| Mechanism of chromatin remodeling. | |
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MedLine Citation:
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PMID: 20142505 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Yahli Lorch; Barbara Maier-Davis; Roger D Kornberg |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2010-02-08 |
Journal Detail:
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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:
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Created Date: 2010-02-25 Completed Date: 2010-04-05 Revised Date: 2010-09-27 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 3458-62 Citation Subset: IM |
Affiliation:
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Department of Structural Biology, Stanford School of Medicine, Stanford, CA 94305, USA. lorch@stanford.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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analogs & derivatives,
chemistry,
metabolism Animals Chromatin Assembly and Disassembly* DNA / metabolism DNA-Binding Proteins / chemistry, metabolism* Deoxyribonuclease I / chemistry Exodeoxyribonucleases / chemistry Histones / metabolism* Hydrolysis Nucleosomes / metabolism* Rats Saccharomyces cerevisiae Proteins / chemistry, metabolism* Transcription Factors / chemistry, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM36659/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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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 3.1.11.2/exodeoxyribonuclease III; EC 3.1.21.1/Deoxyribonuclease I |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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