Single-molecule observation of DNA compaction by meiotic protein SYCP3

eLife

Andrea Candelli¹  Erwin J G Peterman¹  Johanna L Syrjänen²  Owen R Davies³  Iddo Heller³  Luca Pellegrini³  Gijs J L Wuite⁴ 

[1] LaserLaB, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands;Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom;Department of Physics and Astronomy, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands;Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne, United Kingdom;

关键词: SYCP3;    Synaptonemal complex;    Meiosis;    Protein-DNA interactions;    Single-molecule;   

DOI  :  10.7554/eLife.22582

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown