Epistasis among clustered lineage-specific adaptive amino acid substitutions in the Drosophila Trio protein.

ABSTRACT: Intramolecular epistasis is increasingly recognized as a key factor shaping patterns of evolutionary rate variation among protein sites and constraining adaptive evolution. While genome-wide analyses have revealed that intramolecular epistatic interactions can drive the spatial clustering of amino acid substitutions, direct empirical evidence for such interactions and their evolutionary consequences remains limited. Using a population genetic screen for spatially-clustered and lineage-specific adaptive amino acid substitutions in Drosophila proteins, we systematically identify experimentally tractable candidates for functional analysis. As proof of concept, we focus on the Trio protein, a Rho guanine nucleotide exchange factor that exhibits three spatially-clustered adaptive amino a

SUBMITTER: Borne F 

PROVIDER: S-EPMC12621854 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature