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Paul M. Lieberman - One of the best experts on this subject based on the ideXlab platform.
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TAFII250 Phosphorylates Human Transcription Factor IIA on Serine Residues Important for TBP Binding and Transcription Activity
Journal of Biological Chemistry, 2001Co-Authors: Steven P. Solow, Moreh Salunek, Robert F. Ryan, Paul M. LiebermanAbstract:Abstract Transcription Factor IIA (TFIIA) is a positive acting general Factor that contacts the TATA-binding protein (TBP) and mediates an activator-induced conformational change in the Transcription Factor IID (TFIID) complex. Previously, we have found that phosphorylation of yeast TFIIA stimulates TFIIA·TBP·TATA complex formation and Transcription activation in vivo. We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA αβ reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate Transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function. In vitro, holo-TFIID and TBP-associated Factor 250 (TAFII250) phosphorylated TFIIA on the β subunit. Mutation of the four serines required for in vivophosphorylation eliminated TFIID and TAFII250 phosphorylation in vitro. The NH2-terminal kinase domain of TAFII250 was sufficient for TFIIA phosphorylation, and this activity was inhibited by full-length retinoblastoma protein but not by a retinoblastoma protein mutant defective for TAFII250 interaction or tumor suppressor activity. TFIIA phosphorylation had little effect on the TFIIA·TBP·TATA complex in electrophoretic mobility shift assay. However, phosphorylation of TFIIA containing a γ subunit Y65A mutation strongly stimulated TFIIA·TBP·TATA complex formation. TFIIA-γY65A is defective for binding to the β-sheet domain of TBP identified in the crystal structure. These results suggest that TFIIA phosphorylation is important for strengthening the TFIIA·TBP contact or creating a second contact between TFIIA and TBP that was not visible in the crystal structure.
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A Testis-specific Transcription Factor IIA (TFIIAτ) Stimulates TATA-binding Protein-DNA Binding and Transcription Activation
Journal of Biological Chemistry, 2000Co-Authors: Josef Ozer, Paul A. Moore, Paul M. LiebermanAbstract:Abstract The general Transcription Factor IIA (TFIIA) stimulates RNA polymerase II-specific Transcription by stabilizing the association of the TATA-binding protein (TBP) with promoter DNA, inhibiting repressors of TBP, and facilitating activator-dependent conformational changes in the preinitiation complex. TFIIA is encoded by two genes (αβ and γ) that are highly conserved between human and yeast. Here, we report the molecular cloning of a novel human gene that shares significant sequence similarity to the evolutionarily conserved amino- and carboxyl-terminal domains of TFIIAαβ. The TFIIA-related protein (TFIIAτ) was cloned from a testis-specific cDNA library, and its mRNA is expressed predominantly in testis tissue as determined by expressed sequence tag data base analysis and Northern blotting analysis. The TFIIA complex reconstituted with the testis-specific subunit, TFIIA (τ+γ), formed the TFIIA-TBP-TATA DNA (T-A) and TFIIA-TFIIB-TBP-TATA DNA (TAB) complexes indistinguishably from TFIIA (αβ+γ). TFIIA (τ+γ) supported basal and activated Transcription for most activators in reactions reconstituted with TFIIA-depleted nuclear extracts. However, TFIIA (τ+γ) was reduced relative to TFIIA (αβ+γ) for stimulating Transcription with at least one activator, suggesting that these two forms of TFIIA have activator specificity. These results suggest that TFIIAτ may be important for testis-specific Transcription regulation.
