Parallel evolution of chimeric fusion genes

Proc Natl Acad Sci U S A. 2005 Aug 9;102(32):11373-8. doi: 10.1073/pnas.0503528102. Epub 2005 Aug 2.

Abstract

To understand how novel functions arise, we must identify common patterns and mechanisms shaping the evolution of new genes. Here, we take advantage of data from three Drosophila genes, jingwei, Adh-Finnegan, and Adh-Twain, to find evolutionary patterns and mechanisms governing the evolution of new genes. All three of these genes are independently derived from Adh, which enabled us to use the extensive literature on Adh in Drosophila to guide our analyses. We discovered a fundamental similarity in the temporal, spatial, and types of amino acid changes that occurred. All three genes underwent rapid adaptive amino acid evolution shortly after they were formed, followed by later quiescence and functional constraint. These genes also show striking parallels in which amino acids change in the Adh region. We showed that these early changes tend to occur at amino acid residues that seldom, if ever, evolve in Drosophila Adh. Changes at these slowly evolving sites are usually associated with loss of function or hypomorphic mutations in Drosophila melanogaster. Our data indicate that shifting away from ancestral functions may be a critical step early in the evolution of chimeric fusion genes. We suggest that the patterns we observed are both general and predictive.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adaptation, Biological / genetics*
  • Alcohol Dehydrogenase
  • Alcohol Oxidoreductases / genetics*
  • Animals
  • Computational Biology
  • Drosophila
  • Drosophila Proteins / genetics*
  • Evolution, Molecular*
  • Likelihood Functions
  • Models, Genetic*
  • Phylogeny*
  • Species Specificity

Substances

  • Drosophila Proteins
  • Alcohol Oxidoreductases
  • ADH protein, Drosophila
  • Alcohol Dehydrogenase