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Characterization of the sperm molecule bindin in the sea urchin genus Paracentrotus.
Calderón I
,
Turon X
,
Lessios HA
.
???displayArticle.abstract??? Bindin is a sea urchin gamete-recognition protein that plays an essential role in the specificity of egg-sperm interactions and thus may be evolving under sexual selection and be related to speciation. Bindin has been found to evolve under strong selection in some sea urchin genera and neutrally in others. In this study, we characterized bindin in the two extant species of the genus Paracentrotus: P. lividus from the Atlanto-Mediterranean region and P. gaimardi from Brazil. The structure of the bindin molecule in Paracentrotus is similar to that of other genera studied thus far, consisting of a conserved core flanked by two variable regions and an intron of variable length located at the same conserved position as in other genera. Polymorphism in P. lividus is caused mainly by point substitutions and insertions/deletions, and length variations are caused mainly by the number of repeated motifs in the flanking regions. There is no evidence of recombination. Positive selection is acting on amino acid sites located in two regions flanking the conserved core.
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