Abstract
Eleven Australian natural populations of Drosophila melanogaster were screened by electrophoresis for evidence of null and/or low activity variants at the Gdph locus. Of 5018 alleles investigated, 57 had markedly lower GPDH activity, as judged by their heterozygous phenotypes, than control alleles. GPDH assays of 13 of these variant alleles showed that whilst they were heterogeneous in their properties and included electrophoretic variants and two categories of low-activity variant, there were no true null alleles. The most common low-activity variants exhibited dominance for GPDH activity in heterozygotes with normal alleles, and were shown to share this property with an allele previously isolated from a London (UK) population (Langley et al., 1981).
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Bewley, G C. 1978. Heat stability studies at the α-glycerophosphate dehydrogenase locus in populations of Drosophila melanogaster. Biochem Genet, 16, 767–775.
Bewley, G C. 1981. Genetic control of the developmental program of L-glycerol-3-phosphate dehydrogenase isozymes in Drosophila melanogaster. identification of a cisacting temporal element affecting GPDH-3 expression. Dev Genet, 2, 113–129.
Bewley, G C, Cook, J L, Kusakabe, S, Mukai, T, Rigby, D L, and Chambers, G C. 1989. Sequence, structure and evolution of the gene coding for sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster. Nuc Acids Res, 17, 8553–8567.
Bewley, G C, Rawls, J M, Jr, and Lucchesi, J C. 1974. α-glycerophosphate dehydrogenase in Drosophila melanogaster: kinetic differences and developmental differentiation of the larval and adult isozymes. J Insect Physiol, 20, 153–165.
Burkhart, B D, Montgomery, E, Langley, C H, and Voelker, R A. 1984. Characterization of allozyme null and low activity alleles from two natural populations of Drosophila melanogaster. Genetics, 107, 295–306.
Chambers, G K, Felton, A A, Ramshaw, J A M, Rigby, D L, and Sullivan, D T. 1985. Structural analysis of glycerol-3-phosphate dehydrogenase from several Drosophila species. Biochem Genet, 23, 801–814.
Collier, G E, and MacIntyre, R J. 1977a. Microcomplement fixation studies on the evolution of α-glycerophosphate dehydrogenase within the genus Drosophila. Proc Natl Acad Sci, USA, 74, 684–688.
Collier, G E, and MacIntyre, R J. 1977b. Low specific activity of rare allozymes of α-glycerophosphate dehydrogenase in Drosophila. Nature, 267, 839–841.
Cooke, J L, Bewley, G C, and Shaffer, J B. 1988. Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are generated by alternate pathways of RNA processing resulting in different carboxy L-terminal amino acid sequences. J Biol Chem, 263, 10858–10864.
Cook, J L, Shaffer, J B, Bewley, G C, MacIntyre, R J, and Wright, D A. 1986. Isolation of a genomic clone for Drosophila sn-glycerol-3-phosphate dehydrogenase using synthetic oligonucleotides. J Biol Chem, 261, 11751–11755.
Coyne, J A, Eanes, W F, Ramshaw, J A M, and Koehn, R K. 1979. Electrophoretic heterogeneity of α-glycerophosphate dehydrogenase among many species of Drosophila. Syst Zool, 28, 164–175.
Eanes, W F, and Hey, J. 1986. In vivo function of rare G6pd variants from natural populations of Drosophila melanogaster. Genetics, 113, 679–693.
Freeth, A L, and Gibson, J B. 1985. Alcohol dehydrogenase and sn-glycerol-3-phosphate dehydrogenase null activity alleles in natural populations of Drosophila melanogaster. Heredity, 55, 369–374.
Freeth, A L, Gibson, J B, and De Couet, H G. 1986. The partial characterization of alcohol dehydrogenase null alleles from natural populations of Drosophila melanogaster. Biochem Genet, 24, 957–972.
Freeth, A L, Gibson, J B, and Wilks, A V. 1987. Transcription analysis of alcohol dehydrogenase null alleles from natural populations of Drosophila melanogaster. Genome, 30, 25–30.
Gibson, J B, and Wilks, A V. 1989. Molecular structure of a naturally occurring alcohol dehyrogenase null activity allele in Drosophila melanogaster. Biochem Genet, 27, 679–688.
Gibson, J B, Wilks, A V, Cao, A, and Freeth, A L. 1985. Dominance for enzyme activity in Drosophila melanogaster. Experientia, 42, 191–192.
Gibson, J B, Wilks, A V, Cao, A, and Freeth, A L. 1986. Dominance for sn-glycerol-3-phosphate dehydrogenase activity in Drosophila melanogaster: evidence for differential allelic expression mediated via a trans-acting effect. Heredity, 56, 227–235.
Grell, E H. 1967. Electrophoretic variants of α-glycerophosphate dehydrogenase in Drosophila melanogaster. Science, 158, 1319–1320.
