Back to Search Start Over

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

Authors :
Grüne T
Brzeski J
Eberharter A
Clapier CR
Corona DF
Becker PB
Müller CW
Source :
Molecular cell [Mol Cell] 2003 Aug; Vol. 12 (2), pp. 449-60.
Publication Year :
2003

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.

Details

Language :
English
ISSN :
1097-2765
Volume :
12
Issue :
2
Database :
MEDLINE
Journal :
Molecular cell
Publication Type :
Academic Journal
Accession number :
14536084
Full Text :
https://doi.org/10.1016/s1097-2765(03)00273-9