Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI |
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Authors: | Grüne Tim Brzeski Jan Eberharter Anton Clapier Cedric R Corona Davide F V Becker Peter B Müller Christoph W |
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Affiliation: | European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France. |
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Abstract: | 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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