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

Petra Wollmann, Sheng Cui, Ramya Viswanathan, Otto Berninghausen, Melissa N. Wells, Manuela Moldt, Gregor Witte, Agata Butryn, Petra Wendler, Roland Beckmann, David T. Auble () and Karl-Peter Hopfner ()
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Petra Wollmann: Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
Sheng Cui: Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
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
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
David T. Auble: University of Virginia Health System
Karl-Peter Hopfner: Ludwig-Maximilians University, Feodor-Lynen-Strasse 25, 81377 Munich, Germany

Nature, 2011, vol. 475, issue 7356, 403-407

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.

Date: 2011
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DOI: 10.1038/nature10215

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