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rdf:type |
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lifeskim:mentions |
umls-concept:C0036708,
umls-concept:C0085862,
umls-concept:C0127400,
umls-concept:C0162493,
umls-concept:C1167093,
umls-concept:C1299583,
umls-concept:C1314939,
umls-concept:C1363844,
umls-concept:C1413196,
umls-concept:C1549571,
umls-concept:C1608386,
umls-concept:C1704675
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pubmed:issue |
4
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pubmed:dateCreated |
1999-11-26
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pubmed:abstractText |
Mutations in three subunits of the SWI/SNF complex and in the Med2p subunit of the SRB/mediator of pol II holoenzyme impaired Gcn4p-activated transcription of HIS3 without reducing Gcn4p-independent transcription of this gene. Recombinant Gcn4p interacted with SWI/SNF and SRB/mediator subunits in cell extracts in a manner dependent on the same hydrophobic clusters in the Gcn4p activation domain; however, higher concentrations of Gcn4p were required for binding to SWI/SNF versus SRB/mediator subunits. In addition, SRB/mediator and SWI/SNF subunits did not coimmunopreciptate from the extracts. These findings, together with the fact that Gcn4p specifically interacted with purified SWI/SNF, strongly suggest that Gcn4p independently recruits SWI/SNF and holoenzyme to its target promoters in the course of activating transcription.
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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/DNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SRB2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/imidazoleglycerolphosphate...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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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 |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
657-64
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10549298-DNA Polymerase II,
pubmed-meshheading:10549298-DNA-Binding Proteins,
pubmed-meshheading:10549298-Fungal Proteins,
pubmed-meshheading:10549298-Gene Expression Regulation, Fungal,
pubmed-meshheading:10549298-Hydro-Lyases,
pubmed-meshheading:10549298-Mediator Complex,
pubmed-meshheading:10549298-Mutation,
pubmed-meshheading:10549298-Nuclear Proteins,
pubmed-meshheading:10549298-Nucleosomes,
pubmed-meshheading:10549298-Protein Binding,
pubmed-meshheading:10549298-Protein Kinases,
pubmed-meshheading:10549298-Recombinant Proteins,
pubmed-meshheading:10549298-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10549298-Transcription Factors,
pubmed-meshheading:10549298-Transcriptional Activation,
pubmed-meshheading:10549298-Yeasts
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pubmed:year |
1999
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pubmed:articleTitle |
Transcriptional activation by Gcn4p involves independent interactions with the SWI/SNF complex and the SRB/mediator.
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pubmed:affiliation |
Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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