Genetics of octanol dehydrogenase in Drosophila metzii.

CTANOL dehydrogenase (ODH) was studied in Drosophila melanogaster first by URSPRUNG and LEONE (1965) and distinguished from alcohol dehydrogenase by COURTRIGHT, IMBERSKI, and URSPRUNG (1966). The neotropical species Drosophila metzii is polymorphic for complex octanol dehydrogenase patterns which will be shown to depend on two distinct structural genes, ODH,, apparently homologous with the locus studied by COURTRIGHT et al. (1966), and ODH,, responsible for a more slowly migrating isozyme. The ODH loci are unlinked, and variants display unifactorial inheritance. The ODH molecule is considered at least a dimer but probably a tetramer. Isozyme formation can involve combinations of polypeptides produced by either or both of the two structural genes. Genetic evidence will be presented indicating that egg or embryonic and imaginal ODH isozyme patterns depend on the same structural genes.