Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster

@article{Kreitman1983NucleotidePA,
  title={Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster},
  author={Martin Kreitman},
  journal={Nature},
  year={1983},
  volume={304},
  pages={412-417}
}
The sequencing of eleven cloned Drosophila melanogaster alcohol dehydrogenase (Adh) genes from five natural populations has revealed a large number of previously hidden polymorphisms. Only one of the 43 polymorphisms results in an amino acid change, the one responsible for the two electrophoretic variants (fast, Adh-f, and slow, Adh-s) found in nearly all natural populations. The implication is that most amino acid changes in Adh would be selectively deleterious. 
The population genetics of alcohol dehydrogenase activity in Drosophila melanogaster
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Between and within population variation in ADH activity and AD H protein in flies in the wild is mainly due to the relative frequencies of AdhF and Adhs.
Molecular similarity of Drosophila melanogaster alcohol dehydrogenase thermostable alleles from populations on different continents
Allele specific oligonucleotide probes have been used to show that DNA, amplified by the polymerase chain reaction, from eleven thermostable Adh alleles extracted from populations on different
Persistence of an alcohol dehydrogenase thermostable variant in a natural population of Drosophila melanogaster.
A temporal survey of the alcohol dehydrogenase locus in a natural population of Drosophila melanogaster from the Canary Islands has revealed the existence of an electrophoretic Fast thermostable
Conservation and change in the DNA sequences coding for alcohol dehydrogenase in sibling species of Drosophila
The DNA sequences of the alcohol dehydrogenase (Adh) genes of four very closely related species of Drosophila show that the rates of nucleotide change vary greatly in different functional domains of
Adh Nucleotide Variation in Drosophila willistoni: High Replacement Polymorphism in an Electrophoretically Monomorphic Protein
TLDR
DNA sequence analysis of 18 alleles throughout the distribution of the species has revealed six replacement polymorphisms and the ratio of replacement to silent polymorphisms is higher in D. willistoni than in any other Drosophila species studied for Adh nucleotide variation.
Allele-specific population structure of Drosophila melanogaster alcohol dehydrogenase at the molecular level.
TLDR
The results suggest that the current range of Fast and In(2L)t Slow haplotypes is recent and that an older genetic differentiation between populations was followed by allele-specific gene flow.
Molecular population genetics of an electrophoretically monomorphic protein in the alcohol dehydrogenase region of Drosophila pseudoobscura.
TLDR
The results suggest that the ADH enzyme of D. pseudoobscura lacks amino acid polymorphisms because theneutral mutation rate of nonsynonymous sites is low, and the neutral mutation parameter for synonymous sites is heterogeneous between domains of the Adh region.
Dehydrogenase Locus in the
TLDR
Statistical analyses of the Adh alleles suggested the action of balancing selection and revealed significant linkage disequilibrium among three of the variable sites, and the effective population size was estimated to be only slightly smaller than that of continental species and on the same order of magnitude as the actual size.
An association between ADH protein levels and polymorphic nucleotide variation in the Adh gene of Drosophila melanogaster.
TLDR
Southern analysis of the Adh region of 212 Drosophila melanogaster lines collected from the Tahbilk winery revealed linkage disequilibrium between a 37-bp insertion and the fast electrophoretic variant of alcohol dehydrogenase (ADH-F), suggesting that either polymorphic nucleotide-site variants positively associated with delta 2 on the second chromosome or delta 2 itself increases larval levels of ADH protein.
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