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Molecular Analysis of Mutant and Wild Type Alcohol Dehydrogenase Alleles From Drosophila.

Wild type alcohol dehydrogenase polypeptides (ADH) from Drosophila melanogaster transformants were examined using western blots and polyclonal antiserum specific for Drosophila melanogaster ADH. These data indicate that ADH from Hawaiian drosophillds was similar in molecular weight to Drosophila melanogaster ADH, but that the isoelectric points of the Hawaiian electromorphs were distinct. Therefore it was evident that western blots could be used to characterize ADH from different species of Drosophila. Mutants Induced in Drosophila spermatozoa at the alcohol dehydrogenase (Adh) locus using X-rays, 1-ethyl-l-nitrosourea (ENU) or ethyl methanesulfonate (EMS) were characterized using genetic complementation tests, western blots, Southern blots, northern blots and enzymatic amplification of the Adh locus. Genetic complementation tests showed that 22/30 X-ray Induced mutants, and 3/13 ENU and EMS induced mutants were multi-locus deficiencies. Western blot analysis of the intragenic mutations showed that 4/7 X-ray induced mutants produced detectable polypeptides, one of which was normal in molecular weight and charge. In contrast 8/10 intragenic ENU and EMS Induced mutants produced normal polypeptides. Southern blot analysis showed that 5/7 intragenic X-ray induced mutants and all 10 of the intragenic ENU and EMS induced mutants were normal with respect to the alleles they were derived from. These data indicated that X-rays primarily Induced large deletions, while the alkylating agents ENU and EMS predominantly induced missense mutations. Therefore the Adh forward mutation assay recovered a