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

Elife. 2018 Oct 5:7:e37774. doi: 10.7554/eLife.37774.

Abstract

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.

Keywords: Chaetomium thermophilum; Swi2/Snf2 remodeler; X-ray crystallography; molecular biophysics; structural biology; transcription regulation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Apoproteins / chemistry
  • Apoproteins / metabolism
  • Chaetomium / metabolism*
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Crystallography, X-Ray
  • DNA, Fungal / metabolism
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism
  • Models, Molecular
  • Mutation / genetics
  • Protein Domains
  • TATA-Box Binding Protein / metabolism
  • Transcription Factors / chemistry*

Substances

  • Apoproteins
  • Chromosomal Proteins, Non-Histone
  • DNA, Fungal
  • Fungal Proteins
  • SWI-SNF-B chromatin-remodeling complex
  • TATA-Box Binding Protein
  • Transcription Factors
  • Adenosine Triphosphatases