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At least 253 records · Page 14Linked to original sources
PubMed1993

The human cytomegalovirus 86K immediate early (IE) 2 protein requires the basic region of the TATA-box binding protein (TBP) for binding, and interacts with TBP and transcription factor TFIIB via regions of IE2 required for transcriptional regulation.

The 86K immediate early (IE) 2 protein of human cytomegalovirus trans-activates a number of homologous and heterologous promoters, including the cellular promoter for the 70K heat-shock protein (hsp70), and the human immunodeficiency virus long terminal repeat. We have previously shown that IE2 trans-activates these two promoters in a TATA-dependent manner, and that IE2 is able to form a direct contact with TATA-box binding protein (TBP) in vitro. We now show that IE2 binds to the basic repeat region of TBP. In addition IE2 can contact a second general transcription factor, TFIIB. We have mapped the TBP- and TFIIB-binding regions within IE2 and show that these regions overlap, and also lie within parts of the protein previously identified as being required for the trans-activation and autoregulation functions of IE2.

Base Sequence↗
PubMed2002

Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo.

The multisubunit Saccharomyces cerevisiae SAGA (Spt-Ada-Gcn5-acetyltransferase) complex is required to activate transcription of a subset of RNA polymerase II-dependent genes. However, the contribution of each SAGA component to transcription activation is relatively unknown. Here, using a formaldehyde-based in vivo cross-linking and chromatin immunoprecipitation assay, we have systematically analyzed the role of SAGA components in the recruitment of TATA-box binding protein (TBP) to SAGA-dependent promoters. We show that recruitment of TBP is diminished at a number of SAGA-dependent promoters in ada1delta, spt7delta, and spt20delta null mutants, consistent with previous biochemical data suggesting that these components maintain the integrity of the SAGA complex. We also find that Spt3p is generally required for TBP binding to SAGA-dependent promoters, consistent with biochemical and genetic experiments, suggesting that Spt3p interacts with and recruits TBP to the core promoter. By contrast, Spt8p, which has been proposed to be required for the interaction between Spt3p and TBP, is required for TBP binding at only a subset of SAGA-dependent promoters. Ada2p and Ada3p are both required for TBP recruitment to Gcn5p-dependent promoters, supporting previous biochemical data that Ada2p and Ada3p are required for the histone acetyltransferase activity of Gcn5p. Finally, our results suggest that TBP-associated-factor components of SAGA are differentially required for TBP binding to SAGA-dependent promoters. In summary, we show that SAGA-dependent promoters require different combinations of SAGA components for TBP recruitment, revealing a complex combinatorial network for transcription activation in vivo.

Acetyltransferases↗
PubMed1991

Functional significance of sequences following the TATA box of an immunoglobulin promoter studied by random mutagenesis.

We have investigated the importance of sequences downstream to the TATA box of an immunoglobulin promoter by transfection and in vitro transcription assays. A sequence from -11 to +10 with respect to the transcriptional start site was synthesised by a procedure allowing for random misincorporation of nucleotides. The pool of mutant oligonucleotides was cloned into the respective position of a vector carrying a fusion of a synthetic immunoglobulin heavy chain promoter with the human growth hormone gene. From 200 clones sequenced, 115 were mutants with at least one nucleotide exchange in every position. Whereas most mutations are of minor functional importance, changes at or near the transcriptional start site reduce the promoter activity considerably.

Base Sequence↗
PubMed1996

Genomic structure of the maize TATA-box binding protein 1 (TBP-1): conserved exon/intron structure in eukaryotic TBP genes.

The gene system of the TATA-box binding protein (TBP) is well suited for the study of the evolutionary conservation of essential components of eukaryotic transcription initiation. In this context we have isolated and sequenced the maize TBP gene for a comparison with TBP genes from other organisms. In particular, a molecular phylogenetic analysis of the exon/intron structure of these genes including the archaeal TBP homolog (Thermococcus celer) was performed, revealing that the intron insertion probably occurred after the early appearance of the characteristic tandem repeat within the highly conserved C-terminal domain of all known TBPs, but before separation of the eukaryotic progenitor into the different kingdoms.

