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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Grüne, T., Brzeski, J., Eberharter, A., Clapier, C.R., Corona, D.F., Becker, P.B., Müller, C.W. Mol. Cell (2003) [Pubmed]
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