A multidisciplinary approach provides new evidence that strongly supports the differentiation of three taxa previously confounded in a single species, Pachycondyla villosa. All specimens studied were collected in the same location at Ilhéus, Bahia, Brazil. Bivariate plots of petiole heights vs. petiole lengths and isozyme patterns clearly differentiate the three taxa. Chain lengths and chemical structures of cuticular hydrocarbons are characteristic of each taxon. This congruent evidence shows that there are three different valid species. Ecological hypotheses are discussed to explain the benefits of these species remaining sympatric. © 2002 The Linnean Society of London, Biological Journal of the Linnean Society, 2002, 75, 249–259.

No abstract

In Drosophila melanogaster, the male ejaculatory bulb is the site of synthesis of a male-specific pheromone, cis-vaccenyl acetate, which functions as both an attractant and an anti-aphrodisiac. This long monounsaturated acetate is structurally similar to a number of shorter gland-synthesized moth pheromones. The cell monolayer that forms the Drosophila male ejaculatory bulb wall is responsible for the production and secretion of cis-vaccenyl acetate into the seminal fluid. When dissected bulbs were incubated with sodium [14-C]-acetate (or deuterated acetate), a labeled acetate ester was synthesized. The labeled acetate ester co-migrated with cis-vaccenyl acetate in thin layer chromatography. Incubation of the abdomens of males from which the ejaculatory bulbs had been removed, or the abdomens of females, with radiolabeled acetate did not yield any acetate ester, but did yield other lipid products, including hydrocarbons. When the isolated labeled acetate ester was hydrolyzed, no radioactive vaccenol was formed. This strongly suggests that the acetyl group is incorporated via a transacetylation reaction, but that the vaccenyl moiety is not synthetized in the blub. The transacetylation enzyme activity was localized in the microsomal subfraction of the bulb homogenate, and its affinity for vaccenol was not very different from that reported for monounsaturated alcohol substrates in moths.