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Variation in activity and thermostability of alcohol dehydrogenase in Drosophila melanogaster

Published online by Cambridge University Press:  14 April 2009

J. McKay
J. McKay
Affiliation:
Institute of Animal Genetics, West Mains Road, Edinburgh EH9 3JN, Scotland
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The activity and thermostability of alcohol dehydrogenase (ADH) from 247 strains of Drosophila melanogaster were studied by spectrophotometric assay. The strains, in which second chromosomes had been made homozygous in a standard genetic background, were derived from five natural populations from diverse geographical and ecological sites. Evidence is presented that the majority of variation in ADH activity is attributable to the presence, in all five populations, of two electromorphs of the enzyme. However, some variation does exist between strains carrying the same electromorph, to some extent associated with variation hi body weight. Two strains showed atypical ADH activities. Variation in ADH thermostability was almost wholly attributable to the presence of two electromorphs; only two strains had enzymes with thermostabilities atypical of their electromorph. In the four strains with abnormal ADH properties the locus (loci) responsible map in the region of the Adh locus. Therelatively low level of heterogeneity within electrophoretic classes at this locus is discussed in view of recent findings at other enzyme loci in Drosophila.

Type
Research Article
Information
Genetics Research , Volume 37 , Issue 3 , June 1981 , pp. 227 - 237
Copyright
Copyright © Cambridge University Press 1981

