We tested a subset of the genes identified by homology above for their ability to metabolize ethanol using an allyl-alcohol toxicity assay that has been previously used extensively to identify mutants with defects in ethanol metabolism in worms and in other organisms (Williamson et al. 1991). Allyl-alcohol is metabolized by ADH into the toxin acrolein, and wild-type worms that are grown on allyl-alcohol plates die within 24 hours, whereas worms with defects in ADH function are resistant to allyl-alcohol toxicity ((Williamson et al., 1991) and Table 1). Inactivation of sodh-1 conferred profound resistance to allyl-alcohol-induced lethality (Table 1). Previously, Williamson et al. (1991) performed a genetic selection using allyl-alcohol survival to isolate mutations in putative ADHs in the worm, and identified AL2B, and we replicated the allyl-alcohol resistance of this mutant (Table 1). We identified a G to A point mutation in sodh-1 in AL2B, which would result in a Glycine 158 to Glutamate missense mutation (for consistency of nomenclature, AL2B is hereafter referred to as sodh-1(bet20)). Additionally, RNA inactivation of H24K24.3 conferred resistance to allyl-alcohol, however, knock-down of function
