Abstract
The nucleotide sequence of theGpdh gene from six taxa,D. virilis, D. lummei, D. novamexicana, D. a. americana, D. a. texana andD. ezoana, belonging to thevirilis species group was determined to examine details of evolutionary change in the structure of theGpdh gene. TheGpdh gene is comprised of one 5′ non-translated region, eight exons, seven introns and three 3′ non-translated regions. Exon/intron organization was identical in all the species examined, but different from that of mammals. Interspecific nucleotide divergence in the entireGpdh gene followed the common pattern: it was low in the exon, high in the intron and intermediate in the non-translated regions. The degree of nucleotide divergence differed within these regions, suggesting that selection exerts constraints differentially on nucleotide change of theGpdh gene. A phylogenetic tree of thevirilis phylad constructed from nucleotide variation of total sequence was consistent with those obtained from other data.
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Arai, K., H. Tominaga, Y. Yokote & S. Nariss, 1988. The complete amino acid sequence of cytoplasmic glycerol-3-phosphate dehydrogenase fromDrosophola virilis. Biochim. Biophys. Acta 953: 6–13.
Cook, J.L., G.C. Bewley & J.B. Shaffer, 1988.Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes are generated by alternate pathways of RNA processing resulting in different carboxyl-terminal amino acid sequences. J. Biol. Chem. 263: 10858–10864.
Fitch, W.M., 1977. On the problem of discovering the most parsimonious tree. Amer. Natur. 111: 223–257.
Hansfold, R.G. & B. Sacktor, 1971. Oxidative metabolism of insecta. pp. 213–247 in Chemical Zoology Vol. 6, edited by M. Florkin & B.T. Scheer, Academic Press, New York.
Heberlein, U. & G.M. Rubin, 1990. Structural and functional comparisons of theDrosophila virilis andDrosophila melanogaster rough genes. PNAS, U.S.A. 87: 5916–5920.
Henikoff, S., 1987. Unidirectional digestion with exonuclease III in DNA sequence analysis. pp. 156–165 in Methods in Enzymology Vol. 155, edited by R. Wu, Academic Press, New York.
Higgins, D.G. & P.M. Sharp, 1988. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73: 237–244.
Hultmark, D., R. Klemenz & W.J. Gehring, 1986. Translational and transcriptional control elements in the untranslated leader of the heat-shock gene hsp22. Cell 44: 429–438.
Ireland, R.C., M.A. Kotarski, L.A. Johnston, U. Stadler, E. Birkenmeier & L.P. Kozak, 1986. Primary structure of the mouse glycerol-3-phosphate dehydrogenase gene. J. Biol. Chem. 261: 11779–11785.
Jukes, T.H. & C.R. Cantor, 1969. Evolution of protein molecules. pp. 21–132 in Mammalian Protein Metabolism edited by H.N. Munro, Academic Press, New York.
Kimura, M. 1980. A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences. J. Mol. Evol. 16: 111–120.
Kozak, L.P. & J.T. Jensen, 1974. Genetic and developmental control of multiple forms of L-glycerol 3-phosphate dehydrogenase. J. Biol. Chem. 249: 7775–7781.
Narise, S., 1980. Purification and biochemical properties of allelic forms of cytoplasmic glycerol-3-phosphate dehydrogenase fromDrosophila virilis. Biochim. Biophys. Acta 615: 289–298.
Narise, S. & H. Tominaga, 1992. Temperature-dependency differences in αGpdh allozymes associated with a single base change in the coding region of the αGpdh structural gene inDrosophila virilis. Biochem. Genet. (Life Sci. Adv.) 11: 39–45.
Nei, M. & T. Gojobori, 1986. Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol. Biol. Evol. 3: 418–426.
O'Brien, S.J. & R.J. MacIntyre, 1972. The α-glycerophosphate inDrosophila melanogaster II. Genetic aspects. Genetics 71: 127–138.
Ostro, M.J. & T.P. Fondy, 1977. Isolation and characterization of multiple molecular forms of cytosolic NAD-linked glycerol-3-phosphate dehydrogenase from normal and neoplastic rabbit tissues. J. Biol. Chem. 252: 5575–5583.
Reinbold, S. & G.E. Collier, 1990. Molecular systematics of theDrosophila virlis species group (Diptera: Drosophilidae). Ann. Entomol. Soc. Amer. 83: 467–474.
Ross, C.R., S. Curry, A.W. Schwartz & T.P. Fondy, 1971. Multiple molecular forms of cytoplasmic glycerol-3-phosphate dehydrogenase in rat liver. Arch. Biochem. Biophys. 145: 591–603.
Saitou, N. & M. Nei, 1987. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406–425.
Sanger, F., S. Nicklen & A.R. Coulson, 1977. DNA sequencing with chain-terminating inhibitors. PNAS U.S.A. 74: 5463–5467.
Spicer, G.S., 1991. Molecular evolution and phylogeny of theDrosophila virilis species group as inferred by two-dimensional electrophoresis. J. Mol. Evol. 33: 379–394.
Spicer, G.S., 1992. Reevaluation of the phylogeny of theDrosophila virilis species group (Diptera: Drosophilidae). Ann. Entomol. Soc. Amer. 85: 11–25.
Throckmorton, L.H., 1982. Thevirilis species group. pp. 227–296 in The Genetics and Biology ofDrosophila vol. 3b, edited by M. Ashburner, H.L. Carson & T.N. Thompson, Jr., Academic Press, New York.
Tominaga, H., K. Arai & S. Narise, 1989. Single amino acid substitutions in sn-glycerol-3-phosphate dehydrogenase allozymes fromDrosophila virilis. Experientia 45: 312–314.
Tominaga, H., T. Shiba & S. Narise, 1992. Structure ofDrosophila virilis glycerol-3-phosphate dehydrogenase gene and a comparison with theDrosophila melanogaster gene. Biochim. Biophys. Acta 1131: 233–238.
Treier, M., C. Pfeifle & D. Tautz, 1989. Comparison of the gap segmentation gene hunchback betweenDrosophila melanogaster andDrosophila virilis reveals novel modes of evolutionary change. EMBO J. 8: 1517–1525.
Tsuno, K., 1991. An analysis of long base sequences in the 2nd intron ofDrosophila αGpdh. Meikai Univ. J. Arts and Sci. 3: 19–26.
von Kalm, L., J. Weaver, J. DeMarco, R.J. MacIntyre & D.T. Sullivan 1989. Structural characterization of the α-glycerol-3-phosphate dehydrogenase-encoding gene ofDrosophila melanogaster. PNAS U.S.A. 86: 5020–5024.
White III, H.B. & N.O. Kaplan, 1972. Separate physiological roles for two isozymes of pyridine nucleotide-linked glycerol-3-phosphate dehydrogenase in chicken. J. Mol. Evol. 1: 158–172.
Yao, K-M. & K. White, 1991. Organization analysis of elav gene and functional analysis of ELAV protein ofDrosophila melanogaster andDrosophila virilis. Mol. Cell. Biol. 11: 2994–3000.
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Nucleotide sequences for theGpdh gene ofD. lummei, D. novamexicana, D. a. americana, D. a. texana andD. ezoana have been submitted to GenBank with accession numbers D50087, D50088, D50089, D50090 and D50091.
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Tominaga, H., Narise, S. Sequence evolution of theGpdh gene in theDrosophila virilis species group. Genetica 96, 293–302 (1995). https://doi.org/10.1007/BF01439583
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DOI: https://doi.org/10.1007/BF01439583