Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA box

Horikoshi, Masami; Wang, C K; Fujii, Hiroshi; Cromlish, James A.; Weil, P A; Roeder, Robert G.

doi:10.1038/341299a0

Cited by 303 publications

(169 citation statements)

References 37 publications

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“…Since these lysine residues are conserved between species (for a review, see reference 18), they are likely to play an important role in the interaction between TFIIA and TFIID from HeLa cells. The basic lysine repeat region of TFIID was proposed as a potential target for acidic upstream activators (22) on the basis of its potential for forming an amphipathic helix with a high basic charge and in light of previous suggestions of activation mechanisms involving direct interactions between upstream activators and TFIID (20,37). Indeed, the prototypic acidic upstream activator VP16 was shown to interact directly with both yeast and human TFIID (50), although it also was demonstrated to interact more strongly with the basic residue-rich TFIIB (29).…”

Section: Resultsmentioning

confidence: 99%

TFIIA induces conformational changes in TFIID via interactions with the basic repeat.

Lee¹,

DeJong²,

Hashimoto³

et al. 1992

Mol. Cell. Biol.

113

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. Components of the general transcription machinery are functionally conserved among eukaryotes, as evidenced by the ability of TFIIA and TFIID from Saccharomyces cerevisiae to substitute for the corresponding HeLa factors in vitro (2,4,14,21). TFIID binding to the TATA element initiates the assembly of the other factors into a preinitiation complex (1,34,54,55). Yeast TFIID (yTFIID) and the TATA-binding subunit of TFIID (designated TFIIDT or TBP) from higher eukaryotes contain a highly conserved 180-amino-acid C-terminal domain and divergent N-terminal regions (3, 8, 11, 15-18, 22, 25, 33, 35, 47, 52). Biochemical and genetic studies have shown that the conserved C-terminal domain of TFIID'T contains all of the essential regions for DNA binding, transcription initiation, and species specificity (6,13,23,36,40,56,57). TFIID shows unusual binding properties compared with those of the other sequence-specific DNA binding proteins: e.g., a temperature dependency and slow on and off rates (20,28,48).The binding of TFIID to DNA can be stimulated by TFIIA, apparently by direct interactions of TFIIA with TFIID (1, 30). The ability of TFIIA to interact directly with TFIID has allowed efficient purification of this protein from both HeLa cells (7, 7a, 53) and S. cerevisiae (38). TFIIA has been shown to function at an early step in the formation of a preinitiation complex (10,41). In contrast to the absolute requirement for the other transcription factors, a consistent requirement for TFIIA in the initiation of transcription has not been observed (for a review, see reference 42). This may reflect the nature of the TFIID-employed cross-contamination of factors, the presence of alternative factors, or the * Corresponding author. particular conditions of transcription (1, 7, 31, 32, 41-45, 51, 55). For example, the transcription factor TFIIG initially was identified as a factor which substitutes for TFIIA in basal transcription and which further stimulates TFIIAsaturated transcription (51). The initiator-binding transcription factor TFII-I (43) has been shown to substitute for TFIIA in transcription of the adenovirus major late (AdML) core promoter, suggesting alternative pathways for the formation of preinitiation complexes, possibly with different rates of formation and/or complex stabilities (for a review, see reference 42; 42a). The function(s) of TFIIA in preinitiation complex formation and transcription initiation has yet to be elucidated.Interactions of negative cofactors which bind competitively with TFIIA to TFIID on DNA have also been reported elsewhere (31,32). These negative cofactors dissociate TFIIA or TFIIB from the intermediary preinitiation complexes to produce nonproductive preinitiation complexes (negative cofactor-TFIID-DNA complexes) that result in repressed promoter states (for a review, see reference 42). Preincubation of promoters with TFIIA and native TFIID was shown to increase basal levels of transcription with corresponding decreases in promoter stimulation by activators, suggesting the involvem...

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Section: Resultsmentioning

confidence: 99%

TFIIA induces conformational changes in TFIID via interactions with the basic repeat.

Lee¹,

DeJong²,

Hashimoto³

et al. 1992

Mol. Cell. Biol.

