TATA Binding Protein

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 11244 Experts worldwide ranked by ideXlab platform

Robert Tjian - One of the best experts on this subject based on the ideXlab platform.

  • transcription properties of a cell type specific TATA Binding Protein trf
    Cell, 1997
    Co-Authors: Stig K. Hansen, Shinako Takada, Raymond H. Jacobson, John T. Lis, Robert Tjian
    Abstract:

    Abstract Eukaryotic cells are thought to contain a single TATA-Binding Protein (TBP) that directs transcription by cellular RNA polymerases. Here we report a cell type–specific TBP-related factor (TRF) that can form a stable TRF/IIA/IIB TATA DNA complex and substitute for TBP in directing RNA polymerase II transcription in vitro. Transfection studies reveal that TRF can differentially mediate activation by some enhancer Proteins but not others. Like TBP, TRF forms a stable complex containing multiple novel subunits, nTAFs. Antibody staining of embryos and polytene chromosomes reveals cell type–specific expression and gene-selective properties consistent with the shaker/male sterile phenotype of trf mutants. These findings suggest TRF is a homolog of TBP that functions to direct tissue- and gene-specific transcription.

  • Transcription Properties of a Cell Type–Specific TATA-Binding Protein, TRF
    Cell, 1997
    Co-Authors: Stig K. Hansen, Shinako Takada, Raymond H. Jacobson, John T. Lis, Robert Tjian
    Abstract:

    Abstract Eukaryotic cells are thought to contain a single TATA-Binding Protein (TBP) that directs transcription by cellular RNA polymerases. Here we report a cell type–specific TBP-related factor (TRF) that can form a stable TRF/IIA/IIB TATA DNA complex and substitute for TBP in directing RNA polymerase II transcription in vitro. Transfection studies reveal that TRF can differentially mediate activation by some enhancer Proteins but not others. Like TBP, TRF forms a stable complex containing multiple novel subunits, nTAFs. Antibody staining of embryos and polytene chromosomes reveals cell type–specific expression and gene-selective properties consistent with the shaker/male sterile phenotype of trf mutants. These findings suggest TRF is a homolog of TBP that functions to direct tissue- and gene-specific transcription.

  • Reconstitution of TATA-Binding Protein-associated factor/TATA-Binding Protein complexes for in vitro transcription.
    Methods in enzymology, 1996
    Co-Authors: Jin-long Chen, Robert Tjian
    Abstract:

    Publisher Summary This chapter describes strategies for assembling functionally active TAF /TBP (TBP-associated factors/TATA-Binding Protein) complexes. The chapter discusses methods developed to build TAF/TBP complexes in vitro . Using this powerful strategy, studies have revealed that different classes of activators function through different mechanisms involving distinct sets of TAFs to regulate transcription. Moreover, the functional analysis of partial complexes has shown that TAFs are also involved in core promoter recognition in basal transcription. Reconstitution experiments have suggested that the multisubunit nature of the TFIID (transcription factor IID) complex indeed contributes to transcriptional synergism and core promoter switching, two processes involved in important biological regulatory events. Interestingly, there are additional TBP-containing complexes that consist of distinct TAFs important for Pol I and Pol II transcription. In addition to TBP-containing complexes, several other transcription factors are composed of multiple subunits. For example, TFIIH has been shown to consist of at least 7 polypeptides, while RNA Pol II contains more than 10 subunits.

  • A new factor related to TATA-Binding Protein has highly restricted expression patterns in Drosophila
    Nature, 1993
    Co-Authors: Thomas E. Crowley, Timothy Hoey, Jen-kuei Liu, Yuh Nung Jan, Lily Yeh Jan, Robert Tjian
    Abstract:

    The TATA-Binding Protein TBP is necessary for the transcription of eukaryotic genes. Multi-Protein complexes formed by TBP and different TBP-associated factors are involved in the initiation of transcription by polymerases I and II, and probably III as well. During the formation of an active initiation complex, TBP makes specific contacts with other Proteins, for example TFIIB and RNA polymerase II (refs 2-4). Here we describe the cloning and characterization of a Drosophila gene product with considerable sequence similarity to TBP and a highly restricted expression pattern in the embryo. This TBP-related factor is a DNA-Binding Protein but is not likely to be a basal transcription factor. Our results suggest that TBP-related factor is a sequence-specific transcription factor that shares the DNA-Binding properties of TBP.

