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3% of all amino acids in mouse and bull SMCP, respectively. The high content of cysteine residues responsible for the formation of disulﬁde bonds may explain why disulﬁde bond reduction is required to obtain the binding of ubiquitin-speciﬁc antibodies to the mitochondrial sheath of ejaculated (see Fig. 6A), but not testicular, spermatozoa. Disulﬁde bond cross-linking occurring during epididymal maturation lends rigidity to the mitochondrial sheath of the mammalian spermatozoa (Bed- 34 PETER SUTOVSKY AND GERALD SCHATTEN ford, 1979).
1994; Stearns and Kirschner, 1994). Other factors are likely to contribute to the release of the sperm-borne centriole from the connecting piece into the zygotic cytoplasm. , 1998) and possibly other protein kinase substrates. , 1997). The release of Ca2ϩ ions into oocyte cytosol at fertilization may affect the conformation PATERNAL CONTRIBUTIONS TO THE MAMMALIAN ZYGOTE 23 and activity of some proteins in the connecting piece of the fertilizing spermatozoon. , 1995). The release of the sperm centriole into oocyte cytoplasm is followed by the assembly of pericentriolar material.
1991). 2. , 1997). Similarly, the oocyte nucleus is deprived of its NE by germinal vesicle breakdown (Stricker and Schatten, 1989). , 1997; Vigers and Lohka, 1991). This universal step in fertilization marks the formation of nuclear and cytoplasmic compartments in the fertilized oocytes and brings about the need for establishing a bidirectional communication and exchange of molecules necessary for normal pronuclear and embryonic development. The main channel for nucleocytoplasmic transport in animal cells is the nuclear pore complex (Pante and Aebi, 1996), an assembly of the O-glycosylated proteins from the nucleoporin family.