IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms12523.html
   My bibliography  Save this article

Topology and structure of an engineered human cohesin complex bound to Pds5B

Author

Listed:
  • Michael T. Hons

    (Max Planck Institute for Biophysical Chemistry)

  • Pim J. Huis in ‘t Veld

    (Research Institute of Molecular Pathology (IMP)
    Present address: Department of Mechanistic Cell Biology, Max Planck Institute for Molecular Physiology, Otto Hahn Strasse 11, 44227 Dortmund, Germany)

  • Jan Kaesler

    (Max Planck Institute for Biophysical Chemistry)

  • Pascaline Rombaut

    (Gene Center, Ludwig-Maximilian University)

  • Alexander Schleiffer

    (Research Institute of Molecular Pathology (IMP))

  • Franz Herzog

    (Gene Center, Ludwig-Maximilian University)

  • Holger Stark

    (Max Planck Institute for Biophysical Chemistry)

  • Jan-Michael Peters

    (Research Institute of Molecular Pathology (IMP))

Abstract

The cohesin subunits Smc1, Smc3 and Scc1 form large tripartite rings which mediate sister chromatid cohesion and chromatin structure. These are thought to entrap DNA with the help of the associated proteins SA1/2 and Pds5A/B. Structural information is available for parts of cohesin, but analyses of entire cohesin complexes are limited by their flexibility. Here we generated a more rigid ‘bonsai’ cohesin by truncating the coiled coils of Smc1 and Smc3 and used single-particle electron microscopy, chemical crosslinking-mass spectrometry and in silico modelling to generate three-dimensional models of cohesin bound to Pds5B. The HEAT-repeat protein Pds5B forms a curved structure around the nucleotide-binding domains of Smc1 and Smc3 and bridges the Smc3-Scc1 and SA1-Scc1 interfaces. These results indicate that Pds5B forms an integral part of the cohesin ring by contacting all other cohesin subunits, a property that may reflect the complex role of Pds5 proteins in controlling cohesin–DNA interactions.

Suggested Citation

  • Michael T. Hons & Pim J. Huis in ‘t Veld & Jan Kaesler & Pascaline Rombaut & Alexander Schleiffer & Franz Herzog & Holger Stark & Jan-Michael Peters, 2016. "Topology and structure of an engineered human cohesin complex bound to Pds5B," Nature Communications, Nature, vol. 7(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12523
    DOI: 10.1038/ncomms12523
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms12523
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms12523?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12523. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.