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Structural maturation of SYCP1-mediated meiotic chromosome synapsis by SYCE3

Lookup NU author(s): James Dunce, Dr Orla Dunne, Lucy Salmon, Dr Owen Davies


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© 2023, The Author(s), under exclusive licence to Springer Nature America, Inc.In meiosis, a supramolecular protein structure, the synaptonemal complex (SC), assembles between homologous chromosomes to facilitate their recombination. Mammalian SC formation is thought to involve hierarchical zipper-like assembly of an SYCP1 protein lattice that recruits stabilizing central element (CE) proteins as it extends. Here we combine biochemical approaches with separation-of-function mutagenesis in mice to show that, rather than stabilizing the SYCP1 lattice, the CE protein SYCE3 actively remodels this structure during synapsis. We find that SYCP1 tetramers undergo conformational change into 2:1 heterotrimers on SYCE3 binding, removing their assembly interfaces and disrupting the SYCP1 lattice. SYCE3 then establishes a new lattice by its self-assembly mimicking the role of the disrupted interface in tethering together SYCP1 dimers. SYCE3 also interacts with CE complexes SYCE1–SIX6OS1 and SYCE2–TEX12, providing a mechanism for their recruitment. Thus, SYCE3 remodels the SYCP1 lattice into a CE-binding integrated SYCP1–SYCE3 lattice to achieve long-range synapsis by a mature SC.

Publication metadata

Author(s): Crichton JH, Dunce JM, Dunne OM, Salmon LJ, Devenney PS, Lawson J, Adams IR, Davies OR

Publication type: Article

Publication status: Published

Journal: Nature Structural and Molecular Biology

Year: 2023

Volume: 30

Pages: 188-199

Online publication date: 12/01/2023

Acceptance date: 06/12/2022

ISSN (print): 1545-9993

ISSN (electronic): 1545-9985

Publisher: Nature Research


DOI: 10.1038/s41594-022-00909-1


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