Document Detail

Mechanism of chromatin remodeling.
MedLine Citation:
PMID:  20142505     Owner:  NLM     Status:  MEDLINE    
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.
Yahli Lorch; Barbara Maier-Davis; Roger D Kornberg
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-02-08
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  107     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-25     Completed Date:  2010-04-05     Revised Date:  2013-05-30    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3458-62     Citation Subset:  IM    
Department of Structural Biology, Stanford School of Medicine, Stanford, CA 94305, USA.
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MeSH Terms
Adenosine Triphosphate / analogs & derivatives,  chemistry,  metabolism
Chromatin Assembly and Disassembly*
DNA / metabolism
DNA-Binding Proteins / chemistry,  metabolism*
Deoxyribonuclease I / chemistry
Exodeoxyribonucleases / chemistry
Histones / metabolism*
Nucleosomes / metabolism*
Saccharomyces cerevisiae Proteins / chemistry,  metabolism*
Transcription Factors / chemistry,  metabolism*
Grant Support
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Histones; 0/Nucleosomes; 0/RSC complex, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 35094-46-3/adenosine 5'-O-(3-thiotriphosphate); 56-65-5/Adenosine Triphosphate; 9007-49-2/DNA; EC 3.1.-/Exodeoxyribonucleases; EC III; EC I

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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