Requirement for acidic amino acid residues immediately N-terminal to the conserved domain of Saccharomyces cerevisiae TFIID.
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Transcription factor TFIID induces DNA bending upon binding to the TATA element.STD1 (MSN3) interacts directly with the TATA-binding protein and modulates transcription of the SUC2 gene of Saccharomyces cerevisiae.Effect of the non-conserved N-terminus on the DNA binding activity of the yeast TATA binding protein.Evolution of sequence repetition and gene duplications in the TATA-binding protein TBP (TFIID).Metal-regulated transcription in eukaryotesThe conserved core domain of the human TATA binding protein is sufficient to assemble the multisubunit RNA polymerase I-specific transcription factor SL1.The yeast TATA-binding protein (TBP) core domain assembles with human TBP-associated factors into a functional TFIID complexTATA-binding protein and nuclear differentiation in Tetrahymena thermophilaIsolation of STD1, a high-copy-number suppressor of a dominant negative mutation in the yeast TATA-binding protein.TFIIA induces conformational changes in TFIID via interactions with the basic repeatBiochemical and genetic characterization of a yeast TFIID mutant that alters transcription in vivo and DNA binding in vitroSimple derivation of TFIID-dependent RNA polymerase II transcription systems from Schizosaccharomyces pombe and other organisms, and factors required for transcriptional activation.Identification of human TFIID components and direct interaction between a 250-kDa polypeptide and the TATA box-binding protein (TFIID tau).Yeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics.Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding proteinA yeast TATA-binding protein mutant that selectively enhances gene expression from weak RNA polymerase II promoters.Shutoff of RNA polymerase II transcription by poliovirus involves 3C protease-mediated cleavage of the TATA-binding protein at an alternative site: incomplete shutoff of transcription interferes with efficient viral replication.The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters.The Drosophila TATA binding protein contains a strong but masked activation domain.Engineering TATA-binding protein Spt15 to improve ethanol tolerance and production in
P2860
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P2860
Requirement for acidic amino acid residues immediately N-terminal to the conserved domain of Saccharomyces cerevisiae TFIID.
description
1991 nî lūn-bûn
@nan
1991年の論文
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年學術文章
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1991年學術文章
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1991年學術文章
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name
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@ast
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@en
type
label
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@ast
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@en
prefLabel
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@ast
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@en
P2093
P2860
P1433
P1476
Requirement for acidic amino a ...... accharomyces cerevisiae TFIID.
@en
P2093
P2860
P304
P407
P577
1991-07-01T00:00:00Z