| Proteins interacting with the ascidian vitelline-coat sperm receptor HrVC70 as revealed by yeast two-hybrid screening. | |
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MedLine Citation:
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PMID: 17393428 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ascidians are hermaphrodites releasing sperm and eggs nearly simultaneously, but many species are self sterile. We have previously reported that HrVC70 consisting of 12 EGF-like repeats is a major component of the vitelline coat, functioning as a self/nonself-recognizable sperm receptor during fertilization of the ascidian Halocynthia roretzi. Here, in order to identify the binding partner of HrVC70, we explored HrVC70-interacting proteins by yeast two-hybrid screening. HrVC70 is capable of interacting with HrVC70 precursor HrVC120 itself and also with three additional extracellular and/or transmembrane proteins, HrVLP-1, -2, and HrTTSP-1. Specific interaction of HrVC120, HrVLP-1, -2, and HrTTSP-1 with HrVC70 was confirmed by exchanging prey and bait, and also by a pulldown assay using the GST-fusion proteins. HrVLP-1 and -2 are proteins structurally related to HrVC120; both are expressed in the oocytes and may be novel components of the ascidian vitelline coat. HrTTSP-1 appears to be a member of the serine protease family with type II transmembrane topology. HrTTSP-1 is expressed in the testis and its gene product contains multiple conserved motifs known to be involved in protein-protein or protein-carbohydrate interactions. Close inspection revealed that the protease domain of HrTTSP-1 is considerably divergent, in particular around the region of the catalytic center Ser residue. Possible roles of these proteins in ascidian fertilization are also discussed. |
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Authors:
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Yoshito Harada; Hitoshi Sawada |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular reproduction and development Volume: 74 ISSN: 1040-452X ISO Abbreviation: Mol. Reprod. Dev. Publication Date: 2007 Sep |
Date Detail:
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Created Date: 2007-07-03 Completed Date: 2007-11-29 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8903333 Medline TA: Mol Reprod Dev Country: United States |
Other Details:
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Languages: eng Pagination: 1178-87 Citation Subset: IM |
Affiliation:
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Sugashima Marine Biological Laboratory, Graduate School of Science, Nagoya University, Sugashima, Toba, Japan. yharada@bio.nagoya-u.ac.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals DNA, Complementary / genetics Egg Proteins / analysis, genetics, metabolism* Female Fertilization Male Molecular Sequence Data Protein Interaction Mapping RNA, Messenger / analysis, metabolism Receptors, Cell Surface / analysis, metabolism* Two-Hybrid System Techniques Urochordata / metabolism* Vitelline Membrane / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/DNA, Complementary; 0/Egg Proteins; 0/RNA, Messenger; 0/Receptors, Cell Surface; 0/egg surface sperm receptor; 0/vitelline membrane proteins |
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