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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-31
    Description: Gamete interactions during fertilization exhibit species specificity. In abalone, the sperm protein lysin species-specifically creates a hole in the egg envelope. Lysin evolves rapidly by positive Darwinian selection. Evolution of the egg receptor for lysin provides the selective pressure for lysin's divergence. The egg receptor for lysin is a tandemly repeated sequence that evolves by concerted evolution. Concerted evolution in the egg receptor could explain the rapid, adaptive evolution in sperm lysin and may provide an underlying molecular mechanism that gives rise to species-specific fertilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swanson, W J -- Vacquier, V D -- HD12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 31;281(5377):710-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA 92093-0202, USA. jwswanson@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9685267" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Egg Proteins/chemistry/*genetics/metabolism ; *Evolution, Molecular ; Female ; Introns ; Male ; Molecular Sequence Data ; Mollusca/chemistry/*genetics/physiology ; Mucoproteins/chemistry/genetics/*metabolism ; Ovum/chemistry/physiology ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Repetitive Sequences, Nucleic Acid ; Selection, Genetic ; Sequence Alignment ; Species Specificity ; Sperm-Ovum Interactions ; Spermatozoa/chemistry/physiology ; Vitelline Membrane/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-09-25
    Description: REVIEW Although fertilization has been studied for more than a century, the cell surface proteins mediating the process are only now becoming known. Gamete interaction in animals appears to be molecularly complex. Although it is difficult to generalize at present, diversity of structure may be a recurring theme in the evolution of fertilization proteins. Examples of rapid evolution of fertilization proteins by positive selection are known, and concerted evolution can influence the differentiation of gamete recognition proteins between closely related species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vacquier, V D -- HD 12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):1995-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748153" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Egg Proteins/chemistry/genetics/metabolism ; *Evolution, Molecular ; Female ; *Fertilization ; Male ; *Membrane Proteins/chemistry/genetics/physiology ; Mucoproteins/chemistry/genetics/metabolism ; Receptors, Cell Surface/chemistry/genetics/metabolism ; Selection, Genetic ; Sperm-Ovum Interactions
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-02-15
    Description: Extracellular factors from the sea urchin egg induce a change in the electrophoretic mobility of an abundant sperm membrane phosphoprotein. The modified protein was identified as guanylate cyclase. The mobility shift of the cyclase was shown to be associated with a decrease in its enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ward, G E -- Garbers, D L -- Vacquier, V D -- HD-10254/HD/NICHD NIH HHS/ -- HD-12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):768-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Enzyme Activation ; Female ; Fertilization ; Guanylate Cyclase/*metabolism ; Male ; Membrane Proteins/metabolism ; Molecular Weight ; Phosphoproteins/metabolism ; Sea Urchins ; Sperm Maturation ; *Sperm-Ovum Interactions ; Spermatozoa/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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