Origin of ?-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster and their functional relationship in the ?-glycerophosphate cycle

Abstract

The basis for the differentiation of l-glycerol-3-phosphate dehydrogenase (α-GPDH) into larval and adult isozymes in Drosophila melanogaster was investigated by the correlation of a lack of appearance of each isozyme during development within Drosophila bearing α-GPDH “null” alleles and by the study of a putative conversion factor. Conversion studies indicate the presence of a heat-labile RNase-resistant conversion factor present in crude larval extracts with the ability to convert GPDH-1 to GPDH-2 and GPDH-3 but not vice versa. In addition, “null” mutations at the Gpdh locus obliterate all isozymatic species of α-GPDH in all developmental stages. These observations suggest that all α-GPDH isozymes are the product of a single structural gene and that the multiple forms of this enzyme arise during successive developmental stages through an epigenetic modification of the primary Gpdh ⁺ polypeptide. Finally, observations are reported which bear on the functional divergence of the α-glycerophosphate cycle in the adult and larval stage of development.