References

REFERENCES

Band, H. T. (1975). Survey of isozyme polymorphism in a Drosophila melanogaater natural population. Genetics, 80, 760–771.CrossRefGoogle Scholar
Bernstein, S. C., Throckmorton, L. H. & Hubby, J. L. (1973). Still more genetic variability in natural populations. Proceedings of the National Academy of Sciences, U.S.A. 70, 3928–3931.CrossRefGoogle ScholarPubMed
Birley, A. J. & Barnes, B. W. (1973). Genetical variation for enzyme activity in a natural population of Drosophila melanogaster I. Extent of variation for alcohol dehydrogenase. Heredity 31, 413–416.Google Scholar
Clarke, B., (1975). The contribution of ecological genetics to evolutionary theory. Genetics 79, 101–113.Google Scholar
Clarke, B., Camfield, R. G., Galvin, A. M. & Pitts, C. R. (1979). Environmental factors affecting the quantity of alcohol dehydrogenase in Drosophila melanogaster. Nature 280, 517–518.CrossRefGoogle ScholarPubMed
Cochrane, B. J. & Richmond, R. C. (1979). Studies of esterase-6 in Drosophila melanogaster. II. The genetics and frequency distribution of naturally occurring variants studied by electrophoretic and heat stability criteria. Genetics, 93, 461–478.CrossRefGoogle ScholarPubMed
Coyne, J. A., Felton, A. A. & Lewontin, R. C. (1978). The extent of genetic variation at a highly polymorphic esterase locus in Drosophila pseudoobscura. Proceedings of the National Academy of Sciences, U.S.A. 75, 5090–5093.Google Scholar
David, J. R. & Bocquet, C. (1975). Evolution of a cosmopolitan species: genetic latitudinal clines in Drosophila melanogaster wild populations. Experientia 31, 164–166.CrossRefGoogle ScholarPubMed
Day, T. H., Hillier, P. C. & Clarke, B. (1974 a). Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochemical Genetics 11, 141–153.CrossRefGoogle ScholarPubMed
Day, T. H., Hillier, P. C. & Clarke, B. (1974 b). Relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster. Biochemical Genetics 11, 155–165.CrossRefGoogle ScholarPubMed
Hewitt, N. E., Pipkin, S. B., Williams, N. & Chakrabartty, P. K. (1974). Variation in ADH activity in class I and class II strains of Drosophila. Journal of Heredity 65, 141–148.CrossRefGoogle Scholar
Ives, P. T. (1945). The genetic structure of American populations of Drosophila melanogaster. Genetics 30, 167–196.CrossRefGoogle ScholarPubMed
Johnson, G. B. (1977). Characterisation of electrophoretically cryptic variation in the alpine butterfly Colias meadii. Biochemical Genetics 15, 665–693.Google Scholar
Kojima, K., Gillespie, J. & Tobari, Y. N. (1970). A profile of Drosophila species enzymes assayed by electrophoresis. I. Number of alleles, heterozygosity and linkage disequilibrium in glucose and non-glucose metabolising enzymes. Biochemical Genetics 4, 627–637.Google Scholar
Lewontin, R. C. (1974). The genetic basis of evolutionary change. Columbia University Press, New York and London.Google Scholar
Lindsley, D. L. & Grell, E. H. (1967). Genetic variations of Drosophila melanogaster. Carnegie Institution of Washington, Publication 627, Washington, B.C.Google Scholar
McDonald, J. F. & Ayala, F. J. (1978). Genetic and biochemical basis of enzyme activity variation in natural populations. I. Alcohol dehydrogenase in Drosophila melanogaster. Genetica 89, 371–388.CrossRefGoogle ScholarPubMed
McDonald, J. F., Chambers, G. K., David, D. J. & Ayala, F. J. (1977). Adaptive response due to changes in gene regulation: A study with Drosophila. Proceedings of the National Academy of Sciences, U.S.A. 74, 4562–4566.Google Scholar
Malpica, J. M. & Vassallo, J. M. (1980). A test for the selective origin of environmentally correlated allozyme patterns. Nature 286, 406–408.Google Scholar
Marshall, D. R. & Brown, A. H. D. (1975). The charge-state model of protein polymorphism in natural populations. Journal of Molecular Evolution 6, 149–163.Google Scholar
Nei, M. (1968). The frequency distribution of lethal chromosomes in finite populations. Proceedings of the National Academy of Sciences, U.S.A. 60, 517–524.Google Scholar
Nei, M. (1976). Mathematical models of speciation and genetic distance. In ‘Population genetics and ecology’ (ed. Karlin, S. and Nevo, E.. New York and London: Academic Press).Google Scholar
Ohta, T. & Kimura, M. (1974). Simulation studies on electrophoretically detectable genetic variability in a finite population. Genetics 76, 615–624.Google Scholar
Prout, T. (1954). Genetic drift in irradiated experimental populations of Drosophila melanogaster. Genetica 39, 529–545.Google Scholar
Sampsell, B. (1977). Isolation and genetic characterization of alcohol dehydrogenase thermo-stability variants occurring in natural populations of Drosophila melanogaster. Biochemical Genetics 15, 971–988.Google Scholar
Shaw, C. R. & Prasad, R. (1970). Starch gel electrophoresis – a compilation of recipes. Biochemical Genetics, 4, 296–320.Google Scholar
Singh, R. S., Hubby, J. L. & Throckmorton, L. H. (1975). Genetic variation by electrophoresis and heat denaturation in octanol dehydrogenase of the Drosophila virilis species group. Genetics 80, 637–650.Google Scholar
Singh, R. S., Lewontin, R. C. & Felton, A. A. (1976). Genetic heterogeneity within alleles of Xanthine dehydrogenase in Drosophila pseudoobscura. Genetics 84, 609–629.Google Scholar
Thompson, J. N., Ashburner, M. & Woodruff, R. C. (1977). Presumptive control mutation for alcohol dehydrogenase in Drosophila melanogaster. Nature 270, 363.CrossRefGoogle ScholarPubMed
Trippa, G., Loverre, A. & Catamo, A. (1976). Thermostability studies for investigating non-electrophoretic polymorphic alleles in Drosophila melanogaster. Nature 260, 42–44.Google Scholar
Vigue, C. L. & Johnson, F. M. (1973). Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster. Biochemical Genetics 9, 213–227.CrossRefGoogle ScholarPubMed
Voelker, R. A., Schaffer, H. E. & Mukai, T. (1980). Spontaneous allozyme mutation in Drosophila melanogaster. Genetics 94, 961–968.CrossRefGoogle ScholarPubMed
Ward, R. D. (1975). Alcohol dehydrogenase activity in Drosophila melanogaster: a quantitative character. Genetical Research 26, 81–93.Google Scholar