An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila Melanogaster. 11. Post-Electrophoresis Heat-Treatment Screening of Natural Populations

Wilks, Ann Verona; Gibson, JB; Oakeshott, J. G.; Chambers, Geoffrey K.

doi:10.1071/bi9800575

Cited by 49 publications

(30 citation statements)

References 15 publications

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“…As reported by Knibb (1983), F and S were consistently in gametic disequilibrium with In(2L)t: chromosomes carrying In(2L)t generally also bore S. The initial frequencies of the electrophoretically cryptic FCh.D. allele varied between 000 and 005 across the eight base populations and, as reported in Wilks et aL (1980), were not clinally related to latitude. ADH activities were highly correlated with F frequencies (r =086, P <0.001) and, after correction for the covariate effects of F frequencies, did not differ significantly between the eight base populations (F(7gn=O24, P>0O5).…”

Section: Resultsmentioning

confidence: 54%

Selective effects of the genetic background and ethanol on the alcohol dehydrogenase polymorphism in Drosophila melanogaster

1984

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SUMMARYEight freshly caught Australasian mass collections ranging in Adh F frequency from 4 to 96 per cent were each divided into eight selection lines. Two selection lines from each base population were put on one of four types of mediumstandard food supplemented with 0 per cent, 3 per cent, 6 per cent or 9 per cent ethanol. After 30 generations the tolerance of 6 per cent and 9 per cent selection lines on a test dose of 9 per cent ethanol was greater than that of the 0 per cent lines on this dose. The tolerance of the 3 per cent lines on this dose was less than that of the 0 per cent lines. There were no significant differences in the tolerance responses across the eight base populations but in only one did Adh frequencies diverge among the four ethanol selection environments: F frequencies in the Brisbane 9 per cent lines were higher than in the Brisbane 0 per cent, 3 per cent and 6 per cent lines. Although the selection affecting Adh did not generally differ among the four selection environments, it differed highly significantly among the eight base populations. The equilibrium F frequencies predicted from the maximum likelihood estimates of the selection coefficients were in close agreement with the frequencies observed in the original collections. The only aspect of the coefficients which was consistent across base populations was FS heterozygote superiority.

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Section: Resultsmentioning

confidence: 54%

Selective effects of the genetic background and ethanol on the alcohol dehydrogenase polymorphism in Drosophila melanogaster

1984

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“…Thus the results of the latitudinal and climatic analyses for Pgm, like those for Est-6, and indeed for Adh and Gpdh (Wilks et a!., 1980;Oakeshott et a!., 1981) seem unrelated to the in vitro thermostabilities of the relevant allozymes. The thermostability differences may be valuable biochemical tools but their adaptive value for flies in wild populations remains to be established.…”

Section: Resultsmentioning

confidence: 93%

Latitudinal relationships of esterase-6 and phosphoglucomutase gene frequencies in Drosophila melanogaster

et al. 1981

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SUMMARYGeographic variation in Esterase-6 (Est-6) and Phosphoglucomutase (Pgm) gene frequencies in Australasian populations ot Drosophila melanogaster are compared with analogous data collated from 16 previous reports tor North America and Europe/Asia. A large-scale latitudinal dine is found on all three zoogeographic zones for Est-6 and overall, Est-61°°f requency increases from about 20 per cent around 20° latitude to about 80 per cent approaching 50°l atitude. In contrast, there is no consistent evidence for a latitudinal dine in Pgm gene frequencies in any of the three zones, with Pgm1°° frequency generally about 85 per cent and Pgm 1•20 and Pgm°7° frequencies each between 5 per cent and 10 per cent. The consistent Est-6 dines are attributed to latitudinal selection gradients but no consistent correlations are found between Est-6 gene frequencies and maximum or minimum temperature or rainfall which might be associated with these gradients. The directions of the Est-6 dines in tact run counter to expectations based on the in Vitro thermostabilities of the respective allozymes.

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“…Thus, the only major difference in properties between ADH-FCh.D. and ADH-S is that of thermo stability as reported earlier Wilks et al 1980). ADH-FCh.D.…”

Section: Discussionmentioning

confidence: 99%

“…The single-allele Adh F , Adh s and Adh FCh • D • lines of D. meltmagaster were identical with those used as controls in our earlier experiments Wilks et al 1980). All experiments reported here were carried out with crude extracts of 7-day-old adult male flies (10 mg live weight per millilitre of buffer) prepared according to Gibson et al (1980).…”

Section: Melanogaster Stocks and The Preparation Of Enzyme Extractsmentioning

confidence: 99%

“…('fast' Chateau Douglas) and its comparison with the two common forms ADH-F and ADH-S. In earlier reports Wilks et al 1980) it was demonstrated that although the enzyme ADH-FCh.D. has identical electrophoretic mobility to ADH-F on cellulose acetate sheets its substrate specificity is like that of ADH-S. ADH-FCh.D. is distinguished from the two common forms of ADH by being much more heat stable than either of them.…”

Section: Introductionmentioning

confidence: 99%

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An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila melanogaster. III. Biochemical Properties and Comparison with Common Enzyme Forms

Chambers¹,

Wilks²,

Gibson³

1981

Aust. Jnl. Of Bio. Sci.

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The biochemical properties of the heat-stable alcohol dehydrogenase variant ADH-FCh.D. have been investigated and compared with those of the two common enzyme forms ADH-F and ADH-S. The results show that ADH-F and ADH-S differ with respect to substrate specificity, their response to high concentrations of secondary alcohols and their apparent Michaelis constants for three alcohols in two different buffer systems. In all these tests the enzyme ADH-FCh.D. resembles ADH-S much more closely than ADH-F. It is concluded that if natural selection is to distinguish between the alleles Adh s and Adh FCh • D • then it most probably does so on the basis orthe superior thermostability of ADH~FCh.D. The biochemical properties of all three enzymes are discussed in relation to the role of alcohol dehydrogenase in the exploitation of alcohol by D. melanogaster.

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An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila Melanogaster. 11. Post-Electrophoresis Heat-Treatment Screening of Natural Populations

Cited by 49 publications

References 15 publications

Selective effects of the genetic background and ethanol on the alcohol dehydrogenase polymorphism in Drosophila melanogaster

Selective effects of the genetic background and ethanol on the alcohol dehydrogenase polymorphism in Drosophila melanogaster

Latitudinal relationships of esterase-6 and phosphoglucomutase gene frequencies in Drosophila melanogaster

An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila melanogaster. III. Biochemical Properties and Comparison with Common Enzyme Forms

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