PT - JOURNAL ARTICLE AU - Gutierrez-Escribano, Pilar AU - Newton, Matthew D. AU - Llauró, Aida AU - Huber, Jonas AU - Tanasie, Loredana AU - Davy, Joseph AU - Aly, Isabel AU - Aramayo, Ricardo AU - Montoya, Alex AU - Kramer, Holger AU - Stigler, Johannes AU - Rueda, David S. AU - Aragon, Luis TI - A conserved ATP- and Scc2/4-dependent activity for cohesin in tethering DNA molecules AID - 10.1126/sciadv.aay6804 DP - 2019 Nov 01 TA - Science Advances PG - eaay6804 VI - 5 IP - 11 4099 - http://advances.sciencemag.org/content/5/11/eaay6804.short 4100 - http://advances.sciencemag.org/content/5/11/eaay6804.full SO - Sci Adv2019 Nov 01; 5 AB - 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.