Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines

Curr Opin Struct Biol. 2012 Apr;22(2):225-33. doi: 10.1016/j.sbi.2012.02.007. Epub 2012 Mar 23.

Abstract

Swi2/Snf2 (switch/sucrose non-fermentable) enzymes form a large and diverse class of proteins and multiprotein assemblies that remodel nucleic acid:protein complexes, using the energy of ATP hydrolysis. The core Swi2/Snf2 type ATPase domain belongs to the 'helicase and NTP driven nucleic acid translocase' superfamily 2 (SF2). It serves as a motor that functionally and structurally interacts with different targeting domains and functional modules to drive a plethora of remodeling activities in chromatin structure and dynamics, transcription regulation and DNA repair. Recent progress on the interaction of Swi2/Snf2 enzymes and multiprotein assemblies with their substrate nucleic acids and proteins, using hybrid structural biology methods, illuminates mechanisms for complex chemo-mechanical remodeling reactions. For Mot1, a hybrid mechanism of remodeler and chaperone emerged.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / metabolism
  • Animals
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Nucleic Acids / chemistry
  • Nucleic Acids / metabolism
  • Nucleosomes / chemistry
  • Nucleosomes / metabolism
  • Protein Binding
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism

Substances

  • Molecular Chaperones
  • Nucleic Acids
  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Adenosine Triphosphatases
  • SNF2 protein, S cerevisiae