Molecular Biology and Evolution, Vol 16, 839-848, Copyright © 1999 by Society for Molecular Biology and Evolution
ME Hellberg and VD Vacquier
Proteins mediating intercellular recognition face opposing selective forces
as they evolve: purifying selection to maintain function, and diversifying
selection to alter specificity. Lysin is a 16-kDa protein which enables
sperm of free-spawning marine snails to make a hole in the vitelline layer
(VE) surrounding conspecific eggs. Previous work on abalone (Haliotis spp.)
has shown that positive selection promotes rapid interspecific divergence
of lysin. Here, we present data on the specificity of VE dissolution by
four species of teguline gastropods, along with lysin cDNA sequences. The
teguline and abalone lineages diverged over 250 MYA. As in abalone, VE
dissolution by lysin in tegulines is species-selective, and positive
selection promotes rapid interspecific divergence over the entire mature
protein. Nonsynonymous substitution rates, calculated using a mtCOI
molecular clock calibrated by two Tegula species separated by the Isthmus
of Panama, are high (> 25 substitutions per site per 10(9) years).
However, the extensive replacements in teguline lysins are overwhelmingly
conservative with respect to type, charge, and polarity of residues.
Predictions of secondary structure suggest that the size and position of
alpha-helices are also conserved, even through pairwise amino acid
identities between Haliotis rufescens and the different tegulines are less
than 15%.
ORIGINAL ARTICLE
Rapid evolution of fertilization selectivity and lysin cDNA sequences in teguline gastropods
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California, San Diego, USA. mhellbe@lsu.edu
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