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Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A full-length cDNA clone encoding the TATA-binding protein (TBP), the DNA-binding component of the general transcription factor TFIID was cloned from potato tubers. The DNA sequence of this cDNA indicated that the predicted potato protein was very similar to cloned TBP from other species. Genomic southern analysis showed that TBP is encoded in the potato genome as a low-copy-number sequence. The potato TBP cDNA clone was shown to encode a functional protein that interacts in a sequence-specific way with the promoter region of a class-1 potato patatin gene. Functional analysis of carboxy-terminal truncated derivatives of potato TBP showed that important components of DNA binding were located within the carboxy-terminal 54 amino acids. Kinetic and thermodynamic properties of in vitro synthesised potato TBP were investigated, and demonstrated strict salt and temperature preferences for maximum DNA binding activity. In addition on and off-rate measurements showed that both association and dissociation of TBP from DNA is slow. The specific and the non-specific equilibrium constants Ks and Kn were calculated as 5 x 10(9) M-1 and 3.65 x 10(4) M-1 respectively. These results indicate that the interaction of potato TBP with the patatin promoter is highly specific.
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PMID:DNA-binding properties of cloned TATA-binding protein from potato tubers. 137 67

A T7 RNA polymerase expression system has been used for the efficient expression of the yeast RNA polymerase general transcription factor TFIID (TFIIDY), the TATA-box factor (previously called BTF1) in Escherichia coli. Expression of the gene was performed at 25 degrees C instead of 37 degrees C to increase the total amount of soluble TFIIDY. Soluble TFIIDY was purified in three chromatographic steps and was eluted from the final column, a heparin-5PW HPLC column, in two peaks at 0.38 M (peak I) and 0.42 M (peak II) KCl in which this protein was 52% and greater than 95% pure, respectively. The protein in both peaks was active in an in vitro transcription assay. However, while TFIIDY from peak II was essentially indistinguishable from the material isolated from yeast, the protein of peak I differed in a number of biochemical characteristics, having a lower specific activity in an in vitro transcription assay and displaying an altered pattern of bands in a DNA band shift assay. Despite these differences, the proteins in both peaks have identical molecular weights on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, have indistinguishable N-terminal amino acid sequences, and apparently exist as monomers under the conditions used for the heparin-5PW chromatography.
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PMID:Expression in Escherichia coli: purification and properties of the yeast general transcription factor TFIID. 182 18

A gene for a putative homolog of TATA-binding protein (TBP) from Thermococcus celer has been expressed in Escherichia coli, and the function of the purified recombinant protein was studied in a Methanococcus-derived cell-free transcription system. Thermococcus TBP can replace archaeal transcription factor B (aTFB) in cell-free transcription reactions. This transcriptional activation is TATA box-dependent and occurs both on tRNA(Val) and protein-encoding genes as templates indicating that Thermococcus TBP is a general transcription factor. Antibodies raised against Thermococcus TBP bind to Methanococcus aTFB and inhibit a TFB activity. These findings demonstrate that Thermococcus TBP (like eucaryal TBPs) can direct specific transcription from TATA boxes.
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PMID:The translation product of the presumptive Thermococcus celer TATA-binding protein sequence is a transcription factor related in structure and function to Methanococcus transcription factor B. 762 58

The ubiquitous human POU domain protein, Oct-1, and the related B-cell protein, Oct-2, regulate transcription from a variety of eukaryotic genes by binding to a common cis-acting octamer element, 5'-ATTTGCAT-3'. The binding of Oct-1 and Oct-2 to the functionally important lipoprotein lipase (LPL) promoter octamer site was stimulated by the general transcription factor, TFIIB. Comparative analysis of the LPL, histone H2B (H2B), and herpes simplex virus ICPO gene promoter octamer sites revealed that nucleotide sequences within and flanking the octamer sequence determined the degree of TFIIB-mediated stimulation of Oct-1 DNA binding. TFIIB was found to decrease the rate of dissociation of Oct-1 from the LPL octamer site, whereas it increased the rate of association, as well as decreased the rate of dissociation, of Oct-1 from the H2B octamer site. A monoclonal antibody against TFIIB immunoprecipitated a ternary complex containing TFIIB, Oct-1, and the LPL and H2B octamer binding sites. TFIIB did not alter the DNase I footprints generated by Oct-1 on the LPL and H2B promoters. However, Oct-1 on the TATA-binding protein and TFIIB from footprinting the perfect TATA box sequence located 5' of the LPL, NF-Y binding site. In transfection experiments, transcription from the reporters containing the LPL octamer, and either the SV40 or the yeast transcription factor GAL4-dependent enhancers, initiated at a precise position within the octamer sequence. Transcription from reporters containing the H2B octamer and the SV40 enhancer initiated at several positions within and flanking the octamer site, whereas transcription initiated at a precise position within the octamer from reporters with both the H2B octamer and the GAL4-dependent enhancer. These results suggest that octamers and their flanking sequences play an important role in positioning the site of transcription initiation, and that this could be a function of the interaction of Oct-1 with TFIIB.
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PMID:Interaction of Oct-1 with TFIIB. Implications for a novel response elicited through the proximal octamer site of the lipoprotein lipase promoter. 764 49

