Single-molecule observation of DNA compaction by meiotic protein SYCP3

Johanna L. Syrjanen, Iddo Heller, Andrea Candelli, Owen R. Davies, Erwin J. G. Peterman, Gijs J. L. Wuite, Luca Pellegrini

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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.
Original languageEnglish
Article numbere22582
JournaleLife
Volume6
DOIs
Publication statusPublished - 13 Mar 2017

Fingerprint

Dive into the research topics of 'Single-molecule observation of DNA compaction by meiotic protein SYCP3'. Together they form a unique fingerprint.

Cite this