Document Detail


Nucleosome remodeling by the human SWI/SNF complex requires transient global disruption of histone-DNA interactions.
MedLine Citation:
PMID:  11997502     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We utilized a site-specific cross-linking technique to investigate the mechanism of nucleosome remodeling by hSWI/SNF. We found that a single cross-link between H2B and DNA virtually eliminates the accumulation of stably remodeled species as measured by restriction enzyme accessibility assays. However, cross-linking the histone octamer to nucleosomal DNA does not inhibit remodeling as monitored by DNase I digestion assays. Importantly, we found that the restriction enzyme-accessible species can be efficiently cross-linked after remodeling and that the accessible state does not require continued ATP hydrolysis. These results imply that the generation of stable remodeled states requires at least transient disruption of histone-DNA interactions throughout the nucleosome, while hSWI/SNF-catalyzed disruption of just local histone-DNA interactions yields less-stable remodeled states that still display an altered DNase I cleavage pattern. The implications of these results for models of the mechanism of SWI/SNF-catalyzed nucleosome remodeling are discussed.
Authors:
Sayura Aoyagi; Geeta Narlikar; Chunyang Zheng; Saïd Sif; Robert E Kingston; Jeffrey J Hayes
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  22     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-05-08     Completed Date:  2002-06-06     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3653-62     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York 14642, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Cross-Linking Reagents
DNA / metabolism*
DNA-Binding Proteins / chemistry,  metabolism*
Deoxyribonuclease I
Histones / metabolism*
Humans
Macromolecular Substances
Models, Biological
Nucleosomes / metabolism*
Xenopus
Grant Support
ID/Acronym/Agency:
R01GM52426/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Cross-Linking Reagents; 0/DNA-Binding Proteins; 0/Histones; 0/Macromolecular Substances; 0/Nucleosomes; 9007-49-2/DNA; 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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