Evolutionary genetics of the Drosophila alcohol dehydrogenase gene-enzyme system

Genetica ◽  
1993 ◽  
Vol 92 (1) ◽  
pp. 1-22 ◽  
Author(s):  
Pieter W. H. Heinstra
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme System ◽  
Evolutionary Genetics ◽  
Dehydrogenase Gene

scholarly journals The Alcohol Dehydrogenase Gene Is Nested in the outspread Locus of Drosophila melanogaster

Genetics ◽  
1996 ◽  
Vol 143 (2) ◽  
pp. 897-911 ◽  
Author(s):  
S McNabb ◽  
S Greig ◽  
T Davis
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Pcr Amplification ◽  
Transcription Unit ◽  
Adjacent Gene ◽  
Dehydrogenase Gene ◽  
Chromosomal Breakpoints ◽  
Splicing Patterns ◽  
Somatic Musculature

Abstract This report describes the structure and expression of the outspread (osp) gene of Drosophila melanogaster. Previous work showed that chromosomal breakpoints associated with mutations of the osp locus map to both sides of the alcohol dehydrogenase gene (Adh), suggesting that Adh and the adjacent gene Adh' are nested in osp. We extended a chromosomal walk and mapped additional osp mutations to define the maximum molecular limit of osp as 119 kb. We identified a 6-kb transcript that hybridizes to osp region DNA and is altered or absent in osp mutants. Accumulation of this RNA peaks during embryonic and pupal periods. The osp cDNAs comprise two distinct classes based on alternative splicing patterns. The 5′ end of the longest cDNA was extended by PCR amplification. When hybridized to the osp walk, the 5′ extension verifies that Adh and Adh' are nested in osp and shows that osp has a transcription unit of ≥74 kb. In situ hybridization shows that osp is expressed both maternally and zygotically. In the ovary, osp is transcribed in nurse cells and localized in the oocyte. In embryos, expression is most abundant in the developing visceral and somatic musculature.

Molecular biology of enzyme adaptations in higher eukaryotes

Genome ◽  
1989 ◽  
Vol 31 (1) ◽  
pp. 272-283 ◽  
Author(s):  
Donal A. Hickey ◽  
Bernhard F. Benkel ◽  
Charalambos Magoulas
Keyword(s):  
Molecular Biology ◽  
Tissue Specificity ◽  
Enzyme System ◽  
Direct Interaction ◽  
Evolutionary Genetics ◽  
Short Term ◽  
Eukaryotic Genes ◽  
Higher Eukaryotes ◽  
The Relationship

Multicellular eukaryotes have evolved complex homeostatic mechanisms that buffer the majority of their cells from direct interaction with the external environment. Thus, in these organisms long-term adaptations are generally achieved by modulating the developmental profile and tissue specificity of gene expression. Nevertheless, a subset of eukaryotic genes are still involved in direct responses to environmental fluctuations. It is the adaptative responses in the expression of these genes that buffers many other genes from direct environmental effects. Both microevolutionary and macroevolutionary patterns of change in the structure and regulation of such genes are illustrated by the sequences encoding α-amylases. The molecular biology and evolution of α-amylases in Drosophila and other higher eukaryotes are presented. The amylase system illustrates the effects of both long-term and short-term natural selection, acting on both the structural and regulatory components of a gene–enzyme system. This system offers an opportunity for linking evolutionary genetics to molecular biology, and it allows us to explore the relationship between short-term microevolutionary changes and long-term adaptations.Key words: gene regulation, molecular evolution, eukaryotes, Drosophila, amylase.

scholarly journals The upstream stimulatory factor binds to and activates the promoter of the rat class I alcohol dehydrogenase gene

1991 ◽  
Vol 266 (23) ◽  
pp. 15457-15463 ◽  
Author(s):  
J.J. Potter ◽  
D. Cheneval ◽  
C.V. Dang ◽  
L.M. Resar ◽  
E. Mezey ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Class I ◽  
Upstream Stimulatory Factor ◽  
Dehydrogenase Gene ◽  
Stimulatory Factor

Preparation of (1R )[1—2H]- and (1S)[1—2H]-Alcohols by Exchange Reactions Catalyzed by Yeast or a Coupled Enzyme System

1973 ◽  
Vol 28 (5-6) ◽  
pp. 241-246 ◽  
Author(s):  
Helmut Günther ◽  
Miguel A. Alizade ◽  
Max Kellner ◽  
Florian Biller ◽  
Helmut Simon
Keyword(s):  
Alcohol Dehydrogenase ◽  
Exchange Reaction ◽  
Enzyme System ◽  
Deuterium Oxide ◽  
Exchange Reactions ◽  
Ordinary Water

All possible enantiomers of stereospecifically labelled [1-2H] ethanol, propanol and butanol have been prepared on a scale of up to 7 ml. The R forms have been obtained by incubation of the alcohols with alcohol dehydrogenase and diaphorase (NAD: Lipoamide oxidoreductase, EC 1.6.4.3) in presence of catalytic amounts of NAD+/NADH in deuterium oxide. The S forms have been prepared with the same enzymes in ordinary water, from the corresponding [1,1-2H] alcohols. (IS) [1-2H] ethanol was prepared from [1,1-2H] ethanol and ordinary water, by a yeast catalyzed exchange reaction.

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