Article abstract


Nature Structural & Molecular Biology 15, 1272 - 1277 (2008)
Published online: 23 November 2008 | doi:10.1038/nsmb.1524

Structure of a RSC–nucleosome complex and insights into chromatin remodeling

Yuriy Chaban1, Chukwudi Ezeokonkwo1, Wen-Hsiang Chung1, Fan Zhang1, Roger D Kornberg2, Barbara Maier-Davis2, Yahli Lorch2 & Francisco J Asturias1


ATP-dependent chromatin-remodeling complexes, such as RSC, can reposition, evict or restructure nucleosomes. A structure of a RSC–nucleosome complex with a nucleosome determined by cryo-EM shows the nucleosome bound in a central RSC cavity. Extensive interaction of RSC with histones and DNA seems to destabilize the nucleosome and lead to an overall ATP-independent rearrangement of its structure. Nucleosomal DNA appears disordered and largely free to bulge out into solution as required for remodeling, but the structure of the RSC–nucleosome complex indicates that RSC is unlikely to displace the octamer from the nucleosome to which it is bound. Consideration of the RSC–nucleosome structure and published biochemical information suggests that ATP-dependent DNA translocation by RSC may result in the eviction of histone octamers from adjacent nucleosomes.

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  1. Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
  2. Department of Structural Biology, Stanford University Medical Center, Stanford, California 94035, USA.

Correspondence to: Francisco J Asturias1 e-mail: asturias@scripps.edu



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