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Lookup NU author(s): James Dunce, Dr Orla Dunne, Matthew Ratcliff, Dr Suzanne Madgwick, Dr Owen Davies
This is the authors' accepted manuscript of an article that has been published in its final definitive form by Nature Publishing Group, 2018.
For re-use rights please refer to the publisher's terms and conditions.
Meiotic chromosomes adopt unique structures in which linear arrays of chromatin loops are bound together in homologous chromosome pairs by a supramolecular protein assembly, the synaptonemal complex. This three-dimensional scaffold provides the essential structural framework for genetic exchange by crossing over and subsequent homolog segregation. The core architecture of the synaptonemal complex is provided by SYCP1. Here we report the structure and self-assembly mechanism of human SYCP1 through X-ray crystallographic and biophysical studies. SYCP1 has an obligate tetrameric structure in which an N-terminal four-helical bundle bifurcates into two elongated C-terminal dimeric coiled-coils. This building block assembles into a zipper-like lattice through two self-assembly sites. N-terminal sites undergo cooperative head-to-head assembly in the midline, while C-terminal sites interact back to back on the chromosome axis. Our work reveals the underlying molecular structure of the synaptonemal complex in which SYCP1 self-assembly generates a supramolecular lattice that mediates meiotic chromosome synapsis.
Author(s): Dunce JM, Dunne OM, Ratcliff M, Millán C, Madgwick S, Usón I, Davies OR
Publication type: Article
Publication status: Published
Journal: Nature Structural & Molecular Biology
Year: 2018
Volume: 25
Issue: 7
Pages: 557-569
Print publication date: 01/07/2018
Online publication date: 18/06/2018
Acceptance date: 25/04/2018
Date deposited: 20/06/2018
ISSN (print): 1545-9993
ISSN (electronic): 1545-9985
Publisher: Nature Publishing Group
URL: https://doi.org/10.1038/s41594-018-0078-9
DOI: 10.1038/s41594-018-0078-9
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