The Drosophila Alcohol Dehydrogenase Gene–Enzyme System

Chambers, Geoffrey K.

doi:10.1016/s0065-2660(08)60458-7

Cited by 84 publications

(53 citation statements)

References 275 publications

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“…Lipid content is related to resistance to starvation (David et a!., 1983;Zwaan et a!., 1991) and viability and fecundity (Clark, 1989). As heterozygote effects are supposed to play an important role in the maintenance of the polymorphism of both Adh and aGpdh in nature (Bijlsma-Meeles & Bijisma, 1988;Chambers, 1988), our data fit well. We have planned further research on these traits.…”

Section: Discussionsupporting

confidence: 72%

“…This difference is well known from the literature (see review by Chambers, 1988): in Drosophila melanogaster strains that carry the Adhs allele generally have lower ADH activity levels than lines with Adh' alleles, which is largely accounted for by differences in protein level. We found no differences in a GPDH enzyme activity between aGpdh genotypes.…”

Section: Discussionmentioning

confidence: 90%

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Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

et al. 1991

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The role of developmental time in the world-wide dine of Adh and a Gpdh allele frequencies of Drosophila melanogaster, and the relationship with weight and some biochemical characters, were investigated. Experimental strains were constructed with different combinations of Adh and aGpdh alleles but with similar genetic background. Developmental time, adult weight, protein-and triglyceride-content, and ADH and aGPDH enzyme activity were measured at a rearing temperature of 20, 25 and 29°C. Genotype effects were found in all studied characters. In general the developmental times of genotypes were: Ad/IFF < Adh' a GpdhFS = aGpdhSS. Developmental time and adult weight were strongly affected by rearing temperature.Triglyceride content and ADFI and a GPDH enzyme activity were slightly affected by temperature. Interactions between genotype and temperature effects were found for developmental rate, adult weight and protein content. No trade off was observed between developmental time on the one hand and adult weight, protein-and triglyceride-content, and ADH and a GPDH enzyme activity on the other hand. It is argued that developmental rate differences might be one of the underlying mechanisms of the world-wide dine of the Adh and a GPdh allele frequencies.Keywords: Adh, a Gpdh, developmental time, Drosophila melanogaster, temperature, weight. IntroductionThe alcohol dehydrogenase (Adh) and a-glycerophosphate dehydrogenase (a Gpdh) loci are two of the most extensively studied allozyme systems of Drosophila melanogaster. They provide an excellent opportunity to study interactions between physiological effects of gene-enzyme systems. Both loci have two common electrophoretic alleles: AdhF, Adhs, aGpdh' and aGpdhS. Nearly all natural populations are polymorphic for both loci. The frequencies of these alleles show world-wide clinal variation: the frequencies of Adhs and aGpdhF decrease with increasing latitude (Oakeshott et al., 1982). An important question is whether these dines are under the control of natural selection. Correlation analysis of climatic data revealed no consistent significant correlations (Anderson et a!., 1987). In the laboratory, stress from alcohol or temperature can cause differential selection of Adh and aGpdh alleles (e.g. Van Delden, 1982; Zera et a!., 1985). Under normal laboratory conditions equilibrium selection has been demonstrated for Adh (Bijisma-Meeles & Bijlsma, 1988) and aGpdh (Palabost-Charles, 1980). Selection at temperatures between 25 and 30°C may lead to an increase of the Adhs and aGpdh' alleles (Alahiotis, 1982;Van Delden, 1984). Vigue et al. (1982) and Oakeshott et al. (1985), however, found no effect of temperature on Adh or aGpdh allele frequencies. Van Delden (1984) and Van Delden & Kamping (1989) ascribe the advantage of the Adhs and aGpdhF alleles at a higher temperature, for the greater part, to linkage of both alleles with the inversion In(2L)t.Differences in developmental time between genotypes may be an important underlying mechanism of selection. D...

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Section: Discussionsupporting

confidence: 72%

Section: Discussionmentioning

confidence: 90%

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

et al. 1991

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“…Especially for Adh, there is a large body of data on this issue, derived from both field observations and laboratory experiments (for review, see e.g. Chambers, 1988). Even with the low interpopulation differentiation, shown in the present study, the Adh allele frequencies exhibited a statistically significant regression on latitude and the temperature of the hottest month.…”

Section: Discussioncontrasting

confidence: 46%

“…In vitro analysis of thermostabilities and kinetic properties of allozymes under different temperatures yielded results which were frequently in contrast with what could be expected from the existent geographical and seasonal variation (see e.g. Zera et at., 1984 andChambers, 1988 for reviews; Oakeshott et al, 1983a and White et a!., 1988 for discussions). Therefore, it was hypothesized that temperature had also various indirect effects on allozyme genotypes.…”

Section: Discussionmentioning

confidence: 99%

Variation of allozyme loci in populations of Drosophila melanogaster from the former USSR

Bubli

Rakitskaya²,

Imasheva³

1996

Heredity

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“…This duplication is clearly very old, perhaps as old as 180 Myr (Russo, Takezaki, and Nei 1995). The function of Adh is well known: it is the detoxification of dietary alcohols (Chambers 1988;Ashburner 1998). Adhr is of unknown function, although it seems not to be a NAD-dependent dehydrogenase (Jeffs, Holmes, and Ashburner 1994).…”

Section: Introductionmentioning

confidence: 99%

Duplication, Dicistronic Transcription, and Subsequent Evolution of the Alcohol dehydrogenase and Alcohol dehydrogenase-related Genes in Drosophila

Betrán

Ashburner

2000

Molecular Biology and Evolution

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It has recently been discovered that the Alcohol dehydrogenase and Alcohol dehydrogenase-related genes of Drosophila melanogaster and closely related species constitute a single transcription unit and that the Alcohol dehydrogenase-related gene is exclusively expressed from a dicistronic mRNA. Here, we show that in Drosophila lebanonensis, subgenus Scaptodrosophila, Adhr is also transcribed as a dicistronic transcript with Adh. Using degenerate primers designed on the sequence of the known ADHR proteins, we have been able to amplify and sequence a partial sequence of Adhr in species representative of the whole subgenus Drosophila. This has allowed the study of the organization and expression of Adhr in Drosophila buzzatii. We find that in D. buzzatii Adhr is transcribed as a monocistronic transcript. Adh and Adhr are believed to originate by duplication, and our data suggest that the cotranscription of these two genes was the primitive state, and that their independent transcription in the subgenus Drosophila is derived. We can rationalize the D. buzzatii condition as being correlated with the two genes evolving independent transcriptional control. However, why these two genes with clear divergence in the functions of their proteins should remain cotranscribed in groups as divergent as the subgenus Sophophora and the subgenus Scaptodrosophila remains a mystery.

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The Drosophila Alcohol Dehydrogenase Gene–Enzyme System

Cited by 84 publications

References 275 publications

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

Polymorphism at the Adh and αGpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters

Variation of allozyme loci in populations of Drosophila melanogaster from the former USSR

Duplication, Dicistronic Transcription, and Subsequent Evolution of the Alcohol dehydrogenase and Alcohol dehydrogenase-related Genes in Drosophila

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