ATPases Associated with Diverse Cellular Activitie↗
PubMed1991

Induction of dormant HIV-1 by sodium butyrate: involvement of the TATA box in the activation of the HIV-1 promoter.

Reactivation of latent HIV-1 is believed to play a major role in the pathogenesis of AIDS. Here we show that sodium butyrate (NaB), which can cause gene induction or cell differentiation, reactivates dormant HIV-1 in vitro in chronically infected cells of T-lymphoid and monocytoid origin. The effect of NaB on HIV-1 expression in T-lymphoid cells was apparent 3 h after addition of drug and peaked at 24 h. During this time the proportion of HIV-1 antigen expressing cells increased from less than 0.5 to greater than 90%, and virus production increased by three orders of magnitude. The virus released by the NaB-induced cells was infectious. The extent and kinetics of NaB effects were similar to effects of phorbol 12-myristate 13-acetate in T cells, but not monocytes. Transient expression assays using an indicator gene under the control of the HIV-1 long terminal repeat revealed that mutations which altered the nucleotide sequence in the TATA box significantly reduced the NaB effect. These data show that NaB is a potent inducer of dormant HIV-1 and suggest that the TATA motif is required for this activity.

Butyrates↗
PubMed2008

Beta-thalassemia intermedia due to compound heterozygosity for two beta-globin gene promoter mutations, including a novel TATA box deletion.

An 8-year-old African-American boy had a clinical history consistent with mild beta-thalassemia intermedia with moderate anemia, microcytosis, reticulocytosis, and splenomegaly. He was asymptomatic and did not require transfusion. At age 4 years, hemoglobin (Hb) electrophoresis showed Hb A = 37.8%, Hb A(2) = 5.0%, and Hb F = 56.1%. At age 8 years, he was diagnosed to be a compound heterozygote for two beta-globin gene promoter mutations, the relatively common nucleotide (nt) -88 C --> T mutation from the cap site, and a novel two-nucleotide (AA) deletion between nt -29 and -26 within the TATA box of the beta-globin gene. His mother and 14-year-old brother were simple heterozygotes for this novel (AA) deletion. Both heterozygotes had normal Hb level, borderline microcytosis, and elevated Hb A(2).

Child↗
PubMed2003

The critical cis-acting element required for IMD2 feedback regulation by GDP is a TATA box located 202 nucleotides upstream of the transcription start site.

Guanylic nucleotides are essential cellular players, and the critical enzyme in their tightly regulated synthesis in Saccharomyces cerevisiae is encoded by the IMD2 gene. The transcription of IMD2 is subject to general repression by nutrient limitation through the cis nutrient-sensing element. It is also subject to specific feedback regulation by the end products of the guanylic nucleotide synthesis pathway. The critical cis element for this latter mechanism is the guanine response element (GRE), a TATAATA sequence which is located 202 nucleotides upstream of the transcription initiation site and which functions as the IMD2 TATA box. We show that the GRE functions in conjunction with a 52-nucleotide stretch near the transcription start site. This very unusual promoter structure ensures low, basal expression of IMD2 and the recruitment of TFIID to the GRE in response to guanylic nucleotide limitation.

Base Sequence↗
PubMed2001

Identification of a single nucleotide polymorphism in the TATA box of the CYP2A6 gene: impairment of its promoter activity.

Human cytochrome P450 2A6 (CYP2A6) constitutes the major nicotine oxidase, and large interindividual differences are seen in the levels of this enzyme, to a great extent caused by the distribution of several different polymorphic gene variants mainly located in the open reading frame (ORF). In the present study, we report a common polymorphism located in the 5' flanking region of CYP2A6 affecting its expression. DHPLC analysis and complete sequence of the open reading frame of the gene from a Turkish individual revealed a -48T > G substitution disrupting the TATA box. Using dynamic allele-specific hybridization (DASH), genotyping of this novel variant (named CYP2A6*9) was carried out in 116 Swedish, 132 Turkish, and 102 Chinese subjects, and the allele frequencies were found to be 5.2, 7.2, and 15.7%, respectively. The significance of the polymorphism was investigated by the construction of luciferase reporter plasmids containing 135 or 500 bp of the 5'-upstream region of the gene transfected into human hepatoma B16A2 cells. The constructs carrying the -48T > G mutation were only expressed at about 50% of the wild-type alleles. It is concluded that the CYP2A6*9 allele might be one of the most common CYP2A6 variants in Caucasians that alters the levels of enzyme expression.

