Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines

• Published in: Current opinion in structural biology Vol. 22; no. 2; pp. 225 - 233
• Main Authors: Hopfner, Karl-Peter, Gerhold, Christian-Benedikt, Lakomek, Kristina, Wollmann, Petra
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01-04-2012
• Subjects: 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
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/j.sbi.2012.02.007

► Swi2/Snf2 proteins/multiprotein assemblies remodel nucleic acid: protein complexes. ► Core Swi2/Snf2 ATPase domain is a structurally and functionally versatile motor. ► Hybrid methods pave the way toward nucleosome:remodeler structures and mechanisms. ► The remodelers Mot1, Chd1 and Isw1 use different ATP-driven multistep mechanisms. ► Mot1 employs a hybrid mechanism of remodeler and chaperone.
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.