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.
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This investigation was supported in part by NIH Research Grant No. GM-15691 and Genetics Training Grant No. 2 TI GM-685 at the University of North Carolina and by NIH Research Grant No. GM-11546 at North Carolina State University.
Paper No. 5054 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh, North Carolina.
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Bewley, G.C., Lucchesi, J.C. Origin of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster and their functional relationship in the α-glycerophosphate cycle. Biochem Genet 15, 235–251 (1977). https://doi.org/10.1007/BF00484456
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DOI: https://doi.org/10.1007/BF00484456