한빛사 논문
Yoori Kim1,*, Zhubing Shi1,*, Hongshan Zhang2, Ilya J. Finkelstein2,†, Hongtao Yu1,†
1 Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
2 Center for Systems and Synthetic Biology, Institute for Cellular and Molecular Biology, Department of Molecular Biosciences, University of Texas-Austin, Austin, TX 78712, USA.
* These authors contributed equally to this work.
† Corresponding author : Ilya J. Finkelstein, Hongtao Yu
Abstract
Cohesin is a chromosome-bound multisubunit ATPase complex. Following its loading onto chromosomes, cohesin generates chromosome loops to regulate chromosome functions. It has been suggested that cohesin organizes the genome via loop extrusion, but direct evidence is lacking. Here, we use single-molecule imaging to show that recombinant human cohesin-NIPBL complex compacts both naked and nucleosome-bound DNA by extruding DNA loops. DNA compaction by cohesin requires ATP hydrolysis, and is force-sensitive. This compaction is processive over tens of kilobases (kb) at an average rate of 0.5 kb per second. Compaction of double-tethered DNA suggests that a cohesin dimer extrudes DNA loops bidirectionally. Our results establish cohesin-NIPBL as an ATP-driven molecular machine capable of loop extrusion.
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