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Genetic variation in the dietary sucrose modulation of enzyme activities in Drosophila melanogaster*

Published online by Cambridge University Press:  14 April 2009

Billy W. Geer
Affiliation:
Department of Biology, Knox College, Galesburg, Illinois 61401
Cathy C. Laurie-Ahlberg
Affiliation:
Department of Genetics, North Carolina State University, Raleigh, North Carolina 27695

Summary

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Genetic variation in the modulating effect of dietary sucrose was assessed in Drosophila melanogaster by examining 27 chromosome substitution lines coisogenic for the X and second chromosomes and possessing different third isogenic chromosomes derived from natural populations. An increase in the concentration of sucrose from 0·1% to 5% in modified Sang's medium C significantly altered the activities of 11 of 15 enzyme activities in third instar larvae, indicating that dietary sucrose modulates many, but not all, of the enzymes of D. melanogaster. A high sucrose diet promoted high activities of enzymes associated with lipid and glycogen synthesis and low activities of enzymes of the glycolytic and Krebs cycle pathways, reflecting the physiological requirements of the animal. Analyses of variance revealed significant genetic variation in the degrees to which sucrose modulated several enzyme activities. Analysis of correlations revealed some relationships between enzymes in the genetic effects on the modulation process. These observations suggest that adaptive evolutionary change may depend in part on the selection of enzyme activity modifiers that are distributed throughout the genome.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1984

References

REFERENCES

Cavener, D. R. & Clegg, M. T. (1981 a). Multigenic response to ethanol in Drosophila melanogaster. Evolution 35, 110.Google Scholar
Cavener, D. R. & Clegg, M. T. (1981 b). Evidence for biochemical and physiological differences between enzyme genotypes in Drosophila melanogaster. Proceedings of the National Academy of Science, USA 78, 44444447.Google Scholar
Cochrane, B. J., Lucchesi, J. C. & Laurie-Ahlberg, C. C. (1983). Regulation of enzyme activities in Drosophila: genetic variation affecting induction of glucose 6-phosphate and 6-phosphogluconate dehydrogenase in larvae. Genetics 105, 601613.CrossRefGoogle ScholarPubMed
Geer, B. W., Kamiak, S. N., Kidd, K. R., Nishimura, R. A. & Yemm, S. J. (1976). Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. I. Modulation by dietary carbohydrate and lipid. Journal of Experimental Zoology, 195, 1532.CrossRefGoogle ScholarPubMed
Geer, B. W., Krochko, D. & Williamson, J. H. (1979 a). Ontogeny, cell distribution, and the physiological role of NADP-malic enzyme in Drosophila melanogaster. Biochemical Genetics 17, 867879.CrossRefGoogle ScholarPubMed
Geer, B. W., Lindel, D. L. & Lindel, D. M. (1979 b). Relationship of the oxidative pentose shunt pathway to lipid synthesis in Drosophila melanogaster. Biochemical Genetics 17, 881895.CrossRefGoogle ScholarPubMed
Geer, B. W., McKechnie, S. W. & Langevin, M. L. (1983). Regulation of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster larvae by dietary ethanol and sucrose. Journal of Nutrition 113, 16321642.Google Scholar
Geer, B. W. & Newburgh, R. W. (1970). Carnitine acetyltransferase and spermatozoan development in Drosophila melanogaster. Journal of Biological Chemistry 245, 7179.CrossRefGoogle ScholarPubMed
Geer, B. W.Williamson, J. H., Cavener, D. R. & Cochrane, B. J. (1981). Dietary modulation of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Drosophila. In Current Topics in Insect Endocrinology and Nutrition (ed. Bhaskaran, G., Friedman, S. and Rodriguez, J. G.), pp. 253281. New York: Plenum Publishing Co.Google Scholar
Geer, B. W., Woodward, C. G. & Marshall, S. D. (1978). Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. II. The biochemical basis of dietary carbohydrate and D-glycerate modulation. Journal of Experimental Zoology 203, 391402.Google Scholar
Hizi, A. & Yagil, G. (1974). On the mechanism of glucose-6-phosphate dehydrogenase regulation in mouse liver. 3. The rate of enzyme synthesis and degradation. European Journal of Biochemistry 45, 211221.CrossRefGoogle ScholarPubMed
Kelly, D. S., Watson, J. J., Mack, D. O. & Johnson, B. C. (1975). Glucose-6-phosphate dehydrogenase is not induced in the mammalian liver by dietary carbohydrate. Nutrition Reports International 12, 121135.Google Scholar
Laurie-Ahlberg, C. C., Maroni, G., Bewley, G. C., Lucchesi, J. C. & Weir, B. W. (1980). Quantitative genetic variation of enzyme activities in natural populations of Drosophila melanogaster. Proceedings of the National Academy of Science, USA 77, 10731077.Google Scholar
Laurie-Ahlberg, C. C., Wilton, A. N., Curtsinger, J. W. & Emigh, T. H. (1982). Naturally occurring enzyme activity variation in Drosophila melanogaster. I. Sources of variation for 23 enzymes. Genetics 102, 191206.CrossRefGoogle ScholarPubMed
McKechnie, S. W. & Geer, B. W. (1984). Modulation of alcohol dehydrogenase by dietary ethanol and carbohydrate in Drosophila melanogaster. Insect Biochemistry 14, (In the Press.)CrossRefGoogle Scholar
Oakeshott, J. G., Gibson, J. B., Anderson, P. R., Knibb, W. R., Anderson, D. G. & Chambers, G. K. (1982). Alcohol dehydrogenase and glycerol-3-phosphate dehydrogenase clines in Drosophila melanogaster on different continents. Evolution 36, 8696.CrossRefGoogle ScholarPubMed
O'Brien, S. J. & MacIntyre, R. J. (1978). Genetics and biochemistry of enzymes and specific proteins of Drosophila. In The Genetics and Biology of Drosophila, vol 2 a (ed. Ashburner, M. and Wright, T. R. F.), pp. 396552, New York: Academic Press.Google Scholar
Pette, D., Klingenberg, M. & Bucher, T. (1962 a). Comparable and specific proportions in the mitochondrial enzyme activity pattern. Biochemical and Biophysical Research Communications 7, 425429.Google Scholar
Pette, D., Luh, W. & Bucher, T. (1962 b). A constant-proportion group in the enzyme activity pattern of the Embden-Meyerhof chain. Biochemical and Biophysical Research Communications 7, 419424.CrossRefGoogle ScholarPubMed
Stam, L. F. & Laurie-Ahlberg, C. C. (1982). A semi-automated procedure for the assay of 23 enzymes from Drosophila melanogaster. Insect Biochemistry 12, 537544.Google Scholar
Treat-Clemmons, L. G. & Doane, W. W. (1982). Biochemical loci of the “fruit fly” (Drosophila melanogaster). Isozyme Bulletin 15, 724.Google Scholar
Wilson, S. R., Oakeshott, J. G., Gibson, J. B. & Anderson, P. R. (1982). Measuring selection coefficients affecting the alcohol dehydrogenase polymorphism in Drosophila melanogaster. Genetics 100, 113126.CrossRefGoogle ScholarPubMed
Wilton, A. N., Laurie-Ahlberg, C. C., Emigh, T. H. & Curtsinger, J. W. (1982). Naturally occurring enzyme activity variation in Drosophila melanogaster. II. Relationship among enzymes. Genetics 102, 207221.Google Scholar