Source:http://linkedlifedata.com/resource/pubmed/id/15269206
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
41
|
| pubmed:dateCreated |
2004-10-6
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| pubmed:abstractText |
The transcription factor NF-kappaB is involved in the transcriptional control of more than 150 genes, but the way it acts at the level of nucleosomal templates is not known. Here we report on a study examining the interaction of NF-kappaB p50 with its DNA recognition sequence in a positioned nucleosome. We demonstrate that NF-kappaB p50 was able to bind to the nucleosome with an apparent association constant close to that for free DNA. In agreement with this, the affinity of NF-kappaB p50 binding does not depend on the localization of its recognition sequence relative to the nucleosome dyad axis. In addition, the binding of NF-kappaB p50 does not induce eviction of histones and does not perturb the overall structure of the nucleosome. The NF-kappaB p50-nucleosome complex exhibits, however, local structural alterations within the NF-kappaB p50 recognition site. Importantly, these alterations were very similar to those found in the NF-kappaB p50-DNA complex. Our data suggest that NF-kappaB p50 can accommodate the distorted, bent DNA within the nucleosome. This peculiar property of NF-kappaB p50 might have evolved to meet the requirements for its function as a central switch for stress responses.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyl Radical,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B p50 Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.
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| pubmed:issnType |
Print
|
| pubmed:day |
8
|
| pubmed:volume |
279
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
42374-82
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15269206-Animals,
pubmed-meshheading:15269206-Binding Sites,
pubmed-meshheading:15269206-Cryoelectron Microscopy,
pubmed-meshheading:15269206-DNA,
pubmed-meshheading:15269206-Deoxyribonuclease I,
pubmed-meshheading:15269206-Dose-Response Relationship, Drug,
pubmed-meshheading:15269206-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15269206-Histones,
pubmed-meshheading:15269206-Hydroxyl Radical,
pubmed-meshheading:15269206-Lasers,
pubmed-meshheading:15269206-NF-kappa B,
pubmed-meshheading:15269206-NF-kappa B p50 Subunit,
pubmed-meshheading:15269206-Nucleosomes,
pubmed-meshheading:15269206-Oligonucleotides,
pubmed-meshheading:15269206-Plasmids,
pubmed-meshheading:15269206-Protein Binding,
pubmed-meshheading:15269206-Time Factors,
pubmed-meshheading:15269206-Transcription, Genetic,
pubmed-meshheading:15269206-Ultraviolet Rays,
pubmed-meshheading:15269206-Xenopus,
pubmed-meshheading:15269206-Xenopus laevis
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| pubmed:year |
2004
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| pubmed:articleTitle |
The histone octamer is invisible when NF-kappaB binds to the nucleosome.
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| pubmed:affiliation |
Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche Cedex, France.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|