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Genet Res. 2006 Apr;87(2):87-92. Epub 2006 Mar 28.

Aldehyde dehydrogenase is essential for both adult and larval ethanol resistance in Drosophila melanogaster.

Author information

1
Department of Biology, University of Rochester, Rochester, NY 14627, USA. jfry@mail.rochester.edu

Abstract

The enzyme aldehyde dehydrogenase (ALDH) is essential for ethanol metabolism in mammals, converting the highly toxic intermediate acetaldehyde to acetate. The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde. Here, we report the creation and characterization of four null mutants of Aldh, the putative structural locus for ALDH. Aldh null larvae and adults are poisoned by ethanol concentrations easily tolerated by wild-types; their ethanol sensitivity is in fact comparable to that of Adh nulls. The results refute the view that ALDH plays only a minor role in ethanol detoxification in larvae, and suggest that Aldh and Adh may be equally important players in the evolution of ethanol resistance in fruit-breeding Drosophila.

PMID:
16566845
DOI:
10.1017/S0016672306008032
[Indexed for MEDLINE]

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