» Articles » PMID: 103098

Structural Analysis of the ADHS Electromorph of Drosophila Melanogaster

Overview
Specialty Science
Date 1978 Nov 1
PMID 103098
Citations 23
Authors
Affiliations
Soon will be listed here.
Abstract

Population geneticists have often determined the fitness differences that account for the dynamics of naturally occurring genetic polymorphisms. However, to understand causal aspects of evolutionary processes requires, in addition, investigation of the physiological and molecular structural differences underlying adaptively significant genetic polymorphisms. The characteristics of the alcohol dehydrogenase gene--enzyme system in Drosophila melanogaster make it well suited for this kind of study. Natural populations of this species are polymorphic for two electrophoretically detectable variants, ADHF and ADHS, of the enzyme. Structural studies reported here reveal that the two variants differ by (at least) a single amino acid replacement, threonine in ADHF for lysine in ADHS.

Citing Articles

Sequence variation of alcohol dehydrogenase (Adh) paralogs in cactophilic Drosophila.

Matzkin L, Eanes W Genetics. 2003; 163(1):181-94.

PMID: 12586706 PMC: 1462434. DOI: 10.1093/genetics/163.1.181.


Deletion of a conserved regulatory element in the Drosophila Adh gene leads to increased alcohol dehydrogenase activity but also delays development.

Parsch J, Russell J, Beerman I, Hartl D, Stephan W Genetics. 2000; 156(1):219-27.

PMID: 10978287 PMC: 1461225. DOI: 10.1093/genetics/156.1.219.


A highly conserved sequence in the 3'-untranslated region of the drosophila Adh gene plays a functional role in Adh expression.

Parsch J, Stephan W, Tanda S Genetics. 1999; 151(2):667-74.

PMID: 9927459 PMC: 1460503. DOI: 10.1093/genetics/151.2.667.


Substrate and inhibitor specificities of the thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster.

Eisses K, Davies S, Chambers G Biochem Genet. 1994; 32(3-4):91-103.

PMID: 7980388 DOI: 10.1007/BF00554418.


Genetic polymorphism: from electrophoresis to DNA sequences.

Ayala F Experientia. 1983; 39(8):813-23.

PMID: 6873231 DOI: 10.1007/BF01990397.


References
1.
ODonnell J, Gerace L, Leister F, Sofer W . Chemical selection of mutants that affect alcohol dehydrogenase in Drosophila. II. Use of 1-pentyne-3-ol. Genetics. 1975; 79(1):73-83. PMC: 1213261. DOI: 10.1093/genetics/79.1.73. View

2.
McDonald J, Ayala F . Genetic and biochemical basis of enzyme activity variation in natural populations. I. Alcohol dehydrogenase in Drosophila melanogaster. Genetics. 1978; 89(2):371-88. PMC: 1213843. DOI: 10.1093/genetics/89.2.371. View

3.
Crestfield A, Moore S, STEIN W . The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963; 238:622-7. View

4.
Davis B . DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964; 121:404-27. DOI: 10.1111/j.1749-6632.1964.tb14213.x. View

5.
Mendez E, Lai C . Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975; 68(1):47-53. DOI: 10.1016/0003-2697(75)90677-6. View