Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines

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• 作者：Karl-Peter Hopfner¹ ; ² ; ^{hopfner@genzentrum.lmu.de} ; Christian-Benedikt Gerhold¹ ; Kristina Lakomek¹ ; Petra Wollmann¹
• 刊名：Current Opinion in Structural Biology
• 出版年：2012
• 期刊代码：61_0959440x
• 类别：bio
• 出版时间：April, 2012
• 卷：22
• 期：2
• 页码：225-233
• 文件大小：2295 K

摘要

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 鈥榟elicase and NTP driven nucleic acid translocase鈥?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.