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

Published online by Cambridge University Press:  28 March 2006

JAMES D. FRY  and
MOLLY SAWEIKIS
JAMES D. FRY
Affiliation:
Department of Biology, University of Rochester, Rochester, NY 14627, USA
MOLLY SAWEIKIS
Affiliation:
Department of Biology, University of Rochester, Rochester, NY 14627, USA
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Abstract

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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.

Type
Research Article
Information
Genetics Research , Volume 87 , Issue 2 , April 2006 , pp. 87 - 92
Copyright
2006 Cambridge University Press