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Robert G Roeder - One of the best experts on this subject based on the ideXlab platform.
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thyroid hormone receptor associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA Box binding protein associated factors of tfiid
Proceedings of the National Academy of Sciences of the United States of America, 1999Co-Authors: Joseph D Fondell, Mohamed Guermah, Sohail Malik, Robert G RoederAbstract:Coactivators previously implicated in ligand-dependent activation functions by thyroid hormone receptor (TR) include p300 and CREB-binding protein (CBP), the steroid receptor coactivator-1 (SRC-1)-related family of proteins, and the multicomponent TR-associated protein (TRAP) complex. Here we show that two positive cofactors (PC2 and PC4) derived from the upstream stimulatory activity (USA) cofactor fraction act synergistically to mediate thyroid hormone (T3)-dependent activation either by TR or by a TR-TRAP complex in an in vitro system reconstituted with purified factors and DNA templates. Significantly, the TRAP-mediated enhancement of activation by TR does not require the TATA Box-binding protein-associated factors of TFIID. Furthermore, neither the pleiotropic coactivators CBP and p300 nor members of the SRC-1 family were detected in either the TR-TRAP complex or the other components of the in vitro assay system. These results show that activation by TR at the level of naked DNA templates is enhanced by cooperative functions of the TRAP coactivators and the general coactivators PC2 and PC4, and they further indicate a potential functional redundancy between TRAPs and TATA Box-binding protein-associated factors in TFIID. In conjunction with earlier studies on other nuclear receptor-interacting cofactors, the present study also suggests a multistep pathway, involving distinct sets of cofactors, for activation of hormone responsive genes.
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crystal structure of a human TATA Box binding protein TATA element complex
Proceedings of the National Academy of Sciences of the United States of America, 1996Co-Authors: Dimitar B Nikolov, Robert G Roeder, H Chen, E D Halay, Andrew S Hoffman, Stephen K BurleyAbstract:Abstract The TATA Box-binding protein (TBP) is required by all three eukaryotic RNA polymerases for correct initiation of transcription of ribosomal, messenger, small nuclear, and transfer RNAs. The cocrystal structure of the C-terminal/core region of human TBP complexed with the TATA element of the adenovirus major late promoter has been determined at 1.9 angstroms resolution. Structural and functional analyses of the protein-DNA complex are presented, with a detailed comparison to our 1.9-angstroms resolution structure of Arabidopsis thaliana TBP2 bound to the same TATA Box.
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crystal structure of tfiid TATA Box binding protein
Nature, 1992Co-Authors: Dimitar B Nikolov, Robert G Roeder, Judith Lin, Alexander Gasch, Alexander Hoffmann, Masami Horikoshi, Namhai Chua, Stephen K BurleyAbstract:The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-Box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 A resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.
Pellegrino Rossi - One of the best experts on this subject based on the ideXlab platform.
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cyclic adenosine monophosphate camp stimulation of the kit ligand promoter in sertoli cells requires an sp1 binding region a canonical TATA Box and a camp induced factor binding to an immediately downstream gc rich element
Biology of Reproduction, 2003Co-Authors: Paola Grimaldi, Federica Capolunghi, Raffaele Geremia, Pellegrino RossiAbstract:Expression of Kit ligand (KL) mRNA is induced in primary prepuberal Sertoli cells by FSH and by other agents that increase cAMP levels. The cAMP effect is exerted at the transcriptional level and appears to be cell type specific, since it is not observed in other KL-expressing primary cells or cell lines. Deletion analysis of the 5'-flanking region of the mouse KL gene shows that the proximal promoter sequence between -88 and +8 from the transcriptional start site is necessary and sufficient to obtain the full cAMP responsiveness of the promoter in primary mouse Sertoli cells. In the -88/+8 promoter region, several cis-acting elements play a role in cAMP response. The -88/-56 sequence is necessary for full induction of the gene, since its removal causes a drastic decrease in cAMP responsiveness; however, cAMP-stimulated expression is still observed with the minimal promoter region between -55 and +8. A more detailed mutational analysis of the minimal promoter region shows that mutations in the canonical TATA Box sequence and in an immediately downstream GC-rich element completely abolish cAMP responsiveness. DNA-binding experiments show that transcription factor Sp1 binds to the -88/-56 fragment of the KL proximal promoter in both control and cAMP-stimulated cells, whereas a new cAMP-induced complex is observed when the -55/+8 minimal promoter region is used as probe. The canonical TATA Box sequence is essential for formation of the latter complex. We also show that the binding of an unknown nuclear factor (different from Sp1, Egr-1, Rnf6, and AP-2) to a GC-rich element between -19 and +8 increases after cAMP treatment, and this effect seems to be specific of primary Sertoli cells. Thus, cAMP-induced transcription from the KL gene promoter in primary mouse Sertoli cells is mediated by a complex interaction among a Sp1-binding region, factors recognizing the canonical TATA Box sequence, and a not yet identified cAMP-induced factor binding a GC-rich sequence just downstream from it.
