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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5274
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pubmed:dateCreated |
1996-8-12
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pubmed:abstractText |
The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/SNF2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
513-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8662543-Adenosine Triphosphatases,
pubmed-meshheading:8662543-Adenosine Triphosphate,
pubmed-meshheading:8662543-Base Sequence,
pubmed-meshheading:8662543-Binding Sites,
pubmed-meshheading:8662543-DNA, Fungal,
pubmed-meshheading:8662543-DNA-Binding Proteins,
pubmed-meshheading:8662543-Deoxyribonuclease I,
pubmed-meshheading:8662543-Fungal Proteins,
pubmed-meshheading:8662543-Histones,
pubmed-meshheading:8662543-Molecular Sequence Data,
pubmed-meshheading:8662543-Nuclear Proteins,
pubmed-meshheading:8662543-Nucleosomes,
pubmed-meshheading:8662543-Saccharomyces cerevisiae,
pubmed-meshheading:8662543-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8662543-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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