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Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP

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  • Petra Wollmann

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Munich Center for Advanced Photonics, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Sheng Cui

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Present address: Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, No. 9, Dong Dan San Tiao, Beijing 100730, China.)

  • Ramya Viswanathan

    (University of Virginia Health System)

  • Otto Berninghausen

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Melissa N. Wells

    (University of Virginia Health System)

  • Manuela Moldt

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Gregor Witte

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Munich Center for Advanced Photonics, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Center for Integrated Protein Science, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Agata Butryn

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Petra Wendler

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • Roland Beckmann

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Center for Integrated Protein Science, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

  • David T. Auble

    (University of Virginia Health System)

  • Karl-Peter Hopfner

    (Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Munich Center for Advanced Photonics, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
    Center for Integrated Protein Science, Gene Center Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany)

Abstract

Remodelling transcription The Swi2/Snf2 family of proteins uses the energy of ATP hydrolysis to disrupt protein-DNA interactions, a process known as remodelling. In this study, Karl-Peter Hopfner and colleagues have solved the structure of the Mot1 ATPase in complex with the transcription factor TBP, which Mot1 displaces from promoters. The structure reveals how the ATPase specifically interacts with TBP and DNA, acting both to displace TBP and to prevent it from rebinding DNA.

Suggested Citation

  • Petra Wollmann & Sheng Cui & Ramya Viswanathan & Otto Berninghausen & Melissa N. Wells & Manuela Moldt & Gregor Witte & Agata Butryn & Petra Wendler & Roland Beckmann & David T. Auble & Karl-Peter Hop, 2011. "Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP," Nature, Nature, vol. 475(7356), pages 403-407, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10215
    DOI: 10.1038/nature10215
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    Cited by:

    1. Chung-Chi Liao & Yi-Sen Wang & Wen-Chieh Pi & Chun-Hsiung Wang & Yi-Min Wu & Wei-Yi Chen & Kuo-Chiang Hsia, 2023. "Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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