Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

cAMP response element-binding protein (CREB) participates in both constitutive and cAMP-induced transcription of cAMP-responsive genes. CREB-mediated constitutive transcription requires only CREB-binding sites and a minimal promoter region (containing the TATA through start sequences), indicating that CREB interacts directly with components of the general transcription machinery. In this study, a coimmunoprecipitation assay was used to test for interaction of CREB with the general transcription factors (TF) TFIIB and TFIID and the core component of TFIID, TATA-binding protein (TBP). Human TFIIB and TBP, tagged with distinct epitopes (eTFIIB and eTBP), were expressed in and purified from Escherichia coli, and holo-eTFIID, containing eTBP, was obtained from the HeLa cell line LTR alpha 3. 35S-Labeled CREB, synthesized in vitro and incubated with eTFIIB, was coimmunoprecipitated with antibody recognizing eTFIIB, indicating that CREB specifically binds to TFIIB. 35S-CREB was coimmunoprecipitated with antibody against eTBP, but only when incubated with the holo-eTFIID complex, not with eTBP alone. TFIIB interacted with TBP, but CREB was not coprecipitated with the eTBP antibody when incubated with eTBP plus TFIIB, so CREB did not form a stable ternary complex with TFIIB and TBP. Conversely, depletion of TFIIB from the holo-TFIID preparation did not diminish the level of interaction between CREB and TFIID. Thus, CREB interacts independently with TFIIB and TFIID, but not directly with TBP. A protein kinase A phosphorylation site mutant of CREB and wild-type CREB exhibited equivalent interaction with TFIIB, indicating that this phosphorylation is not required. Consistent with the role of CREB in promoting constitutive or basal transcription, the constitutive activation domain of CREB was sufficient for interaction with both TFIIB and TFIID.
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PMID:cAMP response element-binding protein (CREB) interacts with transcription factors IIB and IID. 761 53

We characterized three Arabidopsis thaliana cDNA clones that could rescue the sterile phenotype of the Schizosaccharomyces pombe pde1 mutant, which is defective in cAMP phosphodiesterase. The first clone had a coding capacity of 399 amino acids that is 35% identical with rat protein phosphatase 2C (PP2C). The second had a coding capacity of 159 amino acids that is 41% identical with human Dr1. Dr1 has been shown to interact with TATA-binding protein (TBP) and block its ability to activate transcription. The third encoded Arabidopsis TBP itself. Saccharomyces cerevisiae TBP also could suppress the sterile phenotype if expressed in S.pombe pde1 cells, but overexpression of S.pombe TBP could do so very poorly. These observations suggest preliminarily that PP2C may counteract cAMP-dependent protein kinase in fission yeast cells, and that the heterologous TBPs and Dr1 may interfere with the general transcription factors of S.pombe so that the gene expression in the host cell becomes affirmative of sexual development. Furthermore, the identification of a Dr1-like protein in A.thaliana strongly argues for the ubiquity of this protein among eukaryotic genera and for a conserved mechanism to regulate transcription initiation that involves Dr1.
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PMID:Cloning of cDNAs from Arabidopsis thaliana that encode putative protein phosphatase 2C and a human Dr1-like protein by transformation of a fission yeast mutant. 781 19

The SNF1 protein kinase of Saccharomyces cerevisiae is required to relieve glucose repression of transcription. To identify components of the SNF1 pathway, we isolated multicopy suppressors of defects caused by loss of SNF4, an activator of the SNF1 kinase. Increased dosage of the MSN3 gene restored invertase expression in snf4 mutants and also relieved glucose repression in the wild type. Deletion of MSN3 caused no substantial phenotype, and we identified a homolog, MTH1, encoding a protein 61% identical to MSN3. Both are also homologous to chicken fimbrin, human plastin, and yeast SAC6 over a 43-residue region. Deletion of MSN3 and MTH1 together impaired derepression of invertase in response to glucose limitation. Finally, MSN3 physically interacts with the SNF1 protein kinase, as assayed by a two-hybrid system and by in vitro binding studies. MSN3 is the same gene as STD1, a multicopy suppressor of defects caused by overexpression of the C terminus of TATA-binding protein (R. W. Ganster, W. Shen, and M. C. Schmidt, Mol. Cell. Biol. 13:3650-3659, 1993). Taken together, these data suggest that MSN3 modulates the regulatory response to glucose and may couple the SNF1 pathway to transcription.
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PMID:Dosage-dependent modulation of glucose repression by MSN3 (STD1) in Saccharomyces cerevisiae. 811 28

