Journal
SCIENTIFIC REPORTS
Volume 4, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep07059
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Funding
- 973 Program [2012CB917200, 2013CB910400, 2014CB910201]
- Natural Science Foundation of China [31370826, 31300628, 31170684]
- Tianjin Basic Research Program [14JCQNJ09300]
- Fundamental Research Funds for the Central Universities [65142007, 65121016]
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The key step in meiosis is synaptonemal complex formation, which mediates homologous chromosome alignment and synapsis. False pairing between homologous chromosomes produces infertility. Here, we present a crystal structure of the mouse meiosis-specific protein SYCE3, which is a component of the synaptonemal complex central element. Our studies show that functional SYCE3 most likely forms a dimer or higher order oligomer in cells. Furthermore, we demonstrate that the SYCE3 N-helix interacts with the SYCE1 C-helix, which is another central element component. Our results suggest that helical packing may mediate intra-or inter-association of each central element protein component, thereby playing an essential role in forming the synaptonemal complex central elements.
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