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cyclic amp stimulation of the kit ligand promoter in sertoli cells requires a sp1 binding region a canonical TATA Box and a camp induced factor binding to an immediately downstream gc rich element
2003Co-Authors: Paola Grimaldi, Federica Capolunghi, Raffaele Geremia, Pellegrino RossiAbstract:1 Expression of Kit Ligand (KL) mRNA is induced in primary pre-puberal Sertoli cells by FSH and 2 by other agents which increase cAMP levels. The cAMP effect is exerted at the transcriptional 3 level, and appears to be cell-type specific, since it is not observed in other KL expressing primary 4 cells or cell lines. Deletion analysis of the 5’ flanking region of the mouse KL gene shows that the 5 proximal promoter sequence between –88 and +8 from the transcriptional start site is necessary and 6 sufficient to obtain the full cAMP responsiveness of the promoter in primary mouse Sertoli cells. In 7 the –88/+8 promoter region several cis-acting elements play a role in cAMP response. The –88/-56 8 sequence is necessary for full induction of the gene, since its removal causes a drastic decrease in 9 cAMP responsiveness, however cAMP stimulated expression is still observed with the minimal 10 promoter region between –55 and +8. A more detailed mutational analysis of the minimal promoter 11 region shows that mutations in the canonical TATA Box sequence and in an immediately 12 downstream GC rich element completely abolish cAMP responsiveness. DNA-binding experiments 13 show that transcription factor Sp1 binds to the –88/-56 fragment of the KL proximal promoter in 14 both control and cAMP stimulated cells, whereas a new cAMP-induced complex is observed when 15 the –55/+8 minimal promoter region is used as probe. The canonical TATA Box sequence is 16 essential for formation of the latter complex. We also show that the binding of an unknown nuclear 17 factor (different from Sp1, Egr-1, Rnf6 and AP-2) to a GC-rich element between –19 and +8 18 increases after cAMP treatment, and this effect seems to be specific of primary Sertoli cells. Thus, 19 cAMP-induced transcription from the KL gene promoter in primary mouse Sertoli cells is mediated 20 by a complex interaction between a Sp1 binding region, factors recognizing the canonical TATA 21 Box sequence, and a not yet identified cAMP-induced factor binding a GC-rich sequence just 22 downstream from it. 23 24
Jack Greenblatt - One of the best experts on this subject based on the ideXlab platform.
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Topological localization of the human transcription factors IIA, IIB, TATA Box-binding protein, and RNA polymerase II-associated protein 30 on a class II promoter.
Journal of Biological Chemistry, 1994Co-Authors: Benoit Coulombe, Jack GreenblattAbstract:Abstract The human general transcription factors IIA and IIB bind directly to the TATA Box-binding protein (TBP), and modulate transcription initiation by RNA polymerase II. RAP30, the small subunit of TFIIF, binds to TFIIB and RNA polymerase II and recruits RNA polymerase II to a preinitiation complex containing TBP and TFIIB. By using the adenovirus 2 major late promoter tagged site-specifically with the photoactivatible cross-linking reagent N3R-dUMP we have localized TBP, two subunits of TFIIA (A35 and A21), TFIIB, and RAP30 along promoter DNA. TFIIA cross-linked to the coding strand opposite TBP at the TATA Box and cross-linked upstream of TBP around position -40. RAP30 cross-linked strongly and TFIIB weakly to the coding strand just downstream of TBP at -19. We interpret these data in the context of a molecular structure for the TBP promoter complex.
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species specific interaction of the glutamine rich activation domains of sp1 with the TATA Box binding protein
Molecular and Cellular Biology, 1994Co-Authors: Andrew Emili, Jack Greenblatt, C J InglesAbstract:We have used protein-blotting and protein affinity chromatography to demonstrate that each of the two glutamine-rich activation domains of the human transcription factor Sp1 can bind specifically and directly to the C-terminal evolutionarily conserved domain of the human TATA Box-binding protein (TBP). These activation domains of Sp1 also bind directly to Drosophila TBP but bind much less strongly to TBP from the yeast Saccharomyces cerevisiae. The abilities of the Sp1 activation domains to interact directly with the TBPs of various species correlate well with their abilities to activate transcription in extracts derived from the same species. We also show that a glutamine-rich transcriptional activating region of the Drosophila protein Antennapedia binds directly to TBP in a species-specific manner that reflects its ability to activate transcription in vivo. These results support the notion that TBP is a direct and important target of glutamine-rich transcriptional activators.