113

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“…The amino acid residues involved in these DNA contacts are nearly 100% conserved, with only a single variation in which Arg-204 in hTBP changes to Lys-110 in yTBP and Lys-68 in aTBP (2). The N-terminal domain is, in contrast, heterogenous between the yeast (60 amino acids (14)) and human (159 amino acids (15)) proteins and severely truncated in the A. thaliana protein (18 amino acids (16)). …”

mentioning

confidence: 97%

Native Human TATA-binding Protein Simultaneously Binds and Bends Promoter DNA without a Slow Isomerization Step or TFIIB Requirement

Masters

Parkhurst

Daugherty

et al. 2003

Journal of Biological Chemistry

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The association of TATA-binding protein (TBP) with promoter DNA is central to the initiation and regulation of eukaryotic protein synthesis. Our laboratory has previously conducted detailed investigations of this interaction using yeast TBP and seven consensus and variant TATA sequences. We have now investigated this key interaction using human TBP and the TATA sequence from the adenovirus major late promoter (AdMLP). Recombinant native human protein was used together with fluorescently labeled DNA, allowing real time data acquisition in solution. We find that the wild-type hTBP-DNA AdMLP reaction is characterized by high affinity (K d ‫؍‬ 5 nM), simultaneous binding and DNA bending, and rapid formation of a stable human TBP-DNA complex having DNA bent ϳ100°. These data allow, for the first time, a direct comparison of the reactions of the full-length, native human and yeast TBPs with a consensus promoter, studied under identical conditions. The general reaction characteristics are similar for the human and yeast proteins, although the details differ and the hTBP wt -induced bend is more severe. This directly measured hTBP wt -DNA AdMLP interaction differs fundamentally from a recently published hTBP wt -DNA AdMLP model characterized by low affinity ( M) binding and an unstable complex requiring either a 30-min isomerization or TFIIB to achieve DNA bending. Possible sources of these significant differences are discussed.The recognition and binding of promoter TATA sequences (DNA TATA ) 1 by the TATA-binding protein (TBP) is central to the initiation and regulation of gene transcription in eukaryotes. The importance of the TBP-DNA TATA interaction has prompted extensive biochemical and biophysical investigations, which have revealed complex binding mechanisms and dramatic TBP-induced helical distortion, including DNA TATA bending and unwinding (see Ref. 1 and references therein and Refs. 2-11). The extent of the DNA TATA bending is TATA sequence-dependent in solution (8,9,12,13). Because these collective results have been obtained using different TBPs, full-length and truncated proteins, and diverse experimental conditions, key issues relating to the behavior and structure of TBP-promoter complexes remain unresolved.The 180-residue C-terminal DNA binding domains (CTD) of the TBPs from yeast (yTBP), human (hTBP), and Arabidopsis thaliana (aTBP) are highly conserved, with greater than 80% homology and with generally conservative substitutions in the remainder. The pseudo-symmetric TBP CTD contacts the duplex along the distorted minor groove via interactions that are largely non-polar and hydrophobic. The amino acid residues involved in these DNA contacts are nearly 100% conserved, with only a single variation in which Arg-204 in hTBP changes to Lys-110 in yTBP and Lys-68 in aTBP (2). The N-terminal domain is, in contrast, heterogenous between the yeast (60 amino acids (14)) and human (159 amino acids (15)) proteins and severely truncated in the A. thaliana protein (18 amino acids (16)).How these similarities and di...

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“…We found that the C-terminus of TBP was essential for TBP-TBP interaction. The C-terminal domain of TBP has multiple motifs/domains for DNA binding (basic repeat, direct repeat and sigma homology) (38)(39)(40). X-ray crystallography has shown that TBP forms a saddle shape structure (23).…”

Section: Multinerization Of Tbp In Solutionmentioning

confidence: 99%

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

Kato

Makino²,

Kishimoto³

et al. 1994

Nucl Acids Res

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The conformational states of the mouse TATA-binding protein (TBP) in solution were studied. A histidine tag and a factor Xa recognition site-carrying mouse TBP was expressed in E.coli, highly purified, and its fundamental functions as a TBP were demonstrated. We analyzed the molecular states of mouse TBP by gel filtration and glycerol gradient sedimentation, and found that TBP forms heterogeneous multimers in solution. Direct binding of TBP molecules to each other was proven by the far-Western procedure. Analyses using TBPs truncated at the N-and C-termini demonstrated that the functionally important C-terminal domain was responsible for homomultimer formation, and the N-terminal domain enhances multimerization. Furthermore, it was found that the TATA sequence dissociates homomultimers, and only monomeric TBP binds to the TATA-box. We suggest that TBP shares structural motifs in the C-terminal conserved domain for intermolecular interaction and TATA-binding.

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Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA box

Cited by 303 publications

References 37 publications

TFIIA induces conformational changes in TFIID via interactions with the basic repeat.

TFIIA induces conformational changes in TFIID via interactions with the basic repeat.

Native Human TATA-binding Protein Simultaneously Binds and Bends Promoter DNA without a Slow Isomerization Step or TFIIB Requirement

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

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