Nuclear transcription is repressed when eukaryotic cells enter mitosis. Using Xenopus egg extracts shifted to the mitotic state with recombinant cyclin B1 protein, we have been able to reproduce mitotic repression of transcription in vitro. Active RNA polymerase III transcription is observed in interphase extracts in the absence of added cyclin, but is strongly repressed by the induction of cdc2/cyclin B (maturation/mitosis promoting factor, MPF) kinase activity in the mitotic extract. Studies with protein kinase inhibitors show that protein phosphorylation is required for repression. Add-back experiments indicate that repression of class III gene transcription is due to inactivation of the transcription factor TFIIIB. TFIIIB is composed of the TATA-box binding protein (TBP) and TBP-associated factors of 75 and 92 kDa. In the present study, we show that TBP and a polypeptide of 92 kDa are substrates of the mitotic kinase in highly purified TF- IIIB fractions. We also show that a phosphatase present in the Xenopus egg extract can reactivate transcription after repression by the mitotic kinases. This result suggests a mechanism for reactivation of transcription after exit from mitosis into the G1 phase of the cell cycle. As for pol III genes, purified cdc2/cyclin B kinase is sufficient to inhibit transcription by RNA polymerase II in a reconstituted transcription system containing the basal transcription factors and polymerase.
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PMID:Repression of RNA polymerase II and III transcription during M phase of the cell cycle. 898 11

The highly conserved protein kinase casein kinase II (CKII) is required for efficient Pol III transcription of the tRNA and 5S rRNA genes in Saccharomyces cerevisiae. Using purified factors from wild-type cells to complement transcription extracts from a conditional lethal mutant of CKII we show that TFIIIB is the CKII-responsive component of the Pol III transcription machinery. Dephosphorylation of TFIIIB eliminated its ability to complement CKII-depleted extract, and a single TFIIIB subunit, the TATA-binding protein (TBP), is a preferred substrate of CKII in vitro. Recombinant TBP purified from Escherichia coli is phosphorylated efficiently by CKII and, in the presence of a limiting amount of CKII, is able to substantially rescue transcription in CKII-deficient extract. Our results establish that TBP is a key component of the pathway linking CKII activity and Pol III transcription and suggest that TBP is the target of a CKII-mediated regulatory mechanism that can modulate Pol III transcription.
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PMID:Casein kinase II regulation of yeast TFIIIB is mediated by the TATA-binding protein. 935 48

Our previous studies have shown that the hepatitis B virus protein, X, activates all three classes of RNA polymerase III (pol III)-dependent promoters by increasing the cellular level of TATA-binding protein (TBP) (H.-D. Wang et al., Mol. Cell. Biol. 15:6720-6728, 1995), a limiting transcription component (A. Trivedi et al., Mol. Cell. Biol. 16:6909-6916, 1996). We have investigated whether these X-mediated events are dependent on the activation of the Ras/Raf-1 signaling pathway. Transient expression of a dominant-negative mutant Ras gene (Ras-ala15) in a Drosophila S-2 stable cell line expressing X (X-S2), or incubation of the cells with a Ras farnesylation inhibitor, specifically blocked both the X-dependent activation of a cotransfected tRNA gene and the increase in cellular TBP levels. Transient expression of a constitutively activated form of Ras (Ras-val12) in control S2 cells produced both an increase in tRNA gene transcription and an increase in cellular TBP levels. These events are not cell type specific since X-mediated gene induction was also shown to be dependent on Ras activation in a stable rat 1A cell line expressing X. Furthermore, increases in RNA pol III-dependent gene activity and TBP levels could be restored in X-S2 cells expressing Ras-ala15 by coexpressing a constitutively activated form of Raf-1. These events are serum dependent, and when the cells are serum deprived, the X-mediated effects are augmented. Together, these results demonstrate that the X-mediated induction of RNA pol III-dependent genes and increase in TBP are both dependent on the activation of the Ras/Raf-1 signaling cascade. In addition, these studies define two new and important consequences mediated by the activation of the Ras signal transduction pathway: an increase in the central transcription factor, TBP, and the induction of RNA pol III-dependent gene activity.
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PMID:Hepatitis B virus X protein induces RNA polymerase III-dependent gene transcription and increases cellular TATA-binding protein by activating the Ras signaling pathway. 937 15

To achieve a better understanding of the mechanism of intimal thickening, we used a rabbit model in which aorta was denuded mechanically by a balloon catheter. Total RNA was prepared from each aorta 1, 2, 7, 14, 23, or 30 days after denudation, and from intact aorta of non-denuded control rabbits. Subsequently, using the differential display method, we identified eight genes that were expressed differently during the time course after injury. One of them, RESP18 (encoding regulated endocrine secretory protein 18), was suppressed during the acute reaction. The other seven showed increase in expression during the acute phase: the genes for hTAFII68 (human TATA-binding protein associated factor), NPAT (nuclear protein mapped to the AT locus), OSF2 (osteoblast-specific factor 2), Pyst1, casein kinase 1 alpha, integrin alpha 1, and XP-C complementing protein. Although hTAFII68, NPAT, OSF2, and Pyst1 are thought to be related to transcription, not all four are positive regulators. Considering that none of these genes had previously been reported as being implicated in intimal hyperplasia, we conclude that many known or unknown genes play roles in this process. We believe that differential display is an effective method for screening genes whose variations in expression can provide clues toward understanding the molecular mechanism of intimal hyperplasia.
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PMID:Identification by differential display of eight known genes induced during in vivo intimal hyperplasia. 960 92