  • Isolation of coactivators associated with the TATA-Binding Protein that mediate transcriptional activation
    Cell, 1991
    Co-Authors: Brian David Dynlacht, Timothy Hoey, Robert Tjian
    Abstract:

    A key step in the regulation of transcription involves interactions between promoter-selective factors and various components of the transcriptional apparatus. Here we report the requirements for transcriptional activation directed by NTF-1, a developmentally regulated transcription factor in Drosophila. Reconstituted transcription with fractionated Drosophila basal factors reveals that activation by NTF-1 requires factors present in the endogenous TFIID fraction that are distinct from the purified TATA-Binding Protein (TBP). Glycerol gradient sedimentation and immunoprecipitation analyses indicate that TFIID is a multiProtein complex containing TBP and at least six tightly bound TBP-associated factors (TAFs). Preparations of TBP lacking TAFs after fractionation with denaturants no longer support activation by NTF-1 but retain basal level activity. Addition of immunopurified and renatured TAFs to free TBP restores the ability of NTF-1 to activate transcription without influencing basal transcription. These results suggest that one or more of the TAF polypeptides confer coactivator function.

David T. Auble - One of the best experts on this subject based on the ideXlab platform.

  • The dynamic personality of TATA-Binding Protein.
    Trends in biochemical sciences, 2008
    Co-Authors: David T. Auble
    Abstract:

    TATA-Binding Protein (TBP) is a central component of the transcription apparatus and its association with promoters is dynamically regulated genome-wide. Recent work has shed new light on the functional specificity of Mot1 and NC2, two factors that control TBP distribution and activity. These studies underscore how regulation of TBP globally influences fundamental aspects of gene expression, including the balance of transcriptional output from different types of promoters, and the amplitude and timing of gene activation.

  • regulation of TATA Binding Protein dynamics in living yeast cells
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Rebekka O. Sprouse, Tatiana S. Karpova, Florian Mueller, Arindam Dasgupta, James G. Mcnally, David T. Auble
    Abstract:

    Abstract Although pathways for assembly of RNA polymerase (Pol) II transcription preinitiation complexes (PICs) have been well established in vitro, relatively little is known about the dynamic behavior of Pol II general transcription factors in vivo. In vitro, a subset of Pol II factors facilitates reinitiation by remaining very stably bound to the promoter. This behavior contrasts markedly with the highly dynamic behavior of RNA Pol I transcription complexes in vivo, which undergo cycles of disassembly/reassembly at the promoter for each round of transcription. To determine whether the dynamic behavior of the Pol II machinery in vivo is fundamentally different from that of Pol I and whether the static behavior of Pol II factors in vitro fully recapitulates their behavior in vivo, we used fluorescence recovery after photobleaching (FRAP). Surprisingly, we found that all or nearly all of the TATA-Binding Protein (TBP) population is highly mobile in vivo, displaying FRAP recovery rates of <15 s. These high rates require the activity of the TBP-associated factor Mot1, suggesting that TBP/chromatin interactions are destabilized by active cellular processes. Furthermore, the distinguishable FRAP behavior of TBP and TBP-associated factor 1 indicates that there are populations of these molecules that are independent of one another. The distinct FRAP behavior of most Pol II factors that we tested suggests that transcription complexes assemble via stochastic multistep pathways. Our data indicate that active Pol II PICs can be much more dynamic than previously considered. fluorescence recovery after photobleaching Mot1 TFIID

