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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1997-6-16
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pubmed:abstractText |
To investigate the potential mechanisms by which the SWI/SNF complex differentially regulates different genes we have tested whether transcription factors with diverse DNA binding domains were able to exploit nucleosome disruption by SWI/SNF. In addition to GAL4-VP16, the SWI/SNF complex stimulated nucleosome binding by the Zn2+ fingers of Sp1, the basic helix-loop-helix domain of USF, and the rel domain of NF-kappaB. In each case SWI/SNF action resulted in the formation of a stable factor-nucleosome complex that persisted after detachment of SWI/SNF from the nucleosome. Thus, stimulation of factor binding by SWI/SNF appears to be universal. The degree of SWI/SNF stimulation of nucleosome binding by a factor appears to be inversely related to the extent that binding is inhibited by the histone octamer. Cooperative binding of 5 GAL4-VP16 dimers to a 5-site nucleosome enhanced GAL4 binding relative to a single-site nucleosome, but this also reduced the degree of stimulation by SWI/SNF. The SWI/SNF complex increased the affinity of 5 GAL4-VP16 dimers for nucleosomes equal to that of DNA but no further. Similarly, multimerized NF-kappaB sites enhanced nucleosome binding by NF-kappaB and reduced the stimulatory effect of SWI/SNF. Thus, cooperative binding of factors to nucleosomes is partially redundant with the function of the SWI/SNF complex.
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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 Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gal-VP16,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNF11 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SNF12 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SWI3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sp1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12642-9
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pubmed:dateRevised |
2009-7-3
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pubmed:meshHeading |
pubmed-meshheading:9139720-Adenosine Triphosphate,
pubmed-meshheading:9139720-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9139720-DNA,
pubmed-meshheading:9139720-DNA Footprinting,
pubmed-meshheading:9139720-DNA-Binding Proteins,
pubmed-meshheading:9139720-Fungal Proteins,
pubmed-meshheading:9139720-Macromolecular Substances,
pubmed-meshheading:9139720-Models, Molecular,
pubmed-meshheading:9139720-NF-kappa B,
pubmed-meshheading:9139720-Nuclear Proteins,
pubmed-meshheading:9139720-Nucleic Acid Conformation,
pubmed-meshheading:9139720-Nucleosomes,
pubmed-meshheading:9139720-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9139720-Sp1 Transcription Factor,
pubmed-meshheading:9139720-Trans-Activators,
pubmed-meshheading:9139720-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology and The Center for Gene Regulation, The Pennsylvania State University, University Park, Pennsylvania 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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