Crystal Structure and Functional Analysis of a Nucleosome Recognition Module of the Remodeling Factor ISWI
2003; Elsevier BV; Volume: 12; Issue: 2 Linguagem: Inglês
10.1016/s1097-2765(03)00273-9
ISSN1097-4164
AutoresTim Grüne, Jan Brzeski, Anton Eberharter, Cedric R. Clapier, Davide Corona, Peter B. Becker, Christoph W. Müller,
Tópico(s)Cancer-related gene regulation
ResumoEnergy-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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