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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2003-2-24
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pubmed:abstractText |
An important goal is to identify the direct activation domain (AD)-interacting components of the transcriptional machinery within the context of native complexes. Toward this end, we first demonstrate that the multisubunit TFIID, SAGA, mediator, and Swi/Snf coactivator complexes from transcriptionally competent whole-cell yeast extracts were all capable of specifically interacting with the prototypic acidic ADs of Gal4 and VP16. We then used hexahistidine tags as genetically introduced activation domain-localized cross-linking receptors. In combination with immunological reagents against all subunits of TFIID and SAGA, we systematically identified the direct AD-interacting subunits within the AD-TFIID and AD-SAGA coactivator complexes enriched from whole-cell extracts and confirmed these results using purified TFIID and partially purified SAGA. Both ADs directly cross-linked to TBP and to a subset of TFIID and SAGA subunits that carry histone-fold motifs.
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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/ADA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TAF9 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/TEV protease,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
28
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6779-86
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12501245-Acetyltransferases,
pubmed-meshheading:12501245-Amino Acid Motifs,
pubmed-meshheading:12501245-Binding Sites,
pubmed-meshheading:12501245-Cross-Linking Reagents,
pubmed-meshheading:12501245-Endopeptidases,
pubmed-meshheading:12501245-Histidine,
pubmed-meshheading:12501245-Histone Acetyltransferases,
pubmed-meshheading:12501245-Histones,
pubmed-meshheading:12501245-Models, Biological,
pubmed-meshheading:12501245-Protein Binding,
pubmed-meshheading:12501245-Protein Folding,
pubmed-meshheading:12501245-Protein Structure, Tertiary,
pubmed-meshheading:12501245-Recombinant Fusion Proteins,
pubmed-meshheading:12501245-Recombinant Proteins,
pubmed-meshheading:12501245-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12501245-TATA-Binding Protein Associated Factors,
pubmed-meshheading:12501245-Transcription, Genetic,
pubmed-meshheading:12501245-Transcription Factor TFIID,
pubmed-meshheading:12501245-Transcription Factors,
pubmed-meshheading:12501245-Yeasts
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pubmed:year |
2003
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pubmed:articleTitle |
Use of a genetically introduced cross-linker to identify interaction sites of acidic activators within native transcription factor IID and SAGA.
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pubmed:affiliation |
Department of Microbiology, Goethe University, 60439 Frankfurt am Main, Germany.
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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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