Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state

  1. Agata Butryn
  2. Stephan Woike
  3. Savera Jagathpala Shetty
  4. David Thomas Auble
  5. Karl-Peter Hopfner  Is a corresponding author
  1. Ludwig-Maximilians-Universität München, Germany
  2. University of Virginia Health System, United States

Abstract

Swi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome‑associated processes. The single‑subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Previously we reported how the N-terminal domain of Mot1 it binds TBP, NC2 and DNA, but the location of the C-terminal ATPase domain remained unclear (Butryn et al., 2015). Here, we report the crystal structure of the near full-length Mot1 from Chaetomium thermophilum. Our data show that Mot1 adopts a ring like structure with a catalytically inactive resting state of the ATPase. Biochemical analysis suggests that TBP binding switches Mot1 into an ATP hydrolysis-competent conformation. Combined with our previous results, these data significantly improve the structural model for the complete Mot1:TBP:DNA complex and suggest a general mechanism for Mot1 action.

Data availability

The coordinates and structure factors are deposited in the Protein Data Bank under accession code 6G7E. All data generated or analysed during this study are included in the manuscript and supporting files. Source data files have been provided for Figures 2 and Figure 2-figure supplement 1.

The following data sets were generated

Article and author information

Author details

  1. Agata Butryn

    Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-5227-4770
  2. Stephan Woike

    Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  3. Savera Jagathpala Shetty

    Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United States
    Competing interests
    The authors declare that no competing interests exist.
  4. David Thomas Auble

    Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United States
    Competing interests
    The authors declare that no competing interests exist.
  5. Karl-Peter Hopfner

    Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany
    For correspondence
    hopfner@genzentrum.lmu.de
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-4528-8357

Funding

National Institutes of Health (GM055763)

  • David Thomas Auble

European Commission (ERC Advanced Grant ATMMACHINE)

  • Karl-Peter Hopfner

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

Reviewing Editor

  1. Geeta J Narlikar, University of California, San Francisco, United States

Version history

  1. Received: May 1, 2018
  2. Accepted: October 4, 2018
  3. Accepted Manuscript published: October 5, 2018 (version 1)
  4. Version of Record published: October 15, 2018 (version 2)
  5. Version of Record updated: October 24, 2018 (version 3)

Copyright

© 2018, Butryn 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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  1. Agata Butryn
  2. Stephan Woike
  3. Savera Jagathpala Shetty
  4. David Thomas Auble
  5. Karl-Peter Hopfner
(2018)
Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state
eLife 7:e37774.
https://doi.org/10.7554/eLife.37774

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https://doi.org/10.7554/eLife.37774

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