Extraordinary intraspecific diversity in oyster sperm bindin

In free-spawning invertebrates sperm–egg incompatibility is a barrier to mating between species, and divergence of gamete recognition proteins (GRPs) can result in reproductive isolation. Of interest are processes that create reproductive protein diversity within species, because intraspecific varia...

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Published in:Proceedings of the National Academy of Sciences
Main Authors: Moy, G. W., Springer, S. A., Adams, S. L., Swanson, W. J., Vacquier, V. D.
Format: Text
Language:English
Published: National Academy of Sciences 2008
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538870
http://www.ncbi.nlm.nih.gov/pubmed/18268333
https://doi.org/10.1073/pnas.0711862105
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spelling ftpubmed:oai:pubmedcentral.nih.gov:2538870 2023-05-15T15:58:43+02:00 Extraordinary intraspecific diversity in oyster sperm bindin Moy, G. W. Springer, S. A. Adams, S. L. Swanson, W. J. Vacquier, V. D. 2008-02-12 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538870 http://www.ncbi.nlm.nih.gov/pubmed/18268333 https://doi.org/10.1073/pnas.0711862105 en eng National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538870 http://www.ncbi.nlm.nih.gov/pubmed/18268333 http://dx.doi.org/10.1073/pnas.0711862105 © 2008 by The National Academy of Sciences of the USA Biological Sciences Text 2008 ftpubmed https://doi.org/10.1073/pnas.0711862105 2013-09-02T05:31:28Z In free-spawning invertebrates sperm–egg incompatibility is a barrier to mating between species, and divergence of gamete recognition proteins (GRPs) can result in reproductive isolation. Of interest are processes that create reproductive protein diversity within species, because intraspecific variants are potentially involved in mate choice and early speciation. Sperm acrosomes of the Pacific oyster Crassostrea gigas contain the protein bindin that bonds sperm to egg during fertilization. Oyster bindin is a single-copy gene encoding a diversity of protein variants. Oyster bindins have a conserved N-terminal region followed by one to five tandem fucose-binding lectin (F-lectin) domains. These repeats have diversified by positive selection at eight sites clustered on the F-lectin's fucose binding face. Additional bindin variants result from recombination in an intron in each F-lectin repeat. Males also express alternatively spliced bindin cDNAs with one to five repeats, but typically translate only one or two isoforms into protein. Thus, positive selection, alternative splicing, and recombination can create thousands of bindin variants within C. gigas. Models of sexual conflict predict high male diversity when females are diverse and sexual conflict is strong. The amount of intraspecific polymorphism in male GRPs may be a consequence of the relative efficiency of local (molecular recognition) and global (electrical, cortical, and physical) polyspermy blocks that operate during fertilization. Text Crassostrea gigas Pacific oyster PubMed Central (PMC) Pacific Proceedings of the National Academy of Sciences 105 6 1993 1998
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Biological Sciences
spellingShingle Biological Sciences
Moy, G. W.
Springer, S. A.
Adams, S. L.
Swanson, W. J.
Vacquier, V. D.
Extraordinary intraspecific diversity in oyster sperm bindin
topic_facet Biological Sciences
description In free-spawning invertebrates sperm–egg incompatibility is a barrier to mating between species, and divergence of gamete recognition proteins (GRPs) can result in reproductive isolation. Of interest are processes that create reproductive protein diversity within species, because intraspecific variants are potentially involved in mate choice and early speciation. Sperm acrosomes of the Pacific oyster Crassostrea gigas contain the protein bindin that bonds sperm to egg during fertilization. Oyster bindin is a single-copy gene encoding a diversity of protein variants. Oyster bindins have a conserved N-terminal region followed by one to five tandem fucose-binding lectin (F-lectin) domains. These repeats have diversified by positive selection at eight sites clustered on the F-lectin's fucose binding face. Additional bindin variants result from recombination in an intron in each F-lectin repeat. Males also express alternatively spliced bindin cDNAs with one to five repeats, but typically translate only one or two isoforms into protein. Thus, positive selection, alternative splicing, and recombination can create thousands of bindin variants within C. gigas. Models of sexual conflict predict high male diversity when females are diverse and sexual conflict is strong. The amount of intraspecific polymorphism in male GRPs may be a consequence of the relative efficiency of local (molecular recognition) and global (electrical, cortical, and physical) polyspermy blocks that operate during fertilization.
format Text
author Moy, G. W.
Springer, S. A.
Adams, S. L.
Swanson, W. J.
Vacquier, V. D.
author_facet Moy, G. W.
Springer, S. A.
Adams, S. L.
Swanson, W. J.
Vacquier, V. D.
author_sort Moy, G. W.
title Extraordinary intraspecific diversity in oyster sperm bindin
title_short Extraordinary intraspecific diversity in oyster sperm bindin
title_full Extraordinary intraspecific diversity in oyster sperm bindin
title_fullStr Extraordinary intraspecific diversity in oyster sperm bindin
title_full_unstemmed Extraordinary intraspecific diversity in oyster sperm bindin
title_sort extraordinary intraspecific diversity in oyster sperm bindin
publisher National Academy of Sciences
publishDate 2008
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538870
http://www.ncbi.nlm.nih.gov/pubmed/18268333
https://doi.org/10.1073/pnas.0711862105
geographic Pacific
geographic_facet Pacific
genre Crassostrea gigas
Pacific oyster
genre_facet Crassostrea gigas
Pacific oyster
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538870
http://www.ncbi.nlm.nih.gov/pubmed/18268333
http://dx.doi.org/10.1073/pnas.0711862105
op_rights © 2008 by The National Academy of Sciences of the USA
op_doi https://doi.org/10.1073/pnas.0711862105
container_title Proceedings of the National Academy of Sciences
container_volume 105
container_issue 6
container_start_page 1993
op_container_end_page 1998
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