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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-2-24
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pubmed:abstractText |
Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFIIIA of the 5S RNA gene within model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones also facilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restricting transcription factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules.
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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, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 5S,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIA,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
73-84
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8422685-Acetylation,
pubmed-meshheading:8422685-Animals,
pubmed-meshheading:8422685-Chickens,
pubmed-meshheading:8422685-DNA, Ribosomal,
pubmed-meshheading:8422685-HeLa Cells,
pubmed-meshheading:8422685-Histones,
pubmed-meshheading:8422685-Humans,
pubmed-meshheading:8422685-Nucleosomes,
pubmed-meshheading:8422685-RNA, Ribosomal, 5S,
pubmed-meshheading:8422685-Transcription Factor TFIIA,
pubmed-meshheading:8422685-Transcription Factors,
pubmed-meshheading:8422685-Xenopus,
pubmed-meshheading:8422685-Xenopus laevis
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pubmed:year |
1993
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pubmed:articleTitle |
A positive role for histone acetylation in transcription factor access to nucleosomal DNA.
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pubmed:affiliation |
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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