Functional flexibility as a prelude to signal diversity?: Role of a fatty acyl reductase in moth pheromone evolution

Sex pheromones are the hallmark of reproductive behavior in moths. Mature females perform the task of mate signaling and release bouquets of odors that attract conspecific males at long range. The pheromone chemistry follows a relatively minimal design but still the combinatorial action of a handful of specialized pheromone production enzymes has resulted in remarkably diverse sexual signals that subtly vary in structure and in number and ratio of components. In a recent article,1 we showed that a single reductase gene (pgFAR) enables the conversion of key biosynthetic fatty-acyl precursors into fatty alcohols, the immediate precursors of the multi-component pheromone in small ermine moths (Lepidoptera: Yponomeutidae). In the light of the widespread usage of multi-component pheromone blends across Lepidoptera, it is likely that the pgFAR biochemical flexibility is a regular feature of the moth pheromone machinery and polyvalent reductase genes are emerging as pivots to promote phenotypic transitions in moth mating signals. In addition, the small ermine moth pgFAR nevertheless contributes to regulating the ratio among components. Here we show that the pgFAR substrate specificity is actually counterbalancing the inherent chain-length preference of an upstream desaturase with Δ11-activity and that the enzymes together modulate the final blend ratio between the Z11-16:OH, Z11-14:OH and E11-14:OH compounds before the final acetylation.