1. Chromosomes and Gene Expression
  2. Structural Biology and Molecular Biophysics
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Structural basis for Scc3-dependent cohesin recruitment to chromatin

  1. Yan Li
  2. Kyle Muir  Is a corresponding author
  3. Matthew W Bowler
  4. Jutta Metz
  5. Christian H Haering
  6. Daniel Panne  Is a corresponding author
  1. European Molecular Biology Laboratory, France
  2. European Molecular Biology Laboratory, Germany
Research Article
  • Cited 31
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Cite this article as: eLife 2018;7:e38356 doi: 10.7554/eLife.38356

Abstract

The cohesin ring complex is required for numerous chromosomal transactions, including sister chromatid cohesion, DNA damage repair and transcriptional regulation. How cohesin engages its chromatin substrate has remained an unresolved question. We show here, by determining a crystal structure of the budding yeast cohesin HEAT-repeat subunit Scc3 bound to a fragment of the Scc1 kleisin subunit and DNA, that Scc3 and Scc1 together form a composite DNA interaction module. The Scc3-Scc1 subcomplex engages double-strand DNA through a conserved, positively charged surface. We demonstrate that this conserved domain is required for DNA binding by Scc3-Scc1 in vitro, as well as for the enrichment of cohesin on chromosomes and for cell viability. These findings suggest that the Scc3-Scc1 DNA-binding interface plays a central role in the recruitment of cohesin complexes to chromosomes and therefore for cohesin to faithfully execute its functions during cell division.

Data availability

Diffraction data have been deposited in PDB under the accession code 6H8Q.

The following data sets were generated

Article and author information

Author details

  1. Yan Li

    European Molecular Biology Laboratory, Grenoble, France
    Competing interests
    The authors declare that no competing interests exist.
  2. Kyle Muir

    European Molecular Biology Laboratory, Grenoble, France
    For correspondence
    kmuir@embl.fr
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-0294-5679
  3. Matthew W Bowler

    European Molecular Biology Laboratory, Grenoble, France
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0003-0465-3351
  4. Jutta Metz

    Department of Cell Biology and Biophysics, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  5. Christian H Haering

    Department of Cell Biology and Biophysics, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0001-8301-1722
  6. Daniel Panne

    European Molecular Biology Laboratory, Grenoble, France
    For correspondence
    panne@embl.fr
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0001-9158-5507

Funding

European Molecular Biology Labratory

  • Yan Li
  • Kyle Muir
  • Matthew W Bowler
  • Jutta Metz
  • Christian H Haering
  • Daniel Panne

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

  1. Andrea Musacchio, Max Planck Institute of Molecular Physiology, Germany

Publication history

  1. Received: May 14, 2018
  2. Accepted: August 13, 2018
  3. Accepted Manuscript published: August 15, 2018 (version 1)
  4. Version of Record published: September 3, 2018 (version 2)

Copyright

© 2018, Li et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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