Skip to main content
SpringerLink
Log in

Functional and biochemical features of alcohol dehydrogenase in four species of the obscura group of Drosophila

  • Published:
Genetica Aims and scope Submit manuscript

Abstract

The biochemical features of ADH of four Drosophila species of the obscura group have been studied. The relationship between ethanol tolerance and ADH activity has been investigated. Propan-2-ol and acetone concentrations have been determined in propan-2-ol treated flies and ADH activity has been followed during 96 h of propan-2-ol treatment. Data on the ADH system confirm constructed phylogenies based on electrophoretic variation and chromosome homologies.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Argiles, J. M., 1986. Has acetone a role on the conversion of fat to carbohydrate in mammals? TIBS 11: 61–63.

    Google Scholar 

  • Ashburner, M., Bodmer, M. & Lemeunier, F., 1984. On the evolutionary relationships of Drosophila melanogaster. Devel. Genet. 4: 295–312.

    Google Scholar 

  • Atrian, S. & Gonzàlez-Duarte, R., 1982. Comparison of some biochemical features of the enzyme alcohol dehydrogenase in sixteen species of Drosophila. In: S., Lakovaara, (ed.), Advances in genetics, development and evolution of Drosophila. Plenum Press, New York, pp. 251–261.

    Google Scholar 

  • Atrian, S. & Gonzàlez-Duarte, R., 1985. Purification and molecular characterization of alcohol dehydrogenase from Drosophila hydei: conservation in the biochemical features of the enzyme in several species of Drosophila. Biochem. Genet. 23: 891–911.

    Google Scholar 

  • Bradford, M. M., 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.

    Google Scholar 

  • Cabrera, V. M., Gonzàlez, A. M., Larruga, J. M. & Gullon, A., 1983. Genetic distance and evolutionary relationships in the Drosophila obscura group. Evolution 37: 675–689.

    Google Scholar 

  • Daly, D. & Clarke, B., 1981. Selection associated with the alcohol dehydrogenase locus in Drosophila melanogaster: differential survival of adults maintained on low concentrations of ethanol. Heredity 46: 219–226.

    Google Scholar 

  • David, J. R., Van, Herrewege, J., Monclus, M. & Prevosti, A., 1979. High ethanol tolerance in two distantly related Drosophila species: a probable case of recent convergent adaptation. Comp. Biochem. Physiol. 63C: 53–56.

    Google Scholar 

  • Fletcher, T. S., Ayala, F. J., Thatcher, D. R. & Chambers, G. R., 1978. Structural analysis of the ADHS electromorph of Drosophila melanogaster. Proc. Natn. Acad. Sci. U.S.A. 75: 5609–5612.

    Google Scholar 

  • Geer, B. W., McKechnie, S. W. & Langevin, M. L., 1986. The effect of dietary ethanol on the composition of lipids of Drosophila melanogaster larvae. Biochem. Genet. 24: 51–69.

    Google Scholar 

  • Gonzàlez-Duarte, R. & Vilageliu, Ll., 1985. Metabolic response to ethanol and isopropanol in D. funebris and D. immigrans. Comp. Biochem. Physiol. 80C: 189–192.

    Google Scholar 

  • Gonzàlez-Duarte, R. & Atrian, S., 1986. Metabolic response to alcohol ingesion of Dorosphila hydei. Heredity 56: 123–128.

    Google Scholar 

  • Hatzopoulos, P. & Loukas, M., 1986. Differentiation of the vitellogenin proteins in species of the Drosophila obscura group. Genetica 71: 119–122.

    Google Scholar 

  • Heberlein, U., England, B. & Tjian, R., 1985. Characterization of Drosophila transcription factors that activate the tandem promoters of the alcohol dehydrogenase gene. Cell 41: 965–977.

    Google Scholar 

  • Jacobson, K. B., Murphy, J. B., Knopp, J. A. & Ortiz, J. R., 1972. Multiple forms of Drosophila alcohol dehydrogenase. III. Conversion of one form to another by nicotinamide adenine dinucleotide or acetone. Arch. Biochem. Biophys. 149: 22–35.

    Google Scholar 

  • Juan, E. & Gonzàlez-Duarte, R., 1980. Purification and enzyme stability of alcohol dehydrogenase from Drosophila simulans, Drosophila virilis and Drosophila melanogaster AdhS. Biochem. J. 189: 105–110.

    Google Scholar 

  • Juan, E. & Gonzàlez-Duarte, R., 1981. Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Biochem. J. 195: 61–69.

    Google Scholar 

  • Kamping, A. & Van, Delden, W., 1978. Alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. II. Relation between ADH activity and adult mortality. Biochem. Genet. 16: 541–551.

    Google Scholar 

  • Karlsson, CH., Davies, H., Ohman, J. & Anderson, M., 1973. Applications note LKB 75.

  • Kreitman, M., 1983. Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster. Nature 304: 412–417.

    Google Scholar 

  • Krimbas, C. B. & Loukas, M., 1984. Evolution of the obscura group Drosophila species. I Salivary chromosomes and quantitative characters in D. subobscura and two closely related species. Heredity 53: 469–482.

    Google Scholar 

  • Lakovaara, S., Saura, A. & Falk, C. T., 1972. Genetic distance evolutionary relationships in Drosophila obscura group. Evolution 26: 177–184.

    Google Scholar 

  • Lakovaara, S., Saura, A., Lankinen, Pl, Pohjola, L. & Lokki, J., 1976. The use of isoenzymes in tracing evolution and classifying Drosophilidae. Zoologica Scripta 5: 173–179.

