ALCOHOL TOLERANCE, ADH ACTIVITY, AND ECOLOGICAL NICHE OF DROSOPHILA SPECIES

@article{Merot1994ALCOHOLTA,
  title={ALCOHOL TOLERANCE, ADH ACTIVITY, AND ECOLOGICAL NICHE OF DROSOPHILA SPECIES},
  author={Herv{\'e} Merçot and Danielle Defaye and Pierre Capy and E Pla and Jean R. David},
  journal={Evolution; International Journal of Organic Evolution},
  year={1994},
  volume={48},
  pages={746 - 757}
}
In vitro alcohol dehydrogenase (ADH) activity was measured in adults of species belonging to Drosophila and to the related genus Zaprionus. Data were analyzed according to the known breeding sites and the level of ethanol tolerance of these species. Alcohol dehydrogenase activity was assayed with both ethanol (E) and isopropanol (I). Our results show a very broad range of activities among the 71 species investigated, the ratio of the highest value observed (D. melanogaster) to the lowest (D… Expand
Shaping of Drosophila Alcohol Dehydrogenase Through Evolution: Relationship with Enzyme Functionality
TLDR
Analysis of amino acid variability found in the 57 protein ADH sequences reported, identified the taxon-specific residues, and localized them in a three-dimensional ADH model defines three regions whose shaping has been crucial for ADH differentiation and would be compatible with a contribution of ADH to Drosophila speciation. Expand
Ethanol Tolerance and Alcohol Dehydrogenase (ADH; EC1.1.1.1) Activity in Species of the cardini Group of Drosophila
TLDR
There were small but significant differences in ethanol tolerance and ADH activity and differences in enzyme mobility were in accordance with the proposedphylogeny for the dunni-subgroup species. Expand
Dietary Ethanol Mediates Selection on Aldehyde Dehydrogenase Activity in Drosophila melanogaster1
TLDR
It is hypothesized that variation in ALDH activity may make an important contribution to the observed wide variation in ethanol tolerance within and among Drosophila species. Expand
ADAPTATION TO FERMENTING RESOURCES IN DROSOPHILA MELANOGASTER: ETHANOL AND ACETIC ACID TOLERANCES SHARE A COMMON GENETIC BASIS
TLDR
The data suggest that alcohol dehydrogenase (ADH) activity does not play a major role in explaining the physiological differences known between Afrotropical and European populations, and the metabolic flux permitting the detoxification of ethanol and acetic acid seems to be mainly controlled by acetyl‐coA synthetase (ACS) at least in adult flies. Expand
Sequence variation of alcohol dehydrogenase (Adh) paralogs in cactophilic Drosophila.
TLDR
A pattern of variation consistent with adaptive protein evolution in the D. mojavensis lineage at Adh-1 is observed, suggesting that the cactus host shift that occurred in the divergence of D. arizonae had an effect on the evolution of the larval expressed paralog. Expand
Microspatial genetic differentiation for tolerance and utilization of various alcohols and acetic acid in Drosophila species from India
TLDR
In five Indian localities, it was possible to collect D. melanogaster in two different types of habitats, namely ordinary domestic and alcohol rich ones, and the population from alcohol rich habitat proved to be more tolerant to all the investigated products and also to beMore capable of using them as a resource. Expand
Phenotypic expression of ADH regulatory genes inDrosophila melanogaster: a comparative study between a paleartic and a tropical population
TLDR
In vitro ADH activity was studied in D. melanogaster males from two sets of third chromosome substitution lines, one from a paleartic population (Gigean, France), the other from a tropical population (Brazzaville, Congo) to interpret variations in both structural and regulatory gene polymorphisms. Expand
Activity variation in alcohol dehydrogenase paralogs is associated with adaptation to cactus host use in cactophilic Drosophila
TLDR
Enzyme activity measurements of the ADH‐2 amino acid polymorphism in D. mojavensis suggest that the Fast allozyme allele has a higher activity on 2‐propanol than 1‐ Propanol, and Examination of protein sequences showed that a large number of amino acid fixations between the paralogs have occurred in catalytic residues, which could be responsible for the significant difference in substrate specificity. Expand
