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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-10-10
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pubmed:databankReference |
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pubmed:abstractText |
Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
449-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14536084-Adenosine Triphosphatases,
pubmed-meshheading:14536084-Amino Acid Sequence,
pubmed-meshheading:14536084-Animals,
pubmed-meshheading:14536084-Binding Sites,
pubmed-meshheading:14536084-Chromatin,
pubmed-meshheading:14536084-Crystallography, X-Ray,
pubmed-meshheading:14536084-Drosophila melanogaster,
pubmed-meshheading:14536084-Gene Deletion,
pubmed-meshheading:14536084-Models, Molecular,
pubmed-meshheading:14536084-Molecular Sequence Data,
pubmed-meshheading:14536084-Nucleosomes,
pubmed-meshheading:14536084-Protein Binding,
pubmed-meshheading:14536084-Protein Conformation,
pubmed-meshheading:14536084-Protein Structure, Tertiary,
pubmed-meshheading:14536084-Proto-Oncogene Proteins c-myb,
pubmed-meshheading:14536084-Sequence Homology, Amino Acid,
pubmed-meshheading:14536084-Time Factors,
pubmed-meshheading:14536084-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.
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pubmed:affiliation |
European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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