    Google Scholar 

  • Lakovaara, S. & Saura, A., 1982. Evolution and speciation in the Drosophila obscura group. In: M., Ashburner, H. L., Carson and J.N. Su., Thompson (eds). The genetics and biology of Drosophila. 3b, Academic Press, London, 2–9.

    Google Scholar 

  • Loukas, M., Krimbas, C. B. & Vergini, Y., 1984. Evolution of the obscura group Drosophila species. II Phylogeny of ten species based on electrophoretic data. Heredity 53: 483–493.

    Google Scholar 

  • McDonald, J. F. & Avise, J. C., 1976. Evidence for the adaptive significance of enzyme activity levels: interspecific variation in α-GPDH and ADH in Drosophila. Biochem. Genet. 14: 348–355.

    Google Scholar 

  • McKenzie, S. W. & Morgan, P., 1982. Alcohol dehydrogenase polymorphism of Drosophila melanogaster: Aspects of alcohol and temperature variation in the larval environment. Aust. J. biol. Sci. 35: 85–93.

    Google Scholar 

  • McKenzie, J. A. & Parsons, P. A., 1974. Microdifferentation in a natural population of D. melanogaster to alcohol in the environment. Genetics 77: 385–394.

    Google Scholar 

  • Monclus, M., 1976. Distribución y ecología de Drosofílidos en España. III. Especies de Drosophila de las Islas Canarias, con la descripción de una nueva especie. Bol. R. Soc. Española Hist. Nat. (Biol.) 74: 197–213.

    Google Scholar 

  • Monclus, M., 1984. Drosophilidae of Madeira, with the description of Drosophila madeirensis n. sp. Z. zool. Syst. Evolut. Forsch. 22: 94–103.

    Google Scholar 

  • Posakony, J. W., Fisher, J. A. & Maniatis, T., 1985. Identification of DNA sequences required for the regulation of Drosophila alcohol dehydrogenase gene expression. Cold Spring Harbor Symp. quant. Biol. 50: 515–520.

    Google Scholar 

  • Savakis, C. & Ashburner, M., 1985. A simple gene with a complex pattern of transcription: the alcohol dehydrogenase gene of Drosophila melanogaster. Cold Spring Harbor Symp. quant. Biol. 50: 505–514.

    Google Scholar 

  • Schwartz, M., O'Donnell, J. & Sofer, W., 1979. Origin of the multiple forms of alcohol dehydrogenase from D. melanogaster. Arch. Biochem. Biophys. 194: 365–378.

    Google Scholar 

  • Thatcher, D. R., 1977. Enzyme instability and proteolysis during the purification of an alcohol dehydrogenase from Drosophila melanogaster. Biochem. J. 163: 317–323.

    Google Scholar 

  • Thatcher, D. R., 1980. The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (Adhn−11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster. Biochem. J. 187: 875–886.

    Google Scholar 

  • Ursprung, H. & Leone, J., 1965. Alcohol dehydrogenases: A polymorphism in Drosophila melanogaster. J. exp. Zool. 160: 147–154.

    Google Scholar 

  • Van, Delden, W., 1982. The alcohol dehydrogenase polymorphism in Drosophila melanogaster. In: Evolutionary Biology (K. K., Hecht, B., Wallace and G. T., Prance, eds) 15: 187–222. Plenum Press. New York-London.

    Google Scholar 

  • Vigue, C. L. & Johnson, F. M., 1973. Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environments relationships of allelic alcohol dehydrogenase in D. melanogaster. Biochem. Genet. 9: 213–227.

    Google Scholar 

  • Vilageliu, L1, & Gonzàlez-Duarte, R., 1980. Effect of ethanol and isopropanol on the activity of alcohol dehydrogenase, viability and life-span in Drosophila melanogaster and Drosophila funebris. Experientia 36: 828–829.

    Google Scholar 

  • Vilageliu, Ll. & Gonzàlez-Duarte, R., 1984. Alcohol dehydrogenase from Drosophila funebris and Drosophila immigrans: Molecular and evolutionary aspects. Biochem. Genet. 22: 797–815.

    Google Scholar 

  • Winberg, J. O., Thatcher, D. R. & McKinley-McKee, J. S., 1982. Alcohol dehydrogenase from the fruitfly Drosophila melanogaster substrate specificity of the alleloenzymes AdhS and AdhUF. Biochem. biophys. Acta 704: 7–15.

    Google Scholar 

  • Winberg, J. O., Thatcher, D. R. & McKinley-McKee, J. S., 1983. Drosophila melanogaster alcohol dehydrogenase: An electrophoretic study of the AdhS, AdhF and AdhUF alleloenzymes. Biochem. Genet. 21: 63–79.

    Google Scholar 

  • Winberg, J. O., Hovik, R., McKinley-McKee, J. S., Juan, E. & Gonzàlez-Duarte, R., 1986. Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis. Biochem. J. 235: 481–490.

    Google Scholar 

  • Zwiebel, L. J., Cohn, V. H., Wright, D. R. & Moore, G. P., 1982. Evolution of single-copy DNA and the ADH gene in seven Drosophilids. J. mol. Evol. 19: 62–71.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Departament de Genética, Facultat de Biologia, Universidad de Barcelona, Av. Diagonal, 645, 08028, Barcelona, Spain

    J. J. Hernández, Ll. Vilageliu & R. González-Duarte

Authors
  1. J. J. Hernández
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ll. Vilageliu
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. R. González-Duarte
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hernández, J.J., Vilageliu, L. & González-Duarte, R. Functional and biochemical features of alcohol dehydrogenase in four species of the obscura group of Drosophila . Genetica 77, 15–24 (1988). https://doi.org/10.1007/BF00058547

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00058547

Keywords

Search

Navigation