Mechanism of chromatin remodeling.
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.
Department of Structural Biology, Stanford School of Medicine, Stanford, CA 94305, USA. lorch@stanford.edu
Yahli
Y
Lorch
Barbara
B
Maier-Davis
Roger D
RD
Kornberg
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D042002:Chromatin Assembly and Disassembly; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D003850:Deoxyribonuclease I / Q000737:chemistry; D005090:Exodeoxyribonucleases / Q000737:chemistry; D006657:Histones / Q000378:metabolism*; D006868:Hydrolysis; D009707:Nucleosomes / Q000378:metabolism*; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*
D004268:DNA-Binding Proteins; D006657:Histones; D009707:Nucleosomes; C103337:RSC complex, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D004247:DNA; D005090:Exodeoxyribonucleases; C020133:exodeoxyribonuclease III; D003850:Deoxyribonuclease I