Jiang, C, Gibson, J B, and Chen, J. 1989. Genetic differentiation in populations of Drosophila melanogaster from the Peoples' Republic of China: comparison with patterns on other continents. Heredity, 62, 193–198.
Jiang, C, Gibson, J B, Wilks, A V, and Freeth, A L. 1988. Restriction endonuclease variation in the region of the alcohol dehydrogenase gene: a comparison of null and normal alleles from natural populations of Drosophila melanogaster. Heredity, 60, 101–107.
Johnson, F M, and Schaffer, J E. 1973. Isozyme variability in species of the genus Drosophila. VII. Genotype-environment relationships in populations of D. melanogaster from the eastern United States. Biochem Genet, 10, 149–163.
Kotarski, M A, Pickert, S, Leonard, D A, La Rosa, G T, and MacIntyre, R J. 1983a. The characteriz0ation of α-glycero-phosphate dehydrogenase mutants in Drosophila melanogaster. Genetics, 105, 387–407.
Kotarski, M A, Pickert, S, and MacIntyre, R J. 1983b. A cytogenetic analysis of the chromosomal region surrounding the α-glycerophosphate dehydrogenase locus of Drosophila melanogaster. Genetics, 105, 371–386.
Langley, C H, Voelker, R A, Leigh Brown, A J, Ohnishi, S, Dickson, B, and Montgomery, E. 1981. Null allele frequencies at allozyme loci in natural populations of Drosophila melanogaster. Genetics, 99, 151–156.
Laurie-Ahlberg, C C, and Bewley, G C. 1983. Naturally occurring genetic variation affecting the expression of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster. Biochem Genet, 21, 943–961.
Lee, C-Y, Niesel, D, and Bewley, G C. 1980. Analyses of genzetic variants of a-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster by two-dimensional gel electrophoresis and Immunoelectrophoresis. Biochem Genet, 18, 1003–1018.
Lewis, N, and Gibson, J. 1978. Variation in amount of enzyme protein in natural populations. Biochem Genet, 16, 159–170.
Lindsley, D L, and Grell, E H. 1968. Genetic variations of Drosophila melanogaster. Cam Inst Wash Pub, Number 627.
Niesel, D W, Pan, Y-C E, Bewley, G C, Armstrong, F B, and Li, S S-L. 1982. Structural analysis of adult and larval isozymes of sn-glycerol-3-phosphate dehydrogenase of Drosophila melanogaster. J Biol Chem, 257, 979–983.
Oakeshott, J B, Gibson, J B, Anderson, P R, Knibb, W R, Anderson, D G, and Chambers, G K. 1982. Alcohol dehydrogenase and glycerol-3-phosphate dehydrogenase clines in Drosophila melanogaster on different continents. Evolution, 36, 86–96.
O'Brien, S J, and MacIntyre, R J. 1972. The α-glycerophosphate cycle in Drosophila melanogaster. II. Genetic aspects. Genetics, 71, 127–138.
O'Brien, S J, Wallace, B, and MacIntyre, R J. 1972. The α-glycerophosphate cycle in Drosophila melanogaster. III. Relative viability of ‘null’ mutants at the α-glycerophosphate dehydrogenase-1 locus. Am Nat, 106, 767–771.
Otto, J, Argos, P, and Rossmann, M G. 1980. Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases. Eur J Biochem 109, 325–330.
Sacktor, B. 1970. Regulation of intermediary metabolism with special reference to control mechanisms in insect flight muscle. Adv Insect Physiol 7, 267–347.
Shaffer, J B, and Bewley, G C. 1983. Genetic determination of sn-glycerol-3-phosphate dehydrogenase synthesis in Drosophila melanogaster. J Biol Chem, 258, 10027–10033.
Singh, R S, Hickey, D A, and David, J. 1982. Genetic differentiation between geographically distant populations of Drosophila melanogaster. Genetics, 101, 235–256.
Voelker, R A, Langley, C H, Leigh Brown, A J, Ohnishi, S, Dickson, B, Montgomery, E, and Smith, S. 1980a. Enzyme null alleles in natural populations of Drosophila melanogaster. frequencies in a North Carolina population. Proc Natl Acad Sci USA, 77, 1091–1095.
Voelker, R A, Schaffer, H E, and Mukai, T. 1980b. Spontaneous allozyme mutations in Drosophila melanogaster. rate of occurrence and nature of the mutants. Genetics, 94, 961–968.
Von Kalm, L, Weaver, J, Demarco, J, MacIntyre, R J, and Sullivan, D T. 1989. Structural characterization of the α-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster. Proc Natl Acad Sci USA, 86, 5020–5024.
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Gibson, J., Cao, A., Symonds, J. et al. Low activity sn-glycerol-3-phosphate dehydrogenase variants in natural populations of Drosophila melanogaster. Heredity 66, 75–82 (1991). https://doi.org/10.1038/hdy.1991.10
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DOI: https://doi.org/10.1038/hdy.1991.10
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