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Crystal structure of a TFIIB-TBP-TATA element ternary complex
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Several TAFs are components of both TFIID and histone acetyltransferase complexes. This paper suggests that the histone H2B-like TAF may contact different proteins within each complex.
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0032765083
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Three dimensional structure of the human TFIID-IIA-IIB complex
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•] detail the first low resolution picture of TFIID structure using electron microscopy. A central domain containing TBP is flanked by two other domains in a roughly horse shoe shaped complex.
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Andel, F.I.I.I.1
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Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC
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•], this paper shows low resolution structures of both TFIID and a TAF-containing HAT complex. The two structures are remarkably similar.
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The authors performed an in vitro analysis of transcription complex assembly using an immobilized template assay and various yeast transcription factor mutants and make a case for two kinetically stable intermediates. The first intermediate consists of TFIID and TFIIA bound to the promoter, the second is a fully assembled transcription complex.
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23
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TFIIA regulates TBP and TFIID dimers
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Although TBP can dimerize in vitro, there was substantial skepticism about whether this has any physiological relevance. This paper and others from the same laboratory make a case for dimerization being important in vivo. In addition to its role in stabilization of TBP at the promoter, TFIIA is found to affect TBP's monomer-dimer transition.
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Coleman R.A., Taggart A.K., Burma S., Chicca J.J.I.I., Pugh B.F. TFIIA regulates TBP and TFIID dimers. Mol Cell. 4:1999;451-457. Although TBP can dimerize in vitro, there was substantial skepticism about whether this has any physiological relevance. This paper and others from the same laboratory make a case for dimerization being important in vivo. In addition to its role in stabilization of TBP at the promoter, TFIIA is found to affect TBP's monomer-dimer transition.
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Coleman, R.A.1
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0033500157
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Analysis of TFIIA function in vivo: Evidence for a role in TATA-binding protein recruitment and gene-specific activation
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Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- And developmentally regulated promoter
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This remarkable paper describes the uses of chromatin immunoprecipitation to monitor the dynamics of transcription-factor association following induction of the yeast HO gene. A clear, ordered arrival of activators, chromatin remodeling machinery, and histone acetyltransferase complexes allows a strong prediction of the events required to turn on expression of a gene.
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Binding of TBP to promoters in vivo is stimulated by activators and requires Pol II holoenzyme
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••], the authors monitored the association of TBP with promoters using chromatin immunoprecipitation. Crosslinking of TBP to promoters correlates strongly with transcription levels and is generally dependent upon activators and the mediator complex.
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••], the authors monitored the association of TBP with promoters using chromatin immunoprecipitation. Crosslinking of TBP to promoters correlates strongly with transcription levels and is generally dependent upon activators and the mediator complex.
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Kuras, L.1
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28
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0033542484
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Enhancement of TBP binding by activators and general transcription factors
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•], but they also show that TBP crosslinking is dependent upon TFIIB. TBP crosslinking shows promoter-specific effects of a TAF mutation. Furthermore, the Mot1 protein is shown to reduce levels of TBP crosslinking at uninduced genes and at nonpromoter sequences.
-
•], but they also show that TBP crosslinking is dependent upon TFIIB. TBP crosslinking shows promoter-specific effects of a TAF mutation. Furthermore, the Mot1 protein is shown to reduce levels of TBP crosslinking at uninduced genes and at nonpromoter sequences.
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The general transcription factors IIA, IIB, IIF, and IIE are required for RNA polymerase II transcription from the human U1 small nuclear RNA promoter
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Most snRNA genes of higher eukaryotes are transcribed by pol II but use a TBP-complex distinct from TFIID (see [31]). This paper shows that they still require most, if not all, of the basal factors used by more typical TATA-containing promoters.
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Kuhlman T.C., Cho H., Reinberg D., Hernandez N. The general transcription factors IIA, IIB, IIF, and IIE are required for RNA polymerase II transcription from the human U1 small nuclear RNA promoter. Mol Cell Biol. 19:1999;2130-2141. Most snRNA genes of higher eukaryotes are transcribed by pol II but use a TBP-complex distinct from TFIID (see [31]). This paper shows that they still require most, if not all, of the basal factors used by more typical TATA-containing promoters.
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Teichmann M., Wang Z., Martinez E., Tjernberg A., Zhang D., Vollmer F., Chait B.T., Roeder R.G. Human TATA-binding protein-related factor-2 (hTRF2) stably associates with hTFIIA in HeLa cells. Proc Natl Acad Sci USA. 96:1999;13720-13725.
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A human TATA binding protein-related protein with altered DNA binding specificity inhibits transcription from multiple promoters and activators
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Moore P.A., Ozer J., Salunek M., Jan G., Zerby D., Campbell S., Lieberman P.M. A human TATA binding protein-related protein with altered DNA binding specificity inhibits transcription from multiple promoters and activators. Mol Cell Biol. 19:1999;7610-7620.
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Rabenstein M.D., Zhou S., Lis J.T., Tjian R. TATA box-binding protein (TBP)-related factor 2 (TRF2), a third member of the TBP family. Proc Natl Acad Sci USA. 96:1999;4791-4796.
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Reconstitution of the transcription factor TFIIH: Assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
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Tirode F., Busso D., Coin F., Egly J.M. Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Mol Cell. 3:1999;87-95. The remarkable technical feat of reconstituting the multisubunit TFIIH complex is documented here; it will open the door to interesting mutational analyses of the individual subunits.
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