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direct interaction between the transcriptional activation domain of human p53 and the TATA Box binding protein
Journal of Biological Chemistry, 1993Co-Authors: Ray Truant, C J Ingles, Hua Xiao, Jack GreenblattAbstract:Abstract The human p53 tumor suppressor gene product can activate transcription by RNA polymerase II in the yeast, Saccharomyces cerevisiae, as well as in human cells. Several viral transcriptional activator proteins have been shown to directly contact TBP, the TATA Box-binding subunit of the general initiation factor, TFIID. In this report, we use protein affinity chromatography to show that the cellular transcription factor, p53, interacts directly and specifically with yeast TBP. The TBP binding domain of p53 was localized to its N-terminal 73 amino acids. This highly acidic portion of p53 functions as a transcriptional activation domain and is deleted in some tumors induced by the Friend leukemia virus. A human tumor-derived oncogenic point mutation of p53, which lies outside the activation domain of p53, but reduces its ability to activate transcription, greatly reduced the ability of p53 to bind yeast TBP in vitro. This mutation probably affects the overall conformation of the protein and indirectly interferes with the ability of p53 to contact TBP and activate transcription. In contrast, a mutated oncogenic form of p53 that is unaffected in its ability to activate transcription bound yeast TBP as well as wild type p53. The human TBP activity in a HeLa extract also bound to the activation domain of p53. Our data support a general model in which DNA-bound activator proteins activate transcription by interacting with TBP.
Michael R Green - One of the best experts on this subject based on the ideXlab platform.
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initiation of zebrafish haematopoiesis by the TATA Box binding protein related factor trf3
Nature, 2007Co-Authors: Daniel O Hart, Tamal Raha, Nathan D Lawson, Michael R GreenAbstract:It is shown for the first time that a vertebrate-specific member of the TATA-Box-binding protein (TBP) family, called TRF3, controls haematopoiesis in zebrafish embryogenesis. TATA-Box-binding protein (TBP)-related factor 3, TRF3 (also called TBP2), is a vertebrate-specific member of the TBP family that has a conserved carBoxy-terminal region and DNA-binding domain virtually identical to that of TBP (ref. 1). TRF3 is highly expressed during embryonic development, and studies in zebrafish and Xenopus have shown that it is required for normal embryogenesis2,3. Here we show that zebrafish embryos depleted of Trf3 exhibit multiple developmental defects and, in particular, fail to undergo haematopoiesis. Expression profiling for Trf3-dependent genes identified mespa, which encodes a transcription factor whose murine orthologue is required for mesoderm specification4, and chromatin immunoprecipitation verified that Trf3 binds to the mespa promoter. Depletion of Mespa resulted in developmental and haematopoietic defects markedly similar to those induced by Trf3 depletion. Injection of mespa messenger RNA (mRNA) restored normal development to a Trf3-depleted embryo, indicating mespa is the single Trf3 target gene required for zebrafish embryogenesis. Zebrafish embryos depleted of Trf3 or Mespa also failed to express cdx4, a caudal-related gene required for haematopoiesis. Mespa binds to the cdx4 promoter, and epistasis analysis revealed an ordered trf3–mespa–cdx4 pathway. Thus, in zebrafish, commitment of mesoderm to the haematopoietic lineage occurs through a transcription factor pathway initiated by a TBP-related factor.
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trf3 a TATA Box binding protein related factor is vertebrate specific and widely expressed
Proceedings of the National Academy of Sciences of the United States of America, 2003Co-Authors: Stephan P Persengiev, Xiaochun Zhu, Bharat L Dixit, Glenn A Maston, Ellen L W Kittler, Michael R GreenAbstract:TATA-Box-binding protein (TBP) is a highly conserved RNA polymerase II general transcription factor that binds to the core promoter and initiates assembly of the preinitiation complex. Two proteins with high homology to TBP have been found: TBP-related factor 1 (TRF1), described only in Drosophila melanogaster, and TRF2, which is broadly distributed in metazoans. Here, we report the identification and characterization of an additional TBP-related factor, TRF3. TRF3 is virtually identical to TBP in the C-terminal core domain, including all residues involved in DNA binding and interaction with other general transcription factors. Like other TBP family members, the N-terminal region of TRF3 is divergent. The TRF3 gene is present and expressed in vertebrates, from fish through humans, but absent from the genomes of the urochordate Ciona intestinalis and the lower eukaryotes D. melanogaster and Caenorhabditis elegans. TRF3 is a nuclear protein that is present in all human and mouse tissues and cell lines examined. Despite the highly homologous TBP-like C-terminal core domain, gel filtration analysis indicates that the native molecular weight of TRF3 is substantially less than that of TFIID. Interestingly, after mitosis, reimport of TRF3 into the nucleus occurs subsequent to TBP and other basal transcription factors. In summary, TRF3 is a highly conserved vertebrate-specific TRF whose phylogenetic conservation, expression pattern, and other properties are distinct from those of TBP and all other TRFs.
