Structure of a RSC-nucleosome complex and insights into chromatin remodeling.
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.
Chaban
Yuriy
Y
Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Ezeokonkwo
Chukwudi
C
Chung
Wen-Hsiang
WH
Zhang
Fan
F
Kornberg
Roger D
RD
Maier-Davis
Barbara
B
Lorch
Yahli
Y
Asturias
Francisco J
FJ
D042002:Chromatin Assembly and Disassembly; D020285:Cryoelectron Microscopy; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D009707:Nucleosomes / Q000737:chemistry* / Q000648:ultrastructure*; D020836:Protein Structure, Quaternary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D014157:Transcription Factors / Q000737:chemistry* / Q000648:ultrastructure*
D004268:DNA-Binding Proteins; D009707:Nucleosomes; C103337:RSC complex, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors