Protein SYCP2 provides a link between transverse filaments and lateral elements of mammalian synaptonemal complexes |
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Authors: | Karoline Winkel Manfred Alsheimer Rupert Öllinger Ricardo Benavente |
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Institution: | (1) Department of Cell and Developmental Biology, Biocenter, University of Würzburg, Am Hubland, 97074 Würzburg, Germany |
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Abstract: | Synaptonemal complexes (SCs) are evolutionarily conserved meiosis-specific nuclear structures critically involved in synapsis,
recombination, and segregation of homologous chromosomes. SCs are proteinaceous structures composed of (a) two lateral elements
(LEs), to which the chromatin of the homologs is attached, (b) numerous transverse filaments (TFs) that link the LEs, and
(c) a central element (CE). Major protein components of mammalian SCs are the TF protein SYCP1 and the LE proteins SYCP2 and
SCYP3. How SCs become assembled is presently poorly understood, in particular, it is not known how TFs assemble at the plane
of LEs to interconnect the homologous chromosomes. Therefore, we have investigated possible interactions between SYCP1 and
other SC proteins. In immunoprecipitation experiments we could find that SYCP1 and SYCP2 interact in extracts of meiotic cells.
Using the yeast two-hybrid system, we were able to demonstrate that the C-terminus of SYCP1 directly interacts with SYCP2.
These results were confirmed by different interaction traps. Furthermore, we could narrow down the interacting domain of the
SYCP2 molecule to its C-terminal region. We propose that SYCP2 acts as a linker between SYCP1 and SYCP3 and therefore would
be the missing connecting link between LEs and TFs essential for proper chromosome synapsis. |
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