Abstract
This study deals with biochemical and metabolic-physiological aspects of the relationship between variation in in vivo alcohol dehydrogenase activity and fitness in larvae homozygous for the alleles Adh71k, AdhF, AdhS, of Drosophila melanogaster, and for the common Adh allele of Drosophila simulans. The Adh genotypes differ in the maximum oxidation rates of propan-2-ol into acetone in vivo. There are smaller differences between the Adh genotypes in rates of ethanol elimination. Rates of accumulation of ethanol in vivo are negatively associated with larval-to-adult survival of the Adh genotypes. The rank order of the maximum rates of the ADHs in elimination of propan-2-ol, as well as ethanol, is ADH-71k > ADH-F > ADH-S- > simulans-ADH. The ratio of this maximum rate to ADH quantity reveals the rank order of ADH-S > ADH-F > ADH-71k > simulans-ADH, suggesting a compensation for allozymic efficiency by the ADH quantity in D. melanogaster.—Our findings show that natural selection may act on the Adh polymorphism in larvae via differences in rates of alcohol metabolism.
Full Text
The Full Text of this article is available as a PDF (1.4 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Anderson S. M., McDonald J. F. Biochemical and molecular analysis of naturally occurring Adh variants in Drosophila melanogaster. Proc Natl Acad Sci U S A. 1983 Aug;80(15):4798–4802. doi: 10.1073/pnas.80.15.4798. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cavener D. R., Clegg M. T. Evidence for biochemical and physiological differences between enzyme genotypes in Drosophila melanogaster. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4444–4447. doi: 10.1073/pnas.78.7.4444. [DOI] [PMC free article] [PubMed] [Google Scholar]
- David J. R., Van Herrewege J., De Scheemaeker-Louis M., Pla E. Drosophila alcohol dehydrogenase: detoxification of isopropanol and acetone, substances not used in energy metabolism. Heredity (Edinb) 1981 Oct;47(2):263–268. doi: 10.1038/hdy.1981.83. [DOI] [PubMed] [Google Scholar]
- Dickinson W. J., Rowan R. G., Brennan M. D. Regulatory gene evolution: adaptive differences in expression of alcohol dehydrogenase in Drosophila melanogaster and Drosophila simulans. Heredity (Edinb) 1984 Apr;52(Pt 2):215–225. doi: 10.1038/hdy.1984.23. [DOI] [PubMed] [Google Scholar]
- Eisses K. T., Schoonen W. G., Aben W., Scharloo W., Thörig G. E. Dual function of the alcohol dehydrogenase of Drosophila melanogaster: ethanol and acetaldehyde oxidation by two allozymes ADH-71k and ADH-F. Mol Gen Genet. 1985;199(1):76–81. doi: 10.1007/BF00327513. [DOI] [PubMed] [Google Scholar]
- Geer B. W., Langevin M. L., McKechnie S. W. Dietary ethanol and lipid synthesis in Drosophila melanogaster. Biochem Genet. 1985 Aug;23(7-8):607–622. doi: 10.1007/BF00504295. [DOI] [PubMed] [Google Scholar]
- Geer B. W., McKechnie S. W., Langevin M. L. Regulation of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster larvae by dietary ethanol and sucrose. J Nutr. 1983 Aug;113(8):1632–1642. doi: 10.1093/jn/113.8.1632. [DOI] [PubMed] [Google Scholar]
- Heinstra P. W., Aben W. J., Scharloo W., Thörig G. E. Alcohol dehydrogenase of Drosophila melanogaster: metabolic differences mediated through cryptic allozymes. Heredity (Edinb) 1986 Aug;57(Pt 1):23–29. doi: 10.1038/hdy.1986.82. [DOI] [PubMed] [Google Scholar]
- Kacser H., Burns J. A. The molecular basis of dominance. Genetics. 1981 Mar-Apr;97(3-4):639–666. doi: 10.1093/genetics/97.3-4.639. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McDonald J. F., Anderson S. M., Santos M. Biochemical differences between products of the Adh locus in Drosophila. Genetics. 1980 Aug;95(4):1013–1022. doi: 10.1093/genetics/95.4.1013. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thörig E. W., Schoone A. A., Scharloo W. Variation between electrophoretically identical alleles at the alcohol dehydrogenase locus in Drosophila melanogaster. Biochem Genet. 1975 Oct;13(9-10):721–731. doi: 10.1007/BF00484929. [DOI] [PubMed] [Google Scholar]
- Winberg J. O., Hovik R., McKinley-McKee J. S. The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration. Biochem Genet. 1985 Apr;23(3-4):205–216. doi: 10.1007/BF00504319. [DOI] [PubMed] [Google Scholar]
- Winberg J. O., Thatcher D. R., McKinley-McKee J. S. Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Inhibition studies of the alleloenzymes AdhS and AdhUF. Biochim Biophys Acta. 1982 May 21;704(1):17–25. doi: 10.1016/0167-4838(82)90126-1. [DOI] [PubMed] [Google Scholar]
- Winberg J. O., Thatcher D. R., McKinley-McKee J. S. Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF. Biochim Biophys Acta. 1982 May 21;704(1):7–16. doi: 10.1016/0167-4838(82)90125-x. [DOI] [PubMed] [Google Scholar]