Female preferences in a fish genus without female mate choice.

The evolution and the adaptive logic (if any) of female mate choice are subjects of lively debate. Whereas most researchers believe that females have evolved to recognize signs of male 'quality' (the ability to provide females or their offspring with direct or indirect genetic or material benefits), there is intriguing evidence that males can evolve to appeal to pre-existing female preferences. Evidence for these pre-existing biases is often ambiguous because phylogenetic reconstructions have usually failed to establish conclusively whether the female preference or the favored male traits evolved first. This potential difficulty is minimal in the mosquitofish genus Gambusia, none of whose 45 species appears to have a female-choice mating system in the wild, and none of which shows the male behavioral and morphological traits that are characteristic of female choice. Nevertheless, in an experimental situation in the laboratory, female Gambusia holbrooki readily chose between models of males and demonstrated significant and reliable preferences for a variety of exaggerated male traits that are not seen in their species or their genus. Other morphological alterations were not preferred. The latent willingness of females to choose traits in a genus without such traits and without evident female choice in the wild is remarkable and may indicate a pre-existing bias in females that is ready to drive male evolution, should the social system or the ecological variables that control it change.

Immunological characterization and transmembrane topology of 5-hydroxytryptamine3 receptors by functional epitope tagging.

5-Hydroxytryptamine3 (5-HT3) receptors are the only known monoamine receptors mediating fast excitatory responses in mammalian neurons. Their primary structure as well as their electrophysiological and pharmacological properties show a phylogenetic relation to nicotinic acetylcholine, GABAA, and glycine receptors. As a prototypical member of this gene superfamily, we investigated the membrane topology of functional homomeric 5-HT3 receptors by using epitope tagging of the channel subunits expressed in heterologous systems. Visualization of 5-HT3 receptors in transfected COS-7 cells, either in western blot (molecular mass 61.2 +/- 0.8 kDa) or in situ, was performed with previously characterized antibodies recognizing artificial epitopes as well as with anti-fusion protein antibodies directed against a wild-type receptor intracellular domain. The extracellular location of the distal C-terminal tagged domain demonstrates the presence of a fourth transmembrane domain in 5-HT3 serotonin-gated channels. In this region, the significant homology between members of this class of neurotransmitter-gated channels suggests strongly that they have a common transmembrane organization basically different from glutamate-gated and ATP-gated channels.