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Mechanical disengagement of the cohesin ring

Richeldi, Martina; Pobegalov, Georgii; Higashi, Torahiko L; Gmurczyk, Karolina; Uhlmann, Frank; Molodtsov, Maxim I; (2023) Mechanical disengagement of the cohesin ring. Nature Structural & Molecular Biology 10.1038/s41594-023-01122-4. (In press). Green open access

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Abstract

Cohesin forms a proteinaceous ring that is thought to link sister chromatids by entrapping DNA and counteracting the forces generated by the mitotic spindle. Whether individual cohesins encircle both sister DNAs and how cohesin opposes spindle-generated forces remains unknown. Here we perform force measurements on individual yeast cohesin complexes either bound to DNA or holding together two DNAs. By covalently closing the hinge and Smc3Psm3–kleisin interfaces we find that the mechanical stability of the cohesin ring entrapping DNA is determined by the hinge domain. Forces of ~20 pN disengage cohesin at the hinge and release DNA, indicating that ~40 cohesin molecules are sufficient to counteract known spindle forces. Our findings provide a mechanical framework for understanding how cohesin interacts with sister chromatids and opposes the spindle-generated tension during mitosis, with implications for other force-generating chromosomal processes including transcription and DNA replication.

Type: Article
Title: Mechanical disengagement of the cohesin ring
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/s41594-023-01122-4
Publisher version: https://doi.org/10.1038/s41594-023-01122-4
Language: English
Additional information: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third-party material in this article are included in the Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Keywords: Chromatin, DNA-binding proteins, Molecular biophysics, Single-molecule biophysics
UCL classification: UCL
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy
URI: https://discovery-pp.ucl.ac.uk/id/eprint/10179821
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