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

Human transcription factor TFIID, the TATA-binding protein, was partially purified to a form capable of associating stably with the TATA motif of the adenovirus major late promoter. Binding of the human and yeast TFIID to the TATA motif was stimulated by TFIIA. TFIIA is an integral part of a complex capable of binding other transcription factors. A complex formed with human TFIID and TFIIA (DA complex) was specifically recognized by TFIIB. We found that TFIIB activity was contained in a single polypeptide of 32 kDa and that this polypeptide participated in transcription and was capable of binding to the DA complex to form the DAB complex. Formation of the DAB complex required TFIIA, TFIID, and sequences downstream of the transcriptional start site; however, the DA complex could be formed on an oligonucleotide containing only the adenovirus major late promoter TATA motif. Using anti-TFIIB antibodies and reagents that affect the stability of a transcription-competent complex, we found that yeast and human TFIID yielded DAB complexes with different stabilities.
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PMID:Factors involved in specific transcription by mammalian RNA polymerase II: role of transcription factors IIA, IID, and IIB during formation of a transcription-competent complex. 224 58

TFIID, the TATA-binding protein, was found to stimulate transcription from the adenovirus IVa2 promoter, a promoter considered to lack the TATA motif. Remarkably, a TATA-like sequence element located downstream of the transcription start site binds TFIID and is required for TFIID-dependent transcription from the IVa2 promoter. Transcription from the IVa2 and the adjacent adenovirus major late promoter (Ad-MLP) is divergent, and the cap sites are separated by 212 nucleotides. Nevertheless, the TATA motifs of the IVa2 promoter and Ad-MLP were found to be oriented in the same direction. An initiator motif around the transcription start site is located in the IVa2 promoter, and in contrast to the TATA motifs, the IVa2-initiator is in the opposite orientation with respect to the initiator of the Ad-MLP. A model is presented in which the polar nature of the initiator governs the direction of transcription. We propose that RNA polymerase II and accessory factors recognize the initiator in an orientation-dependent fashion. The recognition of the IVa2 initiator by RNA polymerase is enhanced by the binding of TFIID to the downstream TATA motif.
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PMID:A TATA-like sequence located downstream of the transcription initiation site is required for expression of an RNA polymerase II transcribed gene. 225 81

The first step in the transcription of most protein-encoding genes in eukaryotes is the binding of a transcription factor to the TATA-box promoter element. This TATA-box transcription factor was purified from extracts of the yeast Saccharomyces cerevisiae by using reconstitution of in vitro transcription reactions as an assay. The activity copurified with a protein whose sodium dodecyl sulfate/polyacrylamide gel mobility is 25 kDa. The sequence of the amino-terminal 21 residues of this protein was determined by sequential Edman degradation. A yeast genomic library was screened with mixed oligonucleotides encoding six residues of the protein sequence. The yeast TATA-box factor gene was cloned, and DNA sequencing revealed a 720-base-pair open reading frame encoding a 27,016-Da protein. The identity of the clone was confirmed by expressing the gene in Escherichia coli and detecting TATA-box factor DNA binding and transcriptional activities in extracts of the recombinant E. coli. The TATA-box factor gene was mapped to chromosome five of S. cerevisiae. RNA blot hybridization and nuclease S1 analysis indicated that the major TATA-box factor mRNA is 1.3 kilobases, including an unusually long 5' untranslated region of 188 +/- 5 nucleotides. Homology searches showed a region of distant similarity to the calcium-binding structures of calpains, a structure that has a conformation similar to the helix-turn-helix motif of DNA binding proteins.
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PMID:Yeast TATA-box transcription factor gene. 268 26

Although the yeast his3 promoter region contains two functional TATA elements, TR and TC, the GCN4 and GAL4 upstream activator proteins stimulate transcription only through TR. In combination with GAL4, an oligonucleotide containing the sequence TATAAA is fully sufficient for TR function, whereas almost all single-base-pair substitutions of this sequence abolish the ability of this element to activate transcription. Further analysis of these and other mutations of the TR element led to the following conclusions. First, sequences downstream of the TATAAA sequence are important for TR function. Second, a double mutant, TATTTA, can serve as a TR element even though the corresponding single mutation, TATTAA, is unable to do so. Third, three mutations have the novel property of being able to activate transcription in combination with GCN4 but not with GAL4; this finding suggests that activation by GCN4 and by GAL4 may not occur by identical mechanisms. From these observations, we address the question of whether there is a single TATA-binding factor required for the transcription of all genes.
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PMID:Functional distinctions between yeast TATA elements. 268 58