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Phosphorylation of TFIIA Stimulates TATA Binding Protein-TATA Interaction and Contributes to Maximal Transcription and Viability in Yeast
Molecular and Cellular Biology, 1999Co-Authors: Steven P. Solow, Larissa Lezina, Paul M. LiebermanAbstract:Posttranslational modification of general Transcription Factors may be an important mechanism for global gene regulation. The general Transcription Factor IIA (TFIIA) binds to the TATA binding protein (TBP) and is essential for high-level Transcription mediated by various activators. Modulation of the TFIIA-TBP interaction is a likely target of Transcriptional regulation. We report here that Toa1, the large subunit of yeast TFIIA, is phosphorylated in vivo and that this phosphorylation stabilizes the TFIIA-TBP-DNA complex and is required for high-level Transcription. Alanine substitution of serine residues 220, 225, and 232 completely eliminated in vivo phosphorylation of Toa1, although no single amino acid substitution of these serine residues eliminated phosphorylation in vivo. Phosphorylated TFIIA was 30-fold more efficient in forming a stable complex with TBP and TATA DNA. Dephosphorylation of yeast-derived TFIIA reduced DNA binding activity, and recombinant TFIIA could be stimulated by in vitro phosphorylation with casein kinase II. Yeast strains expressing the toa1 S220/225/232A showed reduced high-level Transcriptional activity at the URA1, URA3, and HIS3 promoters but were viable. However, S220/225/232A was synthetically lethal when combined with an alanine substitution mutation at W285, which disrupts the TFIIA-TBP interface. Phosphorylation of TFIIA could therefore be an important mechanism of Transcription modulation, since it stimulates TFIIA-TBP association, enhances high-level Transcription, and contributes to yeast viability. Eukaryotic RNA polymerases require the formation of a multiprotein preinitiation complex near the promoter start site for efficient Transcription initiation to occur (reviewed in references 8, 42, 49, and 63). The composition of the preinitiation complex may vary among promoters, but the best-studied model promoters indicate that the preinitiation complex consists of the general Transcription Factors TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH. The formation of the preinitiation complex and the subsequent recruitment of RNA polymerase II to the promoter start site can be rate limiting for Transcription in vitro and in vivo and are subject to regulation by activators and repressors. Precisely how activators and repressors
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Transcription Factor IIA Derepresses TATA-binding Protein (TBP)-associated Factor Inhibition of TBP-DNA Binding
Journal of Biological Chemistry, 1998Co-Authors: Josef Ozer, Katherine Mitsouras, Dennis Zerby, Michael F. Carey, Paul M. LiebermanAbstract:Abstract The interaction of the general Transcription Factor (TF) IIA with TFIID is required for Transcription activationin vitro. TFIID consists of the TATA-binding protein (TBP) and TBP associated Factors (TAFIIs). TFIIA binds directly to TBP and stabilizes its interaction with TATA-containing DNA. In this work, we present evidence that TAFIIs inhibit TBP-DNA and TBP-TFIIA binding, and that TFIIA stimulates Transcription, in part, by overcoming this TAFII-mediated inhibition of TBP-DNA binding. TFIIA mutants modestly compromised for interaction with TBP were found to be significantly more defective in forming complexes with TFIID. Subtle changes in the stability or conformation of the TFIIA-TBP complex resulted in a failure of TFIIA to overcome TAFII-mediated inhibition of TBP-DNA binding and Transcription function. Inhibition of TBP-DNA binding by TAFIIs could be partially relieved by limited proteolysis of TFIID. Proteolysis significantly stimulated TFIIA-TFIID-TATA binding in both electrophoresis mobility shift assay and DNase I footprinting but had little effect on complexes formed with TBP. Recombinant TAFII250 inhibits TBP-DNA binding, whereas preincubation of TFIIA with TBP prevents this inhibition. Thus, TFIIA competes with TAFII250 for access to TBP and alters the TATA binding properties of the resulting complex. Transcriptional activation by Zta was enhanced by temperature shift inactivation of TAFII250 in the ts13 cell line, suggesting that TAFII250 has Transcriptional inhibitory activity in vivo. Together, these results suggest that TAFIIs may regulate Transcription initiation by inhibiting TBP-TFIIA and TBP-DNA complex formation.
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Association of Transcription Factor IIA with TATA Binding Protein Is Required for Transcriptional Activation of a Subset of Promoters and Cell Cycle Progression inSaccharomyces cerevisiae
Molecular and Cellular Biology, 1998Co-Authors: Josef Ozer, Larissa Lezina, Joshua Ewing, Salma Audi, Paul M. LiebermanAbstract:The general Transcription Factor IIA (TFIIA) interacts with the TATA binding protein (TBP) and promoter DNA to mediate Transcription activation in vitro. To determine if this interaction is generally required for activation of all class II genes in vivo, we have constructed substitution mutations in yeast TFIIA which compromise its ability to bind TBP. Substitution mutations in the small subunit of TFIIA (Toa2) at residue Y69 or W76 significantly impaired the ability of TFIIA to stimulate TBP-promoter binding in vitro. Gene replacement of wild-type TOA2 with a W76E or Y69A/W76A mutant was lethal in Saccharomyces cerevisiae, while the Y69F/W76F mutant exhibited extremely slow growth at 30°C. Both the Y69A and W76A mutants were conditionally lethal at higher temperatures. Light microscopy indicated that viable toa2 mutant strains accumulate as equal-size dumbbells and multibudded clumps. Transcription of the cell cycle-regulatory genes CLB1, CLB2, CLN1, and CTS1 was significantly reduced in the toa2 mutant strains, while the noncycling genes PMA1 and ENO2 were only modestly affected, suggesting that these toa2 mutant alleles disrupt cell cycle progression. The differential effect of these toa2 mutants on gene Transcription was examined for a number of other genes. toa2 mutant strains supported high levels of CUP1, PHO5, TRP3, and GAL1 gene activation, but the constitutive expression of DED1 was significantly reduced. Activator-induced start site expression for HIS3, GAL80, URA1, and URA3 promoters was defective in toa2 mutant strains, suggesting that the TFIIA-TBP complex is important for promoters which require an activator-dependent start site selection from constitutive to regulated expression. We present evidence to indicate that Transcription defects in toa2 mutants can be both activator and promoter dependent. These results suggest that the association of TFIIA with TBP regulates activator-induced start site selection and cell cycle progression in S. cerevisiae.
