Dominance for sn-glycerol-3-phosphate dehydrogenase activity in Drosophila melanogaster: Evidence for differential allelic expression mediated via a trans-acting effect

Gibson, J. B.; Wilks, Ann Verona; Cao, Anh T.; Freeth, Allan L.

doi:10.1038/hdy.1986.35

Cited by 21 publications

(10 citation statements)

References 29 publications

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“…The 1981 and 1982 collections were also scored for sn-glycerol-3-phosphate dehydrogenase (EC 1.1.1.8.) Gpdh genotypes after electrophoresis on cellulose acetate membranes (Gibson et a!., 1986).…”

Section: And Methodsmentioning

confidence: 99%

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

Gibson

Wilks

1988

Heredity

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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.

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Section: And Methodsmentioning

confidence: 99%

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

Gibson

Wilks

1988

Heredity

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“…GPDH electrophoresis on cellulose acetate membranes with a buffer at pH 6.6 was performed according to Gibson et al (1986).…”

Section: Gpdh Electrophoresismentioning

confidence: 99%

Expression of the GPDH-4 isozyme of sn-glycerol-3-phosphate dehydrogenase in three Drosophila species

et al. 1998

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A fourth recently discovered isozyme of sn-glycerol-3-phosphate dehydrogenase (GPDH-4) in Drosophila melanogaster is shown to be a translational product of the Gpdh transcript which contains exons 1 through 7. This transcript was also found in two other Drosophila species, D. busckii and D. virilis. In contrast to D. melanogaster and D. busckii, the Gpdh transcript containing exons 1-6 is absent in D. virilis adults. The reason for this difference between D. virilis and the two other species is intriguing but remains elusive. We have ruled out the possibility that a replacement of an amino acid residue in exon 7 played any role in generating this interspecific variation.

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“…Such elements can operate at all stages of protein synthesis, from transcriptional (Sassone- Corsi and Borrelli, 1986) to post-translational levels (Beevers, 1982). The inheritance of enzyme activity (quantity) has been also studied in some cases (Gibson et al, 1986;Hammer and Wilson, 1987).…”

Section: Introductionmentioning

confidence: 99%

Linkage relationships of loci controlling protein amounts in maritime pine (Pinus pinaster Ait.)

Bahrman

Damerval

1989

Heredity

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Dominance for sn-glycerol-3-phosphate dehydrogenase activity in Drosophila melanogaster: Evidence for differential allelic expression mediated via a trans-acting effect

Cited by 21 publications

References 29 publications

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

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

Expression of the GPDH-4 isozyme of sn-glycerol-3-phosphate dehydrogenase in three Drosophila species

Linkage relationships of loci controlling protein amounts in maritime pine (Pinus pinaster Ait.)

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