Within the human T-cell leukemia virus type I promoter, there are three copies of a 21-base-pair repeat (hereafter called the tax-responsive element [TRE]) that both contributes to basal promoter activity and mediates induction by the viral activator TAX. We have identified and separated three nuclear proteins that interact with the TRE. The TRE-binding protein designated TREB-3 bound more avidly to a multimerized TRE than to a single-copy TRE, while the other two TRE-binding proteins, TREB-1 and TREB-2, bound equally well to either TRE. TREB-1 has been purified to near homogeneity, and binding activity was localized to a protein of 35 to 43 kilodaltons. The affinity-purified TREB-1 activated transcription from the human T-cell leukemia virus type I promoter in vitro. The purified TREB-1 fraction contained activating transcription factor binding activity and showed a cooperative interaction with the TATA-binding factor (TFIID) on the adenovirus E4 promoter.
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PMID:Purification and characterization of multiple nuclear factors that bind to the TAX-inducible enhancer within the human T-cell leukemia virus type 1 long terminal repeat. 278 41

Hormone activation of MMTV transcription results in the establishment of a tightly bound transcription factor complex at the promoter (Cordingley et al., Cell 48, 261-270, 1987). We have characterized two fractionable binding activities which participate in this complex. One factor, previously identified as the mouse homologue of NF-1 (or CTF), protects sequences -82 to -56 from exonuclease III digestion in vitro. Sequences protected by a second factor (-42 to -4) span the TATA box of the promoter, suggesting that the binding activity in this fraction is equivalent to the HeLa cell transcription factor TFIID (Sawadogo and Roeder, Cell 43, 165-175, 1986). The downstream boundary of exonuclease protection by the putative TATA-binding factor is -4; DNase1 footprinting of this fraction, however, showed additional protection of discrete sites downstream of the cap site. The apparent concentration and promoter-specific binding activity of both factors is unaffected by hormone treatment of the cells.
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PMID:Binding of multiple factors to the MMTV promoter in crude and fractionated nuclear extracts. 282 33

GAL4 is a transcriptional activator found in yeast. Two distinct functions of the protein are required for its activity: one directs sequence-specific DNA binding, and another interacts with some other component of the transcriptional machinery, for example, RNA polymerase II or a TATA-binding protein. Two short regions of GAL4 function as 'activating sequences' when attached to the DNA-binding portion of GAL4 and these regions can be replaced by a large number of peptides encoded by Escherichia coli genomic DNA fragments or by a synthetic peptide designed to form an amphiphilic alpha-helix. All of these activating sequences, like that found in another yeast activator, GCN4 bear an excess negative charge. GAL4 and its derivatives that are active in yeast stimulate transcription in mammalian cells when GAL4 binding sites are introduced upstream of a mammalian gene; similarly, GAL4 activates transcription in Drosophila cells. Here we show that GAL4 derivatives stimulate gene expression in plant cells.
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PMID:Yeast activators stimulate plant gene expression. 316 94

We have converted the TACAAA sequence present at position -29 of the adenovirus EIIa late promoter into a canonical TATA box by oligonucleotide-directed mutagenesis. When linear templates were analyzed in nuclear extracts, transcription of the mutant promoter showed a 10-fold higher level of activity than that of the wild-type promoter. This increase was correlated with an increased affinity of the mutant promoter for transcription initiation factor IID. Further analyses demonstrated that the activating functions of three EIIa late upstream promoter elements (Huang, D.-H., and Roeder, R.G. (1988) Mol. Cell. Biol. 8, 1906-1914) were maintained in the mutant promoter background. These observations indicated, first, that the upstream elements did not act merely to overcome a rate-limiting initiation step imposed by an inefficient TATA element and, second, that the strength of the interaction between transcription initiation factor IID and the TATA box was directly related to promoter activity.
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PMID:Activation of the adenovirus EIIa late promoter by a single-point mutation which enhances binding of transcription factor IID. 341 Aug 53

The yeast transcriptional activator GAL4 binds specific sites on DNA to activate transcription of adjacent genes. The distinct activating regions of GAL4 are rich in acidic residues and it has been suggested that these regions interact with another protein component of the transcriptional machinery (such as the TATA-binding protein or RNA polymerase II) while the DNA-binding region serves to position the activating region near the gene. Here we show that various GAL4 derivatives, when expressed at high levels in yeast, inhibit transcription of certain genes lacking GAL4 binding sites, that more efficient activators inhibit more strongly and that inhibition does not depend on the DNA-binding domain. We suggest that this inhibition, which we call squelching, reflects titration of a transcription factor by the activating region of GAL4.
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PMID:Negative effect of the transcriptional activator GAL4. 341 49

We have presented evidence that apoproteins may exchange, in vitro, between all HDL subclasses tested, including HDL2b, HDL2a, HDL3, and HDL4. This exchange process is influenced by various factors including the concentrations of the subclasses and the presence of added apoprotein. This exchange process should be considered when designing experiments using HDL subclasses in vitro, and the importance of exchange in the in vivo situation should be a subject of further investigation.
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PMID:Factors affecting the exchange of apoproteins between human high density lipoprotein subclasses in vitro. 686 Mar 23


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