  • Regulation of TATA-Binding Protein dynamics in living yeast cells
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Rebekka O. Sprouse, Tatiana S. Karpova, Florian Mueller, Arindam Dasgupta, James G. Mcnally, David T. Auble
    Abstract:

    Abstract Although pathways for assembly of RNA polymerase (Pol) II transcription preinitiation complexes (PICs) have been well established in vitro, relatively little is known about the dynamic behavior of Pol II general transcription factors in vivo. In vitro, a subset of Pol II factors facilitates reinitiation by remaining very stably bound to the promoter. This behavior contrasts markedly with the highly dynamic behavior of RNA Pol I transcription complexes in vivo, which undergo cycles of disassembly/reassembly at the promoter for each round of transcription. To determine whether the dynamic behavior of the Pol II machinery in vivo is fundamentally different from that of Pol I and whether the static behavior of Pol II factors in vitro fully recapitulates their behavior in vivo, we used fluorescence recovery after photobleaching (FRAP). Surprisingly, we found that all or nearly all of the TATA-Binding Protein (TBP) population is highly mobile in vivo, displaying FRAP recovery rates of

  • Regulation of rRNA Synthesis by TATA-Binding Protein-Associated Factor Mot1
    Molecular and cellular biology, 2007
    Co-Authors: Arindam Dasgupta, Rebekka O. Sprouse, Pavel Aprikian, Sarah L. French, Robert D. Hontz, Sarah A. Juedes, Jeffrey S. Smith, Ann L. Beyer, David T. Auble
    Abstract:

    Mot1 is an essential, conserved, TATA-Binding Protein (TBP)-associated factor in Saccharomyces cerevisiae with well-established roles in the global control of RNA polymerase II (Pol II) transcription. Previous results have suggested that Mot1 functions exclusively in Pol II transcription, but here we report a novel role for Mot1 in regulating transcription by RNA polymerase I (Pol I). In vivo, Mot1 is associated with the ribosomal DNA, and loss of Mot1 results in decreased rRNA synthesis. Consistent with a direct role for Mot1 in Pol I transcription, Mot1 also associates with the Pol I promoter in vitro in a reaction that depends on components of the Pol I general transcription machinery. Remarkably, in addition to Mot1's role in initiation, rRNA processing is delayed in mot1 cells. Taken together, these results support a model in which Mot1 affects the rate and efficiency of rRNA synthesis by both direct and indirect mechanisms, with resulting effects on transcription activation and the coupling of rRNA synthesis to processing.

  • A new regulatory domain on the TATA-Binding Protein.
    The EMBO journal, 1999
    Co-Authors: Yong Cang, David T. Auble, Gregory Prelich
    Abstract:

    Recognition of the TATA box by the TATA-Binding Protein (TBP) is a highly regulated step in RNA polymerase II-dependent transcription. Several Proteins have been proposed to regulate TBP activity, yet the TBP domains responsive to all these regulators have not been defined. Here we describe a new class of TBP mutants that increase transcription from core promoters in vivo. The majority of these mutations alter amino acids that cluster tightly on the TBP surface, defining a new TBP regulatory domain. The mutant TBP Proteins are defective for Binding the transcriptional regulator yNC2, are resistant to inhibition by yNC2 in vitro and exhibit allele-specific genetic interactions with yNC2. These results provide strong biochemical and genetic evidence that TBP is directly repressed in vivo, and define a new TBP domain important for transcriptional regulation.

John T. Lis - One of the best experts on this subject based on the ideXlab platform.

  • Transcription Properties of a Cell Type–Specific TATA-Binding Protein, TRF
    Cell, 1997
    Co-Authors: Stig K. Hansen, Shinako Takada, Raymond H. Jacobson, John T. Lis, Robert Tjian
    Abstract:

    Abstract Eukaryotic cells are thought to contain a single TATA-Binding Protein (TBP) that directs transcription by cellular RNA polymerases. Here we report a cell type–specific TBP-related factor (TRF) that can form a stable TRF/IIA/IIB TATA DNA complex and substitute for TBP in directing RNA polymerase II transcription in vitro. Transfection studies reveal that TRF can differentially mediate activation by some enhancer Proteins but not others. Like TBP, TRF forms a stable complex containing multiple novel subunits, nTAFs. Antibody staining of embryos and polytene chromosomes reveals cell type–specific expression and gene-selective properties consistent with the shaker/male sterile phenotype of trf mutants. These findings suggest TRF is a homolog of TBP that functions to direct tissue- and gene-specific transcription.

  • transcription properties of a cell type specific TATA Binding Protein trf
    Cell, 1997
    Co-Authors: Stig K. Hansen, Shinako Takada, Raymond H. Jacobson, John T. Lis, Robert Tjian
    Abstract:

    Abstract Eukaryotic cells are thought to contain a single TATA-Binding Protein (TBP) that directs transcription by cellular RNA polymerases. Here we report a cell type–specific TBP-related factor (TRF) that can form a stable TRF/IIA/IIB TATA DNA complex and substitute for TBP in directing RNA polymerase II transcription in vitro. Transfection studies reveal that TRF can differentially mediate activation by some enhancer Proteins but not others. Like TBP, TRF forms a stable complex containing multiple novel subunits, nTAFs. Antibody staining of embryos and polytene chromosomes reveals cell type–specific expression and gene-selective properties consistent with the shaker/male sterile phenotype of trf mutants. These findings suggest TRF is a homolog of TBP that functions to direct tissue- and gene-specific transcription.

  • Recruiting TATA-Binding Protein to a promoter: transcriptional activation without an upstream activator.
    Molecular and cellular biology, 1995
    Co-Authors: Hua Xiao, J. D. Friesen, John T. Lis
    Abstract:

    The Binding of TATA-Binding Protein (TBP) to the TATA element is the first step in the initiation of RNA polymerase II transcription from many promoters in vitro. It has been proposed that upstream activator Proteins stimulate transcription by recruiting TBP to the promoter, thus facilitating the assembly of a transcription complex. However, the role of activator Proteins acting at this step to stimulate transcription in vivo remains largely speculative. To test whether recruitment of TBP to the promoter is sufficient for transcriptional activation in vivo, we constructed a hybrid Protein containing TBP of the yeast Saccharomyces cerevisiae fused to the DNA-Binding domain of GAL4. Our results show that TBP recruited by the GAL4 DNA-Binding domain to promoters bearing a GAL4-Binding site can interact with the TATA element and direct high levels of transcription. This finding indicates that Binding of TBP to promoters in S. cerevisiae is a major rate-limiting step accelerated by upstream activator Proteins.

H. Th. Marc Timmers - One of the best experts on this subject based on the ideXlab platform.

  • Suppression of intragenic transcription requires the MOT1 and NC2 regulators of TATA-Binding Protein
    Nucleic acids research, 2014
    Co-Authors: Maria J.e. Koster, Frank C. P. Holstege, P. Anthony Weil, Asli D. Yildirim, H. Th. Marc Timmers
    Abstract:

    Chromatin structure in transcribed regions poses a barrier for intragenic transcription. In a comprehensive study of the yeast chromatin remodelers and the Mot1p-NC2 regulators of TATA-Binding Protein (TBP), we detected synthetic genetic interactions indicative of suppression of intragenic transcription. Conditional depletion of Mot1p or NC2 in absence of the ISW1 remodeler, but not in the absence of other chromatin remodelers, activated the cryptic FLO8 promoter. Likewise, conditional depletion of Mot1p or NC2 in deletion backgrounds of the H3K36 methyltransferase Set2p or the Asf1p-Rtt106p histone H3-H4 chaperones, important factors involved in maintaining a repressive chromatin environment, resulted in increased intragenic FLO8 transcripts. Activity of the cryptic FLO8 promoter is associated with reduced H3 levels, increased TBP Binding and tri-methylation of H3K4 and is independent of Spt-Ada-Gcn5-acetyltransferase function. These data reveal cooperation of negative regulation of TBP with specific chromatin regulators to inhibit intragenic transcription.

