Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 12, Pages 1272-1277Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1524
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Funding
- NIGMS NIH HHS [R01 GM067167, R01 GM067167-04] Funding Source: Medline
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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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