Alleles↗
PubMed2001

Extremely reduced evolutionary rate of TATA-box binding protein in higher vertebrates and its evolutionary implications.

Previously we showed that the evolutionary rates of the Pax proteins are markedly reduced in higher vertebrates, as compared with those in the ancestral lineage of vertebrates, and we suggested that the reduced Pax protein evolution might be explained by increased functional constraints due to gene recruitment for other purposes or repeated expression in different developmental stages. To clarify the problem of whether the evolutionary rate variation found in the Pax proteins is an evolutionary feature generally recognized in most transcription factors, we have cloned and sequenced cDNAs encoding the TATA-box binding protein (TBP), a general transcription factor of eukaryotes, from Oryzias latipes, a Japanese medaka, Lampetra reissneri, a lamprey, and Ephydatia fluviatilis, a freshwater sponge. An evolutionary rate analysis of TBP has revealed that the evolutionary rate of TBP is extremely low in higher vertebrates, but not in the ancestral lineage of vertebrates, as found in the Pax proteins. In contrast, no marked reduction of the evolutionary rate in higher vertebrates is observed in the aldolase C, a house keeping enzyme. It is therefore likely that the increased functional constraint on TBP is responsible for the extremely low evolutionary rate in higher vertebrates. The temporal pattern of the evolutionary rate variation during vertebrate evolution was discussed.

Animals↗
PubMed2005

On the TATA box and transcriptional start site of gE gene of pseudorabies virus: a comparison of three methods.

Using the upstream region of glycoprotein E gene of pseudorabies virus (PRV) as a model, a method based on reverse transcriptase-polymerase chain reaction (RT-PCR) for the determination of transcriptional start site was developed. The conventional primer extension method was used to determine the start site. Comparing the results obtained by these two methods, a good agreement on the location of start site was achieved. In addition, a computer program was used to predict the transcriptional start site, and the predicted site was found to be close to the two sites obtained by experiments. Based on the transcriptional start site data and on the general knowledge of the eukaryotic gene, the TATA box of gE gene was assigned at approximately 33 bp upstream to the start site.

Animals↗
PubMed1996

HPV-16 E7 and adenovirus E1a complex formation with TATA box binding protein is enhanced by casein kinase II phosphorylation.

The major transforming protein of HPV-16 is encoded by the E7 gene. This has been shown to cooperate with EJ-ras in the immortalisation of primary rodent cells and with the viral E6 gene in the immortalisation of primary human keratinocytes. HPV-16 E7 protein has been shown to bind to a number of cellular proteins involved in the control of cell growth; including pRB, p107 and cyclin A. Loss of pRb or p107 binding results in the loss of transforming activity. In this paper we demonstrate that HPV-16 E7 can also complex with the core component of TFIID, the TATA Box Binding Protein (TBP). This interaction is partly dependent upon phosphorylation of the E7 protein by cellular casein kinase II (CKII), since phosphorylation of E7 by CKII increases the affinity with which E7 binds TBP. Similar results are also obtained with the Adenovirus Ela protein, indicating a conservation of function between these two viral oncoproteins. Mutation of the CKII site to two acidic amino acids significantly increases the affinity of E7 for TBP, indicating that the incorporation of two negative charges at this region of E7 is important in regulating the interaction with TBP.

Adenovirus E1A Proteins↗
PubMed1994

A novel carbonic anhydrase II mRNA isolated from mature chicken testis displays a TATA box and other promoter sequences in a leader 5' untranslated region not present in somatic tissues.

The primary structure of a novel carbonic anhydrase II-encoding cDNA clone (CAII) isolated from a chicken testis cDNA library is presented. The size of the CAII mRNA obtained from meiotic and haploid chicken testis cells is larger than the corresponding mRNA from immature testis and somatic tissues. The nucleotide sequence of the chicken testis CAII clone revealed a protein-coding region identical to the published sequence of CAII mRNA from erythroid cells. However, the 5' untranslated region (UTR) of the testis CAII mRNA is larger than the corresponding somatic sequence. The 5' UTR contains a leader sequence not present in the CAII mRNA isolated from erythroid cells or chick retina. The additional 5' UTR of the mRNA displays a TATA box, located 23-30 bp upstream from the cap site of the CAII mRNA transcribed in erythroid cells, and several G+C-rich boxes. Our results suggest that the use of a testis-specific promoter would result in the incorporation of somatic promoter sequences into the 5' UTR of the testis message.

