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Mammalian pheromone-receptor complexes contain a common set of seven polypeptides, the G-proteins. The exact set of polypeptides present in the complexes of most teleosts is not known. Therefore, it is particularly difficult to study the evolution of these complexes in divergent vertebrate taxa, such as teleosts. Mammalian pheromone-receptor complexes in teleosts are thought to be more complex than G-proteins, as indicated by the presence of a much larger repertoire of odorant receptors and the existence of multiple pheromone-receptor complexes. Furthermore, mammalian pheromone-receptor complexes have only been isolated using antibodies raised against heterologous G-protein alpha-subunits or, more recently, by cloning the pheromone-receptor. In the present study, we used degenerate primers designed from the conserved pheromone-binding sites of the G-proteins of pheromone glands (PGs) of the large yellow croaker Larimichthys crocea (Lc-PGs) to clone cDNAs encoding putative Lc-PGs from a PG cDNA library. As a result, six Lc-PG cDNAs were cloned, three of which contained the binding site of the G-protein alpha-subunits. The results indicate that the Lc-PGs are complex pheromone-receptor complexes, closely resembling the mammalian olfactory pheromone-receptor complexes.Q:

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