91
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Cryo-EM structure of the human cohesin-NIPBL-DNA complex

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          As a ring-shaped ATPase machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister-chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo-electron microscopy, we determine the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72-base pair DNA. NIPBL and DNA promote the engagement of cohesin’s ATPase head domains and ATP binding. The hinge domains of cohesin adopt an "open washer" conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA, and provides insight into DNA entrapment by cohesin.

          Related collections

          Author and article information

          Journal
          Science
          Science
          American Association for the Advancement of Science (AAAS)
          0036-8075
          1095-9203
          May 14 2020
          : eabb0981
          Affiliations
          [1 ]Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
          [2 ]Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
          [3 ]Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
          [4 ]School of Life Sciences, Westlake University, Hangzhou, Zhejiang 310024, China.
          Article
          10.1126/science.abb0981
          32409525
          229aa297-6770-43b8-a163-92eaa93823e3
          © 2020
          History

          Comments

          Comment on this article