Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state.,Butryn A, Woike S, Shetty SJ, Auble DT, Hopfner KP Elife. 2018 Oct 5;7. pii: 37774. doi: 10.7554/eLife.37774. PMID:30289385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Butryn A, Woike S, Shetty SJ, Auble DT, Hopfner KP. Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state. Elife. 2018 Oct 5;7. pii: 37774. doi: 10.7554/eLife.37774. PMID:30289385 doi:http://dx.doi.org/10.7554/eLife.37774