  • Chromatin interaction of TATA-Binding Protein is dynamically regulated in human cells.
    Journal of cell science, 2010
    Co-Authors: Petra De Graaf, Florence Mousson, Laszlo Tora, Bart Geverts, Elisabeth Scheer, Adriaan B Houtsmuller, H. Th. Marc Timmers
    Abstract:

    Gene transcription in mammalian cells is a dynamic process involving regulated assembly of transcription complexes on chromatin in which the TATA-Binding Protein (TBP) plays a central role. Here, we investigate the dynamic behaviour of TBP by a combination of fluorescence recovery after photobleaching (FRAP) and biochemical assays using human cell lines of different origin. The majority of nucleoplasmic TBP and other TFIID subunits associate with chromatin in a highly dynamic manner. TBP dynamics are regulated by the joint action of the SNF2-related BTAF1 Protein and the NC2 complex. Strikingly, both BTAF1 and NC2 predominantly affect TBP dissociation rates, leaving the association rate unchanged. Chromatin immunoprecipitation shows that BTAF1 negatively regulates TBP and NC2 Binding to active promoters. Our results support a model for a BTAF1-mediated release of TBP-NC2 complexes from chromatin.

  • The TATA box regulates TATA-Binding Protein (TBP) dynamics in vivo.
    Trends in biochemical sciences, 2010
    Co-Authors: Laszlo Tora, H. Th. Marc Timmers
    Abstract:

    Early work established the TATA box as the predominant DNA element of core promoters which directed accurate transcription initiation by RNA polymerase II. This element is recognized by TATA-Binding Protein (TBP), the central DNA-Binding subunit of TFIID. In vitro Binding and structural experiments indicate that TBP has a strong preference for TATA and induces severe DNA bending. Recent in vivo studies in Saccharomyces cerevisiae indicate that TBP turnover is higher at TATA-containing than at TATA-less promoters; this turnover seems to be regulated by NC2 and Mot1p. We propose that bending of TATA by TBP acts in synergy with NC2 and Mot1p to release TBP more rapidly from TATA promoters in vivo, thus providing a rationale for the predominance of TATA boxes in highly regulated promoters versus constitutively active TATA-less promoters.

  • Quantitative Proteomics Reveals Regulation of Dynamic Components within TATA-Binding Protein (TBP) Transcription Complexes
    Molecular & cellular proteomics : MCP, 2007
    Co-Authors: Florence Mousson, Annemieke Kolkman, W.w.m. Pim Pijnappel, H. Th. Marc Timmers, Albert J. R. Heck
    Abstract:

    Affinity purification in combination with isotope labeling of Proteins has proven to be a powerful method to discriminate specific from nonspecific interactors. However, in the standard SILAC (stable isotope labeling by amino acids in cell culture) approach dynamic components may easily be assigned as nonspecific. We compared two affinity purification protocols, which in combination revealed information on the dynamics of Protein complexes. We focused on the central component in eukaryotic transcription, the human TATA-Binding Protein, which is involved in different complexes. All known TATA-Binding Protein-associated factors (TAFs) were detected as specific interactors. Interestingly one of them, BTAF1, exchanged significantly in cell extracts during the affinity purification. The other TAFs did not display this behavior. Cell cycle synchronization showed that BTAF1 exchange was regulated during mitosis. The combination of the two affinity purification protocols allows a quantitative approach to identify transient components in any Protein complex.

Stephen P. Jackson - One of the best experts on this subject based on the ideXlab platform.

