1. Structural Biology and Molecular Biophysics
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Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1

  1. Agata Butryn
  2. Jan M Schuller
  3. Gabriele Stoehr
  4. Petra Runge-Wollmann
  5. Friedrich Förster
  6. David T Auble
  7. Karl-Peter Hopfner  Is a corresponding author
  1. Ludwig-Maximilians-University Munich, Germany
  2. Max Planck Institute of Biochemistry, Germany
  3. University of Virginia Health System, United States
  4. Ludwig Maximilian University Munich, Germany
Research Article
  • Cited 12
  • Views 1,695
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Cite this article as: eLife 2015;4:e07432 doi: 10.7554/eLife.07432

Abstract

Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA associated processes, but detailed structural information on the ATP-dependent remodeling reactions is largely absent. The single subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes, offering a useful system to address the structural mechanisms of Swi2/Snf2 ATPases. Here we report the crystal structure of the N-terminal domain of Mot1 in complex with TBP, DNA, and the transcription regulator NC2. Our data show that Mot1 reduces DNA:NC2 interactions and unbends DNA as compared to the TBP:DNA:NC2 state, suggesting that Mot1 primes TBP:NC2 displacement in an ATP-independent manner. Electron microscopy and cross-linking data suggest that the Swi2/Snf2 domain of Mot1 associates with the upstream DNA and the histone fold of NC2, thereby revealing parallels to some nucleosome remodelers. This study provides a structural framework for how a Swi2/Snf2 ATPase interacts with its substrate DNA:protein complex.

Article and author information

Author details

  1. Agata Butryn

    Gene Center, Department of Biochemistry, Ludwig-Maximilians-University Munich, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  2. Jan M Schuller

    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  3. Gabriele Stoehr

    Gene Center, Department of Biochemistry, Ludwig-Maximilians-University Munich, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  4. Petra Runge-Wollmann

    Gene Center, Department of Biochemistry, Ludwig-Maximilians-University Munich, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  5. Friedrich Förster

    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Munich, Germany
    Competing interests
    The authors declare that no competing interests exist.
  6. David T 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.
  7. Karl-Peter Hopfner

    Gene Center, Department of Biochemistry, Ludwig Maximilian University Munich, Munich, Germany
    For correspondence
    hopfner@genzentrum.lmu.de
    Competing interests
    The authors declare that no competing interests exist.

Reviewing Editor

  1. John Kuriyan, Howard Hughes Medical Institute, University of California, Berkeley, United States

Publication history

  1. Received: March 11, 2015
  2. Accepted: August 8, 2015
  3. Accepted Manuscript published: August 10, 2015 (version 1)
  4. Version of Record published: September 11, 2015 (version 2)

Copyright

© 2015, 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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