Lookup NU author(s): Dr Owen Davies
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© Syrjänen et al. In a previous paper (Syrjänen et al., 2014), we reported the first structural characterisation of a synaptonemal complex (SC) protein, SYCP3, which led us to propose a model for its role in chromosome compaction during meiosis. As a component of the SC lateral element, SYCP3 has a critical role in defining the specific chromosome architecture required for correct meiotic progression. In the model, the reported compaction of chromosomal DNA caused by SYCP3 would result from its ability to bridge distant sites on a DNA molecule with the DNA-binding domains located at each end of its strut-like structure. Here, we describe a single-molecule assay based on optical tweezers, fluorescence microscopy and microfluidics that, in combination with bulk biochemical data, provides direct visual evidence for our proposed mechanism of SYCP3-mediated chromosome organisation.
Author(s): Syrjanen JL, Heller I, Candelli A, Davies OR, Peterman EJG, Wuite GJL, Pellegrini L
Publication type: Article
Publication status: Published
Online publication date: 13/03/2017
Acceptance date: 04/03/2017
Date deposited: 06/06/2017
ISSN (electronic): 2050-084X
Publisher: eLife Sciences Publications Ltd
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