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Grüne, Tim; Brzeski, Jan; Eberharter, Anton; Clapier, Cedric R; Corona, Davide F.V; Becker, Peter B; Müller, Christoph W
Molecular cell, August 2003, 2003-Aug, 2003-08-00, 20030801, Letnik: 12, Številka: 2Journal Article
Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two α-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
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