Document Detail

Proteins interacting with the ascidian vitelline-coat sperm receptor HrVC70 as revealed by yeast two-hybrid screening.
MedLine Citation:
PMID:  17393428     Owner:  NLM     Status:  MEDLINE    
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.
Yoshito Harada; Hitoshi Sawada
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular reproduction and development     Volume:  74     ISSN:  1040-452X     ISO Abbreviation:  Mol. Reprod. Dev.     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-07-03     Completed Date:  2007-11-29     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8903333     Medline TA:  Mol Reprod Dev     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1178-87     Citation Subset:  IM    
Sugashima Marine Biological Laboratory, Graduate School of Science, Nagoya University, Sugashima, Toba, Japan.
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MeSH Terms
Amino Acid Sequence
DNA, Complementary / genetics
Egg Proteins / analysis,  genetics,  metabolism*
Molecular Sequence Data
Protein Interaction Mapping
RNA, Messenger / analysis,  metabolism
Receptors, Cell Surface / analysis,  metabolism*
Two-Hybrid System Techniques
Urochordata / metabolism*
Vitelline Membrane / metabolism*
Reg. No./Substance:
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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