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

eLife

David T Auble¹  Stephan Woike¹  Karl-Peter Hopfner²  Agata Butryn³  Savera J Shetty³ 

[1] Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany;Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United States;Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany;

关键词: Chaetomium thermophilum;    X-ray crystallography;    transcription regulation;    Swi2/Snf2 remodeler;   

DOI  :  10.7554/eLife.37774

来源: DOAJ

【 摘 要 】

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 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.

【 授权许可】

Unknown