Transcriptional activation of target genes by the human progesterone receptor is thought to involve direct or indirect protein-protein interactions between the progesterone receptor and general transcription factors. A key role in transcription plays the general factors. A key role in transcription plays the general transcription factor TFIID, a multiprotein complex consisting of the TATA-binding protein and several tightly associated factors (TAFs). TAFs have been shown to be required for activated transcription and are, thus, potential targets of activator proteins. Using in vitro interaction assays, we could identify specific interactions between the progesterone receptor and the TATA-binding protein-associated factor dTAFII110. The dTAFII110 domain responsible for the interaction is distinct from that reported to suffice for binding to Sp1. Somewhat surprisingly, deletion analysis indicated that the previously identified activation functions 1 and 2 of the progesterone receptor are not required for this interaction but pointed to an important role of the DNA binding domain. In cotransfection experiments and an in vitro transcription assay, the DNA binding domain of the progesterone receptor displayed significant activation potential. These findings, taken together, suggest that an interaction between the progesterone receptor and TAFII110 may represent an important step in the mechanism of activation.
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PMID:Identification of a transactivation function in the progesterone receptor that interacts with the TAFII110 subunit of the TFIID complex. 767 70

The general transcription factor TFIID is a multiprotein complex containing the TATA-binding protein and several associated factors (TAFs), some of which may function as coactivators that are essential for activated, but not basal, transcription. Here we describe the isolation and characterization of the first gene encoding a TAF protein. The deduced amino acid sequence of TAF110 revealed the presence of several glutamine- and serine/threonine-rich regions reminiscent of the protein-protein interaction domains of the regulatory transcription factor Sp1 that are involved in transcription activation and multimerization. In both Drosophila cells and yeast, TAF110 specifically interacts with the glutamine-rich activation domains of Sp1. Moreover, purified Sp1 selectively binds recombinant TAF110 in vitro. These findings taken together suggest that TAF110 may function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 and the TFIID complex.
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PMID:Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. 767 80

TATA-binding protein (TBP) is a general transcription factor involved in transcriptional initiation. We have used oligonucleotide primers flanking a polymorphic stretch of 38 glutamine codons in the 5' coding region of the TBP gene to genetically map this gene. We report the location of the human TBP gene to be at 6qter.
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PMID:Mapping of the human TATA-binding protein gene (TBP) to chromosome 6qter. 769 28

Eukaryotic transcriptional activators may stimulate RNA polymerase II activity by promoting assembly of preinitiation complexes on promoters through their interactions with one or more components of the basal machinery. On the basis of its central role in initiating transcription-complex formation upon binding to the TATA box, the general transcription factor TFIID, which includes the TATA-binding protein (TBP) and several TBP-associated factors, has been implicated as a target for activators. Consistent with this idea, an increasing number of activators have been reported to bind directly to TBP. To assess the functional importance of these in vitro interactions for transcriptional regulation in vivo, we made use of a novel strategy in yeast to show that a physical interaction with TBP is sufficient for a sequence-specific DNA-binding protein to increase initiation of transcription by RNA polymerase II. These results imply that binding of TFIID to promoter elements is a limiting step in transcription complex assembly in vivo.
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PMID:Stimulation of RNA polymerase II transcription initiation by recruitment of TBP in vivo. 772 29

In mammalian and Drosophila cells, the central RNA polymerase II general transcription factor TFIID is a multisubunit complex containing the TATA-binding protein (TBP) and TBP-associated factors (TAFs) bound to the conserved TBP carboxy-terminal core domain. TBP also associates with alternative TAFs in these cells to form general transcription factors required for initiation by RNA polymerases I and III. Although extracts of human HeLa cells contain little TBP that is not associated with TAFs, free TBP is readily isolated from yeast cell extracts. However, recent studies indicate that yeast TBP can also interact with other yeast polypeptides to form multiprotein complexes. We established stable human HeLa cell lines expressing yeast TBP and several yeast-human TBP hybrids to study TBP-TAF interactions. We found that the yeast TBP core domain assembles with a complete set of human TAFs into a stable TFIID complex that can support activated transcription in vitro. The fact that the yeast TBP core, which differs from human TBP core in approximately 20% of its amino acid residues, has the structural features required to form a stable complex with human TAFs implies that Saccharomyces cerevisiae probably contains TAFs that are structurally and functionally analogous to human TAFs. Surprisingly, the non-conserved amino terminus of yeast TBP inhibited association between the yeast core domain and human TAFs.
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PMID:The yeast TATA-binding protein (TBP) core domain assembles with human TBP-associated factors into a functional TFIID complex. 779 63

TFIIA is a general transcription factor that modulates class II transcription initiation in vitro by functionally and physically interacting with TFIID or the derived TATA-binding protein (TBP). TFIIA was previously purified from human, bovine, rat, and yeast sources and has recently been identified in association with TFIID in Drosophila. Here, we report the cloning of a cDNA encoding the 12.5-kDa subunit of TFIIA from Drosophila melanogaster (dTFIIA-S) and the identification of a partial dTFIIA-S gene in Drosophila virilis. The deduced amino acid sequence of dTFIIA-S indicates a high degree of homology to the small TFIIA subunit from yeast and to a partial TFIIA-S cDNA identified in rice. A hybrid TFIIA consisting of recombinant dTFIIA-S and the recombinant human TFIIA/alpha gene product mimics natural TFIIA activity in a TBP-dependent DNA binding assay. The promoter complex formed with this hybrid TFIIA depends upon the TATA element and can be efficiently incorporated into a higher order preinitiation complex upon addition of TFIIB. The presence of dTFIIA-S within the TBP-TFIIA-promoter complex was demonstrated using anti-dTFIIA-S antiserum. Finally, the ability of recombinant dTFIIA-S to reconstitute transcriptionally active TFIIA was demonstrated in a well defined human transcription system.
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PMID:Characterization of the highly conserved TFIIA small subunit from Drosophila melanogaster. 792 95


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