  • Cloning and functional analysis of the TATA Binding Protein from Sulfolobus shibatae
    Nucleic acids research, 1995
    Co-Authors: Sohail A. Qureshi, Tracey Rowlands, Peter Baumann, Bernard Khoo, Stephen P. Jackson
    Abstract:

    Archaea (formerly archaebacteria) comprise a domain of life that is phylogenetically distinct from both Eucarya and Bacteria. Here we report the cloning of a gene from the Archaeon Sulfolobus shibatae that encodes a Protein with strong homology to the TATA Binding Protein (TBP) of eukaryotes. Sulfolobus shibatae TBP is, however, almost as diverged from other archaeal TBPs that have been cloned as it is from eukaryotic TBPs. DNA Binding studies indicate that S.shibatae TBP recognizes TATA-like A-box sequences that are present upstream of most archaeal genes. By quantitatively immunodepleting S.shibatae TBP from an in vitro transcription system, we demonstrate that Sulfolobus RNA polymerase is capable of transcribing the 16S/23S rRNA promoter weakly in the absence of TBP. Most significantly, we show that addition of recombinant S.shibatae TBP to this immunodepleted system leads to transcriptional stimulation and that this stimulation is dependent on the A-box sequence of the promoter. Taken together, these findings reveal fundamental similarities between the transcription machineries of Archaea and eukaryotes.

  • Mitotic regulation of a TATA-Binding-Protein-containing complex.
    Molecular and cellular biology, 1995
    Co-Authors: Robert J. White, Tanya M. Gottlieb, C S Downes, Stephen P. Jackson
    Abstract:

    The mitotic state is associated with a generalized repression of transcription. We show that mitotic repression of RNA polymerase III transcription can be reproduced by using extracts of synchronized HeLa cells. We have used this system to investigate the molecular basis of transcriptional repression during mitosis. We find a specific decrease in the activity of the TATA-Binding-Protein (TBP)-containing complex TFIIIB. TBP itself is hyperphosphorylated at mitosis, but this does not appear to account for the loss of TFIIIB activity. Instead, one or more TBP-associated components appear to be regulated. The data suggest that changes in the activity of TBP-associated components contribute to the coordinate repression of gene expression that occurs at mitosis.

  • the TATA Binding Protein a general transcription factor in eukaryotes and archaebacteria
    Science, 1994
    Co-Authors: Tracey Rowlands, Peter Baumann, Stephen P. Jackson
    Abstract:

    The TATA-Binding Protein TBP appears to be essential for all transcription in eukaryotic cell nuclei, which suggests that its function was established early in evolution. Archaebacteria constitute a kingdom of organisms distinct from eukaryotes and eubacteria. Archaebacterial gene regulatory sequences often map to TATA box-like motifs. Here it is shown that the archaebacterium Pyrococcus woesei expresses a Protein with structural and functional similarity to eukaryotic TBP molecules. This suggests that TBP9s role in transcription was established before the archaebacterial and eukaryotic lineages diverged and that the transcription systems of archaebacteria and eukaryotes are fundamentally homologous.

  • Mechanism of TATA-Binding Protein recruitment to a TATA-less class III promoter
    Cell, 1992
    Co-Authors: Robert J. White, Stephen P. Jackson
    Abstract:

    The TATA-Binding Protein (TBP) is required for transcription by RNA polymerase III (pol III), even though many pol III templates, such as the adenovirus VA1 gene, lack a consensus TATA box. We show that TBP alone does not form a stable, productive interaction with VA1 DNA. However, it can be incorporated into an initiation complex if the other class III basal factors, TFIIIB and TFIIIC, are also present. TFIIIB can associate with the evolutionarily conserved C-terminal domain of TBP in the absence of DNA or TFIIIC, suggesting that TFIIIB exists in solution as a complex with TBP. The stable association of TBP with an essential component of the pol III transcription apparatus may account for the ability of TATA-less class III genes to recruit TBP.

Related terms

TATA Binding Protein - 15 days free trial to Access Experts & Abstracts