Grune, T., Brzeski, J., Eberharter, A., Clapier, C.R., Corona, D.F., Becker, P.B., Muller, C.W. (2003). Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.  Mol. Cell 12(2): 449--460.

FBrf0167877

Research paper

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.