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Sci Adv. 2019 Nov 27;5(11):eaay6804. doi: 10.1126/sciadv.aay6804. eCollection 2019 Nov.

A conserved ATP- and Scc2/4-dependent activity for cohesin in tethering DNA molecules.

Author information

1
Cell Cycle Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK.
2
Single Molecule Imaging Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK.
3
Molecular Virology, Department of Medicine, Imperial College London, Du Cane Road, London W12 0NN, UK.
4
LUMICKS, De Boelelaan 1085, 1081 HV, Amsterdam, Netherlands.
5
Gene Center, Ludwig-Maximilians-University, 81377 Munich, Germany.
6
Microscopy Facility, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK.
7
Biological Mass Spectrometry and Proteomics Facility, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK.

Abstract

Sister chromatid cohesion requires cohesin to act as a protein linker to hold chromatids together. How cohesin tethers chromatids remains poorly understood. We have used optical tweezers to visualize cohesin as it holds DNA molecules. We show that cohesin complexes tether DNAs in the presence of Scc2/Scc4 and ATP demonstrating a conserved activity from yeast to humans. Cohesin forms two classes of tethers: a "permanent bridge" resisting forces over 80 pN and a force-sensitive "reversible bridge." The establishment of bridges requires physical proximity of dsDNA segments and occurs in a single step. "Permanent" cohesin bridges slide when they occur in trans, but cannot be removed when in cis. Therefore, DNAs occupy separate physical compartments in cohesin molecules. We finally demonstrate that cohesin tetramers can compact linear DNA molecules stretched by very low force (below 1 pN), consistent with the possibility that, like condensin, cohesin is also capable of loop extrusion.

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