Amino Acid Sequence↗
PubMed1998

Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein.

beta-catenin, the vertebrate homolog of the Drosophila Armadillo protein, has been shown to have dual cellular functions, as a component of both the cadherin-catenin cell adhesion complex and the Wnt signaling pathway. At Wnt signaling, beta-catenin becomes stabilized in the cytoplasm and subsequently available for interaction with transcription factors of the lymphocyte enhancer factor-1/T-cell factor family, resulting in a nuclear localization of beta-catenin. Although beta-catenin does not bind DNA directly, its carboxyl- and amino-terminal regions exhibit a transactivating activity still not well understood molecularly. Here we report the identification of an interaction partner of beta-catenin, a nuclear protein designated Pontin52. Pontin52 binds beta-catenin in the region of Armadillo repeats 2-5 and, more importantly, also binds the TATA box binding protein. We provide evidence for an in vivo multiprotein complex composed of Pontin52, beta-catenin, and lymphocyte enhancer factor-1/T-cell factor. Our results suggest involvement of Pontin52 in the nuclear function of beta-catenin.

Amino Acid Sequence↗
PubMed2004

TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain.

A number of transcription factor proteins contain domains that are fully or partially unstructured. The means by which such proteins acquire naturally folded conformations are not well understood. When they encounter their proper binding partner(s), several of these proteins adopt a folded conformation through an induced-fit mechanism. The glucocorticoid receptor (GR) is a ligand-activated transcription factor. Expressed independently as a recombinant peptide, the N-terminal transactivation domain (AF1) of the GR shows little structure and appears to exist as a collection of random coil configurations. The GR AF1 is known to interact with other transcription factors, including a critical component of the general transcription machinery proteins, the TATA box binding protein (TBP). We tested whether this interaction can lead to acquisition of structure in the GR AF1. Our results show that recombinant GR AF1 acquires a significant amount of helical content when it interacts with TBP. These structural changes were monitored by Fourier transform infrared and NMR spectroscopies, and by proteolytic digestions. Our results support a model in which TBP binding interaction with the GR AF1 induces significantly greater helical structure in the AF1 domain. This increased helical content in the GR AF1 appears to come mostly at the expense of random coil conformation. These results are in accordance with the hypothesis that an induced-fit mechanism gives structure to the GR AF1 when it encounters TBP.

Circular Dichroism↗
PubMed1992

Cell-specific transcription of the peripherin gene in neuronal cell lines involves a cis-acting element surrounding the TATA box.

Peripherin is a neurone-specific intermediate filament protein expressed mostly in the peripheral nervous system. To localize sequences that are important for the regulation of peripherin gene transcription, we have functionally dissected its promoter. Transfection into different cell lines and deletion mapping of peripherin-lacZ hybrid constructs indicated that the first 98 bp preceding the transcription start site of the gene were sufficient to confer cell-type specific expression. DNase I footprinting experiments revealed three protected sequences in this region, that were named PER1, PER2 and PER3. The PER2 and PER3 elements, localized between -98 to -46, interact with proteins that seem widely distributed. Deletion of these elements severely decreased the level of reporter gene activity. The PER1 element, which overlaps the TATA box, interacts with a DNA-binding protein prevailing in peripherin expressing cell lines. However, the core promoter, which contains the PER1 element, was inefficient in driving gene expression. Experiments designed to test the contribution of each element showed that PER2 and PER3 were important in determining the level of expression, while PER1 was important for cell-type specificity. In fact the polyoma virus enhancer linked to the peripherin gene core promoter was found to limit reporter gene activity to peripherin expressing cell lines. Together, these experiments indicate that co-operative interactions between different regions of the promoter are necessary for efficient and cell-type specific transcription of the peripherin gene in a subset of neuronal cells.

