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.
- David Thomas Auble
- Karl-Peter Hopfner
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
- Geeta J Narlikar, University of California, San Francisco, United States
© 2018, Butryn et al.
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