Paola Grimaldi - One of the best experts on this subject based on the ideXlab platform.
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cyclic adenosine monophosphate camp stimulation of the kit ligand promoter in sertoli cells requires an sp1 binding region a canonical TATA Box and a camp induced factor binding to an immediately downstream gc rich element
Biology of Reproduction, 2003Co-Authors: Paola Grimaldi, Federica Capolunghi, Raffaele Geremia, Pellegrino RossiAbstract:Expression of Kit ligand (KL) mRNA is induced in primary prepuberal Sertoli cells by FSH and by other agents that increase cAMP levels. The cAMP effect is exerted at the transcriptional level and appears to be cell type specific, since it is not observed in other KL-expressing primary cells or cell lines. Deletion analysis of the 5'-flanking region of the mouse KL gene shows that the proximal promoter sequence between -88 and +8 from the transcriptional start site is necessary and sufficient to obtain the full cAMP responsiveness of the promoter in primary mouse Sertoli cells. In the -88/+8 promoter region, several cis-acting elements play a role in cAMP response. The -88/-56 sequence is necessary for full induction of the gene, since its removal causes a drastic decrease in cAMP responsiveness; however, cAMP-stimulated expression is still observed with the minimal promoter region between -55 and +8. A more detailed mutational analysis of the minimal promoter region shows that mutations in the canonical TATA Box sequence and in an immediately downstream GC-rich element completely abolish cAMP responsiveness. DNA-binding experiments show that transcription factor Sp1 binds to the -88/-56 fragment of the KL proximal promoter in both control and cAMP-stimulated cells, whereas a new cAMP-induced complex is observed when the -55/+8 minimal promoter region is used as probe. The canonical TATA Box sequence is essential for formation of the latter complex. We also show that the binding of an unknown nuclear factor (different from Sp1, Egr-1, Rnf6, and AP-2) to a GC-rich element between -19 and +8 increases after cAMP treatment, and this effect seems to be specific of primary Sertoli cells. Thus, cAMP-induced transcription from the KL gene promoter in primary mouse Sertoli cells is mediated by a complex interaction among a Sp1-binding region, factors recognizing the canonical TATA Box sequence, and a not yet identified cAMP-induced factor binding a GC-rich sequence just downstream from it.
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cyclic amp stimulation of the kit ligand promoter in sertoli cells requires a sp1 binding region a canonical TATA Box and a camp induced factor binding to an immediately downstream gc rich element
2003Co-Authors: Paola Grimaldi, Federica Capolunghi, Raffaele Geremia, Pellegrino RossiAbstract:1 Expression of Kit Ligand (KL) mRNA is induced in primary pre-puberal Sertoli cells by FSH and 2 by other agents which increase cAMP levels. The cAMP effect is exerted at the transcriptional 3 level, and appears to be cell-type specific, since it is not observed in other KL expressing primary 4 cells or cell lines. Deletion analysis of the 5’ flanking region of the mouse KL gene shows that the 5 proximal promoter sequence between –88 and +8 from the transcriptional start site is necessary and 6 sufficient to obtain the full cAMP responsiveness of the promoter in primary mouse Sertoli cells. In 7 the –88/+8 promoter region several cis-acting elements play a role in cAMP response. The –88/-56 8 sequence is necessary for full induction of the gene, since its removal causes a drastic decrease in 9 cAMP responsiveness, however cAMP stimulated expression is still observed with the minimal 10 promoter region between –55 and +8. A more detailed mutational analysis of the minimal promoter 11 region shows that mutations in the canonical TATA Box sequence and in an immediately 12 downstream GC rich element completely abolish cAMP responsiveness. DNA-binding experiments 13 show that transcription factor Sp1 binds to the –88/-56 fragment of the KL proximal promoter in 14 both control and cAMP stimulated cells, whereas a new cAMP-induced complex is observed when 15 the –55/+8 minimal promoter region is used as probe. The canonical TATA Box sequence is 16 essential for formation of the latter complex. We also show that the binding of an unknown nuclear 17 factor (different from Sp1, Egr-1, Rnf6 and AP-2) to a GC-rich element between –19 and +8 18 increases after cAMP treatment, and this effect seems to be specific of primary Sertoli cells. Thus, 19 cAMP-induced transcription from the KL gene promoter in primary mouse Sertoli cells is mediated 20 by a complex interaction between a Sp1 binding region, factors recognizing the canonical TATA 21 Box sequence, and a not yet identified cAMP-induced factor binding a GC-rich sequence just 22 downstream from it. 23 24
