Proceedings of the National Academy of Sciences · 2010 · 115 citations · 25 references
Molecular BiologyEpigeneticsProtein FoldingHistone SurfaceDna TranslocationDna ComputingBiophysicsAtp HydrolysisMacromolecular MachineDna ReplicationChromatin BiologyNuclear OrganizationCell BiologyStructural BiologyChromatin FunctionChromatinChromatin StructureChromatin RemodelingNatural SciencesEpigenomicsMedicine
Results from biochemical and structural studies of the RSC chromatin-remodeling complex prompt a proposal for the remodeling mechanism: RSC binding to the nucleosome releases the DNA from the histone surface and initiates DNA translocation (through one or a small number of DNA base pairs); ATP binding completes translocation, and ATP hydrolysis resets the system. Binding energy thus plays a central role in the remodeling process. RSC may disrupt histone-DNA contacts by affecting histone octamer conformation and through extensive interaction with the DNA. Bulging of the DNA from the octamer surface is possible, and twisting is unavoidable, but neither is the basis of remodeling.
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Crystal structure of the nucleosome core particle at 2.8 Å resolution
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ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex
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