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J. Biol. Chem., Vol. 276, Issue 10, 6913-6921, March 9, 2001
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From the SVS VII, one of seven major proteins in mouse
seminal vesicle secretion, was purified to homogeneity. Neither
glycoconjugate nor free thiol group was detected in the protein. The
primary structure deduced from the corresponding cDNA was confirmed
using amino acid sequence determination, which supported the
finding that SVS VII consists of 76 amino acid residues with
five disulfide bridges. Accordingly, it has a theoretical molecular
mass of 8538, which was proven using the mass spectrum of SVS VII. The
CD spectrum of SVS VII in 50 mM phosphate buffer at
pH 7.4 appeared as one negative band arising from the The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF134204.
A Novel Heat-labile Phospholipid-binding Protein, SVS VII, in
Mouse Seminal Vesicle as a Sperm Motility Enhancer*
§,, and¶
Institute of Biochemical Sciences, College
of Science, National Taiwan University, Taipei 106, Taiwan and
the ¶ Institute of Biological Chemistry, Academia Sinica,
Taipei 106, Taiwan
form at 217 nm and several fine structures due to nonpeptide chromophores including
a prominent band for the disulfide bond at 250 nm. This,
together with the predicted secondary structures, indicated no helices
but a mixture of form, turn, and unordered form in SVS VII. A
cytochemical study illustrated the presence of the SVS VII-binding
region on the entire surface of mouse sperm. The SVS VII-sperm binding
was inhibited by the dispersed sperm lipids. The results of TLC overlay assay for the binding of 125I-SVS VII to phospholipids and
the interaction between SVS VII and phospholipid liposomes demonstrated
a specific binding of this protein to both phosphatidylethanolamine and
phosphatidylserine. The SVS VII-sperm binding greatly enhanced sperm
motility but did not induce sperm capacitation. Heating the protein
solution for 10 min at 90 °C unfolded the protein molecule, and the
unfolded SVS VII immobilized the sperm.
*
This work was supported in part by National Science Council,
Taipei, Taiwan (grants NSC 89-2311-B-002-038 and NSC
89-2311-B-001-106).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Institute of
Biochemical Sciences, College of Science, National Taiwan University, P.O. Box 23-106, Taipei 106, Taiwan. Tel.: 886-2-2362-0261; Fax: 886-2-2363-5038; E-mail: mrlab@ccms.ntu.edu.tw or
bc304@gate.sinica.edu.tw.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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