Origin and evolution of a new gene descended from alcohol dehydrogenase in Drosophila.
Drosophila alcohol dehydrogenase (Adh) is highly conserved in size, organization, and amino acid sequence. Adh-psi was hypothesized to be a pseudogene derived from an Adh duplication in the repleta group of Drosophila; however, several results from molecular analyses of this gene conflict with currently held notions of molecular evolution. Perhaps the most difficult observations to reconcile with the pseudogene hypothesis are that the hypothetical replacement sites of Adh-psi evolve only slightly more quickly than replacement sites of closely related, functional Adh genes, and that the replacement sites of the pseudogenes evolve considerably more slowly than neighboring silent sites. The data have been presented as a paradox that challenges our understanding of the mechanisms underlying DNA sequence divergence. Here I show that Adh-psi is actually a new, functional gene recently descended from an Adh duplication. This descendant recruited approximately 60 new N-terminal amino acids, is considerably more basic than ADH, and is evolving at a faster rate than Adh. Furthermore, though the descendant is clearly functional, as inferred from molecular evolution and population genetic data, it retains no obvious ADH activity. This probably reflects functional divergence from its Adh ancestor.
Begun
D J
DJ
Section of Evolution and Ecology, University of California, Davis 95616, USA. djbegun@mail.utexas.edu
D000426:Alcohol Dehydrogenase / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA; D004330:Drosophila / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D019143:Evolution, Molecular; D017344:Genes, Insect; D014644:Genetic Variation; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010802:Phylogeny
D004247:DNA; D000426:Alcohol Dehydrogenase