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Mol Cell. 2003 Aug;12(2):449-60.

Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.

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European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France.


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 alpha-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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