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Molecular structure of human synaptonemal complex protein SYCE1

Lookup NU author(s): Dr Orla Dunne, Dr Owen Davies

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

The reduction in chromosome number during meiosis is essential for the production of haploid germ cells and thereby fertility. To achieve this, homologous chromosomes are first synapsed together by a protein assembly, the synaptonemal complex (SC), which permits genetic exchange by crossing over and the subsequent accurate segregation of homologues. The mammalian SC is formed of a zipper-like array of SYCP1 molecules that bind together homologous chromosomes through self-assembly in the midline that is structurally supported by the central element. The SC central element contains five proteins—SYCE1, SYCE3, SIX6OS1, and SYCE2-TEX12—that permit SYCP1 assembly to extend along the chromosome length to achieve full synapsis. Here, we report the structure of human SYCE1 through solution biophysical methods including multi-angle light scattering and small-angle X-ray scattering. The structural core of SYCE1 is formed by amino acids 25–179, within the N-terminal half of the protein, which mediates SYCE1 dimerization. This α-helical core adopts a curved coiled-coil structure of 20-nm length in which the two chains are arranged in an anti-parallel configuration. This structure is retained within full-length SYCE1, in which long C-termini adopt extended conformations to achieve an elongated molecule of over 50 nm in length. The SYCE1 structure is compatible with it functioning as a physical strut that tethers other components to achieve structural stability of the SC central element.


Publication metadata

Author(s): Dunne OM, Davies OR

Publication type: Article

Publication status: Published

Journal: Chromosoma : Biology of the Nucleus

Year: 2019

Pages: ePub ahead of print

Online publication date: 03/01/2019

Acceptance date: 13/12/2018

ISSN (print): 0009-5915

ISSN (electronic): 1432-0886

Publisher: Springer

URL: https://doi.org/10.1007/s00412-018-00688-z

DOI: 10.1007/s00412-018-00688-z


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