Journal
MOLECULAR CELL
Volume 12, Issue 2, Pages 449-460Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(03)00273-9
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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 a-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by along helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
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