Browse by author
Lookup NU author(s): James Dunce,
Dr Orla Dunne,
Dr Owen Davies
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
© 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.
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
Online publication date: 12/01/2023
Acceptance date: 06/12/2022
ISSN (print): 1545-9993
ISSN (electronic): 1545-9985
Publisher: Nature Research
Altmetrics provided by Altmetric