran genomes. Overall divergence at pathogenic amino acid sites is reduced. However, similar to10% of the substitutions at these sites carry the exact same pathogenic amino acid found in D. melanogaster mutants. Hence compensatory mutation(s) must have evolved. Surprisingly, the fraction 10% is not affected by phylogenetic distance. These results support a selection-driven process that allows compensated amino acid substitutions to become rapidly fixed in taxa with large populations.
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