The alcohol dehydrogenase polymorphism of Drosophila melanogaster in relation to environmental ethanol, ethanol tolerance and alcohol dehydrogenase activity

Abstract

Ethanol levels in Drosophila breeding sites were higher in a winery storing fortified wines than in nearby grape pressings or in orchard fruits. The relative abundance of D. simulans to D. melanogaster was negatively correlated with ethanol levels. In D. melanogaster there were no significant differences in AdhF frequency between the orchard and winery populations. The ethanol tolerance of wild caught D. melanogaster males paralleled the levels of ethanol in the breeding sites but Adh alleles and ethanol tolerance segregated largely independently of each other. Levels of ADH activity were positively associated with the ethanol tolerance of the different populations and with levels of ethanol in the breeding sites, but it is argued that the ethanol levels are not causative. Flies from inside the winery had higher ADH levels due mainly to greater amounts of ADH-F. The difference in activity persisted for at least one generation in the laboratory. After ten generations of laboratory culture the differences in ethanol tolerance were still present but there were no significant differences in ADH activity.

Ethanol tolerance and variation at the alcohol dehydrogenase (Adh) locus of Drosophila mauritiana

“…The evidence from breeding sites of wild populations is that D. melanogaster and D. simulans occupy different niches with respect to alcohol concentration (McKenzie & Parsons, 1972;Parsons, 1977Parsons, , 1981Gibson & Wilks, 1988). McKenzie & McKechnie (1979) found only D. inelanogaster larvae when ethanol concentration was about 7 per cent.…”

The alcohol dehydrogenase polymorphism in natural populations of Drosophila melanogaster: ADH activity variation restriction site polymorphism and the Adh cline

“…ADH was assayed in each line using flies from two replicate cultures. To provide similar progeny densities each culture was set up with 20 pairs of flies in 250-mi plastic containers with standard culture medium (Gibson & Wilks, 1988). Two sets of male flies from the progeny of each culture were aged for 5-7 days, weighed and then homogenized in cold 100 mM sodium phosphate buffer (pH 7.5) to a final concentration of 10 mg live weight/mi.…”

“…The ADH enzyme of Drosophila melanogaster has a role in alcohol detoxification, as flies homozygous for Adh null activity alleles do not survive exposure to *Present address: Department of Zoology, Louisiana State University, Baton Rouge, Louisiana, 70803-1725, U.S.A. lTo whom correspondence should be addressed. ethanol levels above 6 per cent (Grell et al, 1968;Freeth et a!., 1986;Van Delden & Kamping, 1988), although the relationship between fitness and variation within the normal range of activity remains controversial (for regions see Van Delden, 1982;Gibson & Wilks, 1988).…”

Allozyme polymorphism at the αGpdh and Adh loci and fitness in Drosophila melanogaster

“…Even so, the key to alcohol detoxification does not depend exclusively upon the ADH catalysis (McKenzie and Parsons, 1974;Oakeshott, 1976;McKenzie and McKechnie, 1978;Gibson et a!., 1981;Van Delden and Kamping, 1983;Oakeshott et a!., 1984a;Kerver and Van Delden, 1985; Gibson and Wilks, 1988).…”