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Significance Acyl-homoserine lactone (AHL) quorum sensing (QS) has received interest as a possible target for controlling microbial activities and as a model for communication involved in coordinating activities of bacteria. Recent advances show there are two related families of AHL QS signal synthesis enzymes, which differ in whether they acquire the organic acid reaction substrate from biosynthetic or primarily catabolic pathways. Most known AHL synthases utilize fatty acids activated with an acyl carrier protein from fatty acid biosynthesis. Some AHL synthases use coenzyme-A–activated organic acids. We describe a coenzyme-A–dependent AHL synthase QS system. We also set forth an experimental approach for discovering new signals that will allow further expansion of our understanding of the diversity of AHL signaling.

An aryl-homoserine lactone quorum-sensing signal produced by a dimorphic prosthecate bacterium