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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2001-2-2
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pubmed:abstractText |
The TATA box binding protein (TBP) is required by all three RNA polymerases for the promoter-specific initiation of transcription. All eukaryotic TBP-DNA complexes observed in crystal structures show the conserved C-terminal domain of TBP (TBPc) bound to the TATA box in a single orientation that is consistent with assembly of a preinitiation complex (PIC) possessing a unique polarity. The binding of TBP to the TATA box is believed to orient the PIC correctly on the promoter and can function as the rate-limiting step in PIC assembly. Previous work performed with TBP from Saccharomyces cerevisiae (yTBP) showed that, despite the oriented binding of eukaryotic TBP observed in crystal structures, yTBP in solution does not orient itself uniquely on the adenovirus major late promoter (AdMLP) TATA box. Instead, yTBP binds the AdMLP as a mixture of two orientational isomers that are related by a 180 degree rotation about the pseudo-dyad axis of the complex. In addition, these orientational isomers are not restricted to the 8 bp TATA box, but rather bind a distribution of sites that partially overlap the TATA box. Two members of the PIC, general transcription factor (TF) IIB and TFIIA individually enhance the orientational and axial specificity of yTBP binding to the TATA box, but fail to fix yTBP in a single orientation or a unique position on the promoter.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1074-5521
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
601-10
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11048951-Adenoviridae,
pubmed-meshheading:11048951-Base Sequence,
pubmed-meshheading:11048951-DNA,
pubmed-meshheading:11048951-DNA Footprinting,
pubmed-meshheading:11048951-DNA-Binding Proteins,
pubmed-meshheading:11048951-Deoxyribonuclease I,
pubmed-meshheading:11048951-Holoenzymes,
pubmed-meshheading:11048951-Models, Molecular,
pubmed-meshheading:11048951-Mutation,
pubmed-meshheading:11048951-Oligodeoxyribonucleotides,
pubmed-meshheading:11048951-Protein Binding,
pubmed-meshheading:11048951-Protein Conformation,
pubmed-meshheading:11048951-Protein Structure, Tertiary,
pubmed-meshheading:11048951-RNA Polymerase II,
pubmed-meshheading:11048951-Saccharomyces cerevisiae,
pubmed-meshheading:11048951-TATA Box,
pubmed-meshheading:11048951-TATA-Box Binding Protein,
pubmed-meshheading:11048951-Transcription Factor TFIIA,
pubmed-meshheading:11048951-Transcription Factor TFIIB,
pubmed-meshheading:11048951-Transcription Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Virtually unidirectional binding of TBP to the AdMLP TATA box within the quaternary complex with TFIIA and TFIIB.
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pubmed:affiliation |
Department of Chemistry, Yale University, New Haven, CT 06511-8118, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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