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Vol. 16, Issue 1, 212-217, January 2005

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Mammalian Protein SCP1 Forms Synaptonemal Complex-like Structures in the Absence of Meiotic Chromosomes

Department of Cell and Developmental Biology, Biocenter, University of Würzburg, D-97074 Würzburg, Germany

Submitted September 3, 2004; Revised October 6, 2004; Accepted October 8, 2004
Monitoring Editor: Joseph Gall

Synaptonemal complexes (SCs) are evolutionary conserved, meiosis-specific structures that play a central role in synapsis of homologous chromosomes, chiasmata distribution, and chromosome segregation. However, it is still for the most part unclear how SCs do assemble during meiotic prophase. Major components of mammalian SCs are the meiosis-specific proteins SCP1, 2, and 3. To investigate the role of SCP1 in SC assembly, we expressed SCP1 in a heterologous system, i.e., in COS-7 cells that normally do not express SC proteins. Notably, under these experimental conditions SCP1 is able to form structures that closely resemble SCs (i.e., polycomplexes). Moreover, we show that mutations that modify the length of the central -helical domain of SCP1 influence the width of polycomplexes. Finally, we demonstrate that deletions of the nonhelical N- or C-termini both affect polycomplex assembly, although in a different manner. We conclude that SCP1 is a primary determinant of SC assembly that plays a key role in synapsis of homologous chromosomes.

This article is dedicated to Professor Omar Trujillo-Cenóz (IIBCE, Montevideo, Uruguay) on the occasion of his 70th birthday. Together with the late Prof. J. R. Sotelo, he published in 1960 the first description of polycomplexes.

Abbreviations used: SC, synaptonemal complex; EM, electron microscopy.

^* Corresponding author. E-mail address: benavente{at}biozentrum.uniwuerzburg.de.

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