Phorbol ester treatment of U937 leukemic cells results in the activation of numerous protein kinase pathways, followed by cell cycle arrest and differentiation into macrophage-like cells. Because major changes in gene transcription are associated with this process, the role of general transcription factors in the cell response to phorbol esters was examined. Experiments demonstrate that phorbol ester treatment of U937 cells stimulates the phosphorylation of the TATA-binding protein (TBP); this phosphorylation occurs within 30 min and is still apparent, although greatly reduced, at 4 h. The following results demonstrate that TBP phosphorylation occurs as a result of activation of an extracellular signal-regulated kinase (ERK) protein kinase: (a) overexpression of mitogen-activated protein kinase phosphatase-1 blocks phorbol 12-myristate 13-acetate (PMA)-induced phosphorylation of TBP both in vitro and in vivo; (b) pretreatment with the ERK kinase kinase inhibitor PD098059 also blocks PMA-induced phosphorylation of TBP both in vitro and in vivo; and (c) phosphorylation of TBP is observed when serum-starved NIH 3T3 cells are stimulated with fresh serum, another activator of the ERK pathway. TBP can be phosphorylated in vitro by extracts of U937 cells or by bacterially expressed activated ERK2; the phosphorylation sites were mapped to ERK kinase consensus sites in the TBP amino-terminal domain. Using glutathione S-transferase-TBP fusion proteins, cellular proteins that bind specifically to the TBP amino terminus have been identified. These observations suggest that ERK-mediated phosphorylation of TBP occurs during the PMA-induced differentiation of U937 cells and the stimulation of the G0-G1 transition in fibroblasts and could play a role in the regulation of TBP protein interactions and thus regulate gene transcription during these two processes.
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PMID:Activation of the mitogen-activated protein kinase pathway in U937 leukemic cells induces phosphorylation of the amino terminus of the TATA-binding protein. 971 83

Mounting evidence suggests that eukaryotic RNA polymerases preassociate with multiple transcription factors in the absence of DNA, forming RNA polymerase holoenzyme complexes. We have purified an apparent RNA polymerase I (Pol I) holoenzyme from Xenopus laevis cells by sequential chromatography on five columns: DEAE-Sepharose, Biorex 70, Sephacryl S300, Mono Q, and DNA-cellulose. Single fractions from every column programmed accurate promoter-dependent transcription. Upon gel filtration chromatography, the Pol I holoenzyme elutes at a position overlapping the peak of Blue Dextran, suggesting a molecular mass in the range of approximately 2 MDa. Consistent with its large mass, Coomassie blue-stained sodium dodecyl sulfate-polyacrylamide gels reveal approximately 55 proteins in fractions purified to near homogeneity. Western blotting shows that TATA-binding protein precisely copurifies with holoenzyme activity, whereas the abundant Pol I transactivator upstream binding factor does not. Also copurifying with the holoenzyme are casein kinase II and a histone acetyltransferase activity with a substrate preference for histone H3. These results extend to Pol I the suggestion that signal transduction and chromatin-modifying activities are associated with eukaryotic RNA polymerases.
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PMID:Histone acetyltransferase and protein kinase activities copurify with a putative Xenopus RNA polymerase I holoenzyme self-sufficient for promoter-dependent transcription. 985 2

The Drosophila homeodomain protein Even-skipped (Eve) is a well characterized transcriptional repressor. Here, we show that Eve's ability to function in vitro is negatively regulated by phosphorylation. DNA-binding activity was unaffected by phosphorylation, but phosphorylated Eve was unable to interact with the TATA-binding protein (TBP), a known target for repression. Unexpectedly, phosphorylation of the Eve N terminus, which is dispensable for repression and TBP binding, was necessary and sufficient to inactivate Eve. LiCl, which specifically inhibits glycogen synthase kinase-3 (GSK-3), reduced Eve phosphorylation in nuclear extract and blocked inhibition of repression. In addition, Eve was phosphorylated and inactivated by purified GSK-3 beta plus casein kinase II. Our results suggest a novel mechanism of transcriptional control involving phosphorylation-induced allosteric interference with a repressive protein-protein interaction.
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PMID:Allosteric regulation of even-skipped repression activity by phosphorylation. 1002 81


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