Animals↗
PubMed1994

A point mutation in the putative TATA box, detected in nondiseased individuals and patients with hereditary breast cancer, decreases promoter activity of the 17 beta-hydroxysteroid dehydrogenase type 1 gene 2 (EDH17B2) in vitro.

EDH17B2, the gene encoding 17 beta-hydroxysteroid dehydrogenase type 1, has been suggested as a candidate for the familial breast cancer gene, BRCA1, located on 17q12-q21. We analyzed the promoter region of EDH17B2 in DNA from 20 control individuals and 40 patients with familial breast cancer. Two frequent (designated vI and vIII) and two rare (vII and vIV) nucleotide variations were present in both the breast cancer patients and the controls, except the alteration vII, which was found only in one patient. Although the data do not support the identification of EDH17B2 as the BRCA1 gene, it is of interest that point mutation vIV (A-->C) was located in the putative TATA box of the EDH17B2 gene. Reporter gene analyses showed that the mutation vIV decreases EDH17B2 promoter activity by an average of 45% in in vitro assays, suggesting that nucleotide A at position -27 is significant for efficient transcription.

17-Hydroxysteroid Dehydrogenases↗
PubMed1996

The actions of 2,3,7,8-tetrachlorodibenzo-p-dioxin on transforming growth factor-beta2 promoter activity are localized to the TATA box binding region and controlled through a tyrosine kinase-dependent pathway.

2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD), a widespread environmental contaminant and suspected human carcinogen, is believed to act by altering expression of a number of genes involved in cell growth control. In a previous study, we demonstrated the transcriptional down regulation of transforming growth factor-beta2 (TGF-beta2) by TCDD. To identify the region of the TGF-beta2 promoter necessary for the observed down-regulation by TCDD, we studied the effect of TCDD on a series of TGF-beta2 gene promoter deletions ranging from 1391 to 64 base pairs upstream of the transcription start site. We demonstrate that the effect of TCDD on TGF-beta2 promoter activity is localized to the TATA box sequence. The effect of TCDD on TGF-beta2 transcription is dose-dependent, exhibiting saturation kinetics maximal by 10 nM. Time course experiments show that the maximum decrease (30-50%) in promoter activity by a 10 nM dose of TCDD is complete by 24 hr. DNAase I footprinting and gel shift experiments indicate a single shifted protein complex in this region that we conclude is the transcription initiation complex. TCDD does not appear to significantly alter this complex suggesting that gross alterations in the proteins associated with this sequence do not occur. Treatment of the cells with various protein kinase inhibitors had no significant effect on the TCDD-induced decrease in promoter activity with the exception of genistein, a tyrosine kinase inhibitor. Genistein reverses the effect of TCDD on TGF-beta2 promoter activity back to control levels. Thus, TCDD can modulate gene transcription by acting at the transcription initiation complex via a tyrosine kinase-dependent pathway.

2-Aminopurine↗
PubMed2005

Cooperation between small nuclear RNA-activating protein complex (SNAPC) and TATA-box-binding protein antagonizes protein kinase CK2 inhibition of DNA binding by SNAPC.

Protein kinase CK2 regulates RNA polymerase III transcription of human U6 small nuclear RNA (snRNA) genes both negatively and positively depending upon whether the general transcription machinery or RNA polymerase III is preferentially phosphorylated. Human U1 snRNA genes share similar promoter architectures as that of U6 genes but are transcribed by RNA polymerase II. Herein, we report that CK2 inhibits U1 snRNA gene transcription by RNA polymerase II. Decreased levels of endogenous CK2 correlates with increased U1 expression, whereas CK2 associates with U1 gene promoters, indicating that it plays a direct role in U1 gene regulation. CK2 phosphorylates the general transcription factor small nuclear RNA-activating protein complex (SNAP(C)) that is required for both RNA polymerase II and III transcription, and SNAP(C) phosphorylation inhibits binding to snRNA gene promoters. However, restricted promoter access by phosphorylated SNAP(C) can be overcome by cooperative interactions with TATA-box-binding protein at a U6 promoter but not at a U1 promoter. Thus, CK2 may have the capacity to differentially regulate U1 and U6 transcription even though SNAP(C) is universally utilized for human snRNA gene transcription.

Binding Sites↗