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Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly

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.

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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.

Publication metadata

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


DOI: 10.1038/s41594-018-0078-9


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Funder referenceFunder name
104158/Z/14/ZWellcome Trust