Evolutionary and structural analyses uncover a role for solvent interactions in the diversification of cocoonases in butterflies.

ABSTRACT: Multi-omic approaches promise to supply the power to detect genes underlying disease and fitness-related phenotypes. Optimal use of the resulting profusion of data requires detailed investigation of individual candidate genes, a challenging proposition. Here, we combine transcriptomic and genomic data with molecular modelling of candidate enzymes to characterize the evolutionary history and function of the serine protease cocoonase. Heliconius butterflies possess the unique ability to feed on pollen; recent work has identified cocoonase as a candidate gene in pollen digestion. Cocoonase was first described in moths, where it aids in eclosure from the cocoon and is present as a single copy gene. In heliconiine butterflies it is duplicated and highly expressed in the mou

SUBMITTER: Smith G 

PROVIDER: S-EPMC5784194 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature