J. Cell Biol., Volume 142, Number 2, July 27, 1998 331-339

The Synaptonemal Complex Protein SCP3 Can Form Multistranded, Cross-striated Fibers In Vivo

Li Yuan,^* Jeanette Pelttari,^* Eva Brundell,^* Birgitta Björkroth,^* Jian Zhao,^* Jian-Guo Liu,^* Hjalmar Brismar,^§ Bertil Daneholt,^* and Christer Höög^*§

^* Department of Cell and Molecular Biology (CMB), The Medical Nobel Institute,  Center for Genomics Research, Karolinska Institutet, S-171 77 Stockholm, Sweden; and ^§ Department of Woman and Child Health, Pediatric Unit, St. Göran's Children's Hospital, S-112 81 Stockholm, Sweden

The synaptonemal complex protein SCP3 is part of the lateral element of the synaptonemal complex, a meiosis-specific protein structure essential for synapsis of homologous chromosomes. We have investigated the fiber-forming properties of SCP3 to elucidate its role in the synaptonemal complex. By synthesis of SCP3 in cultured somatic cells, it has been shown that SCP3 can self-assemble into thick fibers and that this process requires the COOH-terminal coiled coil domain of SCP3, as well as the NH₂-terminal nonhelical domain. We have further analyzed the thick SCP3 fibers by transmission electron microscopy and immunoelectron microscopy. We found that the fibers display a transversal striation with a periodicity of ~20 nm and consist of a large number of closely associated, thin fibers, 5-10 nm in diameter. These features suggest that the SCP3 fibers are structurally related to intermediate filaments. It is known that in some species the lateral elements of the synaptonemal complex show a highly ordered striated structure resembling that of the SCP3 fibers. We propose that SCP3 fibers constitute the core of the lateral elements of the synaptonemal complex and function as a molecular framework to which other proteins attach, regulating DNA binding to the chromatid axis, sister chromatid cohesion, synapsis, and recombination.

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