Patterns of natural selection at the Alcohol dehydrogenase gene of Drosophila americana
TLDR
An analysis of selection affecting sequence variation in the Alcohol dehydrogenase (Adh) gene of Drosophila americana shows that if there has been a similar adaptive response to climate in D. americana, it is not within the coding region of Adh, and supports the notion that noncoding sites in Dosophila are often subject to stronger selection pressures than synonymous sites. Expand
Note: Loss of Expression of Alcohol Dehydrogenase in Adult Males of Drosophila pachea
TLDR
It is demonstrated that expression of ADH activity in adult females of D. pachea is not localized in the ovaries and, in addition, it is shown that enzyme activity inAdult males can be induced with short-term exposure to exogenous ethanol. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 51 REFERENCES
Adaptation to alcoholic fermentation in Drosophila species: Relationship between alcohol tolerance and larval habitat
TLDR
It is concluded that the level of ethanol tolerance in Drosophila species cannot be entirely explained by their adaptation to alcoholic resources. Expand
High ethanol tolerance in two distantly related Drosophila species: A probable case of recent convergent adaptation
Abstract 1. D. lebanonensis was found to be more abundant in wine cellars of Spain than outdoors. 2. This suggested that the species could have developed a high alcohol tolerance in a similar way toExpand
Physiological significance of the alcohol dehydrogenase polymorphism in larvae of Drosophila.
TLDR
The findings show that natural selection may act on the Adh polymorphism in larvae via differences in rates of alcohol metabolism, suggesting a compensation for allozymic efficiency by the ADH quantity in D. melanogaster. Expand
Alcohol tolerance and alcohol utilisation in Drosophila: Partial independence of two adaptive traits
TLDR
Three natural populations of D. melanogaster with different ethanol tolerance, and a population of D.'sophila simulans were successfully selected for an increased capacity to withstand alcohol, controlled, at least partly, by different genetic mechanisms. Expand
Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF.
TLDR
The high activity observed with secondary alcohols and especially with (R)-(+)-cis-verbenol, indicates that these flies can metabolize terpenes and may be part of the pheromone system in the flies with D. melanogaster alcohol dehydrogenase playing a role in pherOMone metabolism. Expand
Metabolic control analysis and enzyme variation: nutritional manipulation of the flux from ethanol to lipids in Drosophila.
TLDR
It is suggested that ADH is the major rate-limiting enzyme for the ethanol-to-lipid pathway in Drosophila larvae under the current experimental conditions. Expand
Adaptive response due to changes in gene regulation: a study with Drosophila.
TLDR
Drosophila melanogaster flies selected for increased tolerance to ethanol exhibited higher levels of alcohol dehydrogenase (alcohol:NAD+ oxidoreductase; EC 1.1.1) activity than unselected controls. Expand
ORIGIN AND EXPRESSION OF AN ALCOHOL DEHYDROGENASE GENE DUPLICATION IN THE GENUS DROSOPHILA
TLDR
An alcohol dehydrogenase (Adh) gene duplication associated with a major adaptive radiation within the genus Drosophila within the mulleri subgroup is document. Expand
The involvement of catalase in alcohol metabolism in Drosophila melanogaster larvae.
TLDR
Catalase apparently represents a minor pathway for ethanol degradation in Drosophila melanogaster larvae, but it may be an important route for methanol elimination from D. melanogasters at moderately low dietary concentrations. Expand
Dominance at Adh locus in response of adult Drosophila melanogaster to environmental alcohol
TLDR
The relationship between mortality and genotype at the alcohol dehydrogenase (Adh) locus when adult Drosophila are exposed to environmental ethanol is examined and the highest in vitro activity on starch substrates of all common amylase variants is found. Expand
...
1
2
3
4
5
...