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J Biol Chem, Vol. 273, Issue 27, 16748-16755, July 3, 1998

Membrane Fusion Is Induced by a Distinct Peptide Sequence of the Sea Urchin Fertilization Protein Bindin

Anne S. Ulrich, Marlies Otter^¶, Charles G. Glabe, and Dick Hoekstra^¶

From the  Institute of Molecular Biology, University of Jena, Winzerlaer Strasse 10, 07745 Jena, Germany, the ^¶ Department of Physiological Chemistry, University of Groningen, Deusinglaan 1, 9713 AV Groningen, The Netherlands, and the  Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92717

Fertilization in the sea urchin is mediated by the membrane-associated acrosomal protein bindin, which plays a key role in the adhesion and fusion between sperm and egg. We have investigated the structure/function relationship of an 18-amino acid peptide fragment "B18," which represents the minimal membrane binding motif of the protein and resembles a putative fusion peptide. The peptide was found to mimic the behavior of its parent protein bindin with respect to (a) its high affinity for lipid bilayers, (b) the ability to aggregate and fuse vesicles, (c) the binding of Zn²⁺ by a histidine-rich motif, (d) the tendency to self-assemble, and (e), as indicated earlier, the adhesion to cell surface polysaccharides. Fluorescence and light scattering assays were used here to monitor peptide-induced lipid mixing, leakage, and aggregation of large unilamellar sphingomyelin/cholesterol vesicles. For these activities, B18 requires the presence of Zn²⁺ ions, with which it forms oligomeric complexes and assumes a partially -helical conformation, as observed by circular dichroism. We conclude that aggregation and fusion involves a "trans-complex" between peptides on apposing vesicles that are connected by Zn²⁺ bridges.

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