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A conserved ATP- and Scc2/4-dependent activity for cohesin in tethering DNA molecules
File | Description | Size | Format | |
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eaay6804.full.pdf | Published version | 3.6 MB | Adobe PDF | View/Open |
Title: | A conserved ATP- and Scc2/4-dependent activity for cohesin in tethering DNA molecules |
Authors: | Gutierrez-Escribano, P Newton, MD Llauro, A Huber, J Tanasie, L Davy, J Aly, I Aramayo, R Montoya, A Kramer, H Stigler, J Rueda, DS Aragon, L |
Item Type: | Journal Article |
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. |
Issue Date: | 27-Nov-2019 |
Date of Acceptance: | 22-Oct-2019 |
URI: | http://hdl.handle.net/10044/1/88132 |
DOI: | 10.1126/sciadv.aay6804 |
ISSN: | 2375-2548 |
Publisher: | American Association for the Advancement of Science |
Start Page: | 1 |
End Page: | 15 |
Journal / Book Title: | Science Advances |
Volume: | 5 |
Issue: | 11 |
Copyright Statement: | © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). This is an open-access article distributed under the terms of the Creative Commons Attribution license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
Sponsor/Funder: | Wellcome Trust |
Funder's Grant Number: | 100955/Z/13/Z |
Keywords: | Science & Technology Multidisciplinary Sciences Science & Technology - Other Topics SISTER-CHROMATID COHESION CHROMOSOME CONDENSATION TRANSLOCATION PROTEINS REVEALS COMPLEX Adenosine Triphosphate Cell Cycle Proteins Chromatids Chromosomal Proteins, Non-Histone DNA, Fungal Humans Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Chromatids Humans Saccharomyces cerevisiae Cell Cycle Proteins Saccharomyces cerevisiae Proteins Chromosomal Proteins, Non-Histone DNA, Fungal Adenosine Triphosphate Science & Technology Multidisciplinary Sciences Science & Technology - Other Topics SISTER-CHROMATID COHESION CHROMOSOME CONDENSATION TRANSLOCATION PROTEINS REVEALS COMPLEX |
Publication Status: | Published |
Open Access location: | https://advances.sciencemag.org/content/5/11/eaay6804 |
Article Number: | ARTN eaay6804 |
Online Publication Date: | 2019-11-27 |
Appears in Collections: | Department of Infectious Diseases Institute of Clinical Sciences |
This item is licensed under a Creative Commons License