Publication Abstract from PubMed
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.
Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.,Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW Mol Cell. 2003 Aug;12(2):449-60. PMID:14536084[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