Kevin Struhl - One of the best experts on this subject based on the ideXlab platform.
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Transcriptional Activation in Yeast Cells Lacking Transcription Factor IIA
Genetics, 1999Co-Authors: Susanna Chou, Sukalyan Chatterjee, Mark Lee, Kevin StruhlAbstract:The general Transcription Factor IIA (TFIIA) forms a complex with TFIID at the TATA promoter element, and it inhibits the function of several negative regulators of the TATA-binding protein (TBP) subunit of TFIID. Biochemical experiments suggest that TFIIA is important in the response to Transcriptional activators because activation domains can interact with TFIIA, increase recruitment of TFIID and TFIIA to the promoter, and promote isomerization of the TFIID-TFIIA-TATA complex. Here, we describe a double-shut-off approach to deplete yeast cells of Toa1, the large subunit of TFIIA, to
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Transcriptional activation in yeast cells lacking Transcription Factor IIA
Genetics, 1999Co-Authors: Susanna Chou, Sukalyan Chatterjee, Mark Lee, Kevin StruhlAbstract:The general Transcription Factor IIA (TFIIA) forms a complex with TFIID at the TATA promoter element, and it inhibits the function of several negative regulators of the TATA-binding protein (TBP) subunit of TFIID. Biochemical experiments suggest that TFIIA is important in the response to Transcriptional activators because activation domains can interact with TFIIA, increase recruitment of TFIID and TFIIA to the promoter, and promote isomerization of the TFIID-TFIIA-TATA complex. Here, we describe a double-shut-off approach to deplete yeast cells of Toa1, the large subunit of TFIIA, to <1% of the wild-type level. Interestingly, such TFIIA-depleted cells are essentially unaffected for activation by heat shock Factor, Ace1, and Gal4-VP16. However, depletion of TFIIA causes a general two- to threefold decrease of Transcription from most yeast promoters and a specific cell-cycle arrest at the G2-M boundary. These results indicate that Transcriptional activation in vivo can occur in the absence of TFIIA.
Taka-aki Tamura - One of the best experts on this subject based on the ideXlab platform.
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activity of the upstream tata less promoter of the p21waf1 cip1 gene depends on Transcription Factor IIA tfIIA in addition to tfIIA reactive tbp like protein
FEBS Journal, 2014Co-Authors: Hidefumi Suzuki, Tomoyoshi Nakadai, Ryo Maeda, Taka-aki TamuraAbstract:TATA-binding protein-like protein (TLP) binds to Transcription Factor IIA (TFIIA) with high affinity, although the significance of this binding is poorly understood. In this study, we investigated the role of TFIIA in Transcriptional regulation of the p21Waf1/Cip1 (p21) gene. It has been shown that TLP is indispensable for p53-activated Transcription from an upstream TATA-less promoter of the p21 gene. We found that mutant TLPs having decreased TFIIA-binding ability exhibited weakened Transcriptional activation function for the upstream promoter. Activity of the upstream promoter was enhanced considerably by an increased amount of TFIIA in a p53-dependent manner, whereas activity of the TATA-containing downstream promoter was enhanced only slightly. TFIIA potentiated the upstream promoter additively with TLP. Although TFIIA is recruited to both promoters, activity of the upstream promoter was much more dependent on TFIIA. Recruitment of TFIIA and TLP to the upstream promoter was augmented in etoposide-treated cells, in which the amount of TFIIA–TLP complex is increased, and TFIIA-reactive TLP was required for the recruitment of both Factors. It was confirmed that etoposide-stimulated Transcription depends on TLP. We also found that TFIIA-reactive TLP acts to decrease cell growth rate, which can be explained by interaction of the p21 promoter with the Transcription Factors that we examined. The results of the present study suggest that the upstream TATA-less promoter of p21 needs TFIIA and TFIIA-reactive TLP for p53-dependent Transcriptional enhancement. Structured digital abstract TLP physically interacts with TFIIA beta and TFIIA alpha by anti tag coimmunoprecipitation (View interaction) TFIIA alpha/beta physically interacts with TLP by anti bait coip (View interaction)
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Activity of the upstream TATA-less promoter of the p21Waf1/Cip1 gene depends on Transcription Factor IIA (TFIIA) in addition to TFIIA-reactive TBP-like protein
FEBS Journal, 2014Co-Authors: Hidefumi Suzuki, Tomoyoshi Nakadai, Ryo Maeda, Taka-aki TamuraAbstract:TATA-binding protein-like protein (TLP) binds to Transcription Factor IIA (TFIIA) with high affinity, although the significance of this binding is poorly understood. In this study, we investigated the role of TFIIA in Transcriptional regulation of the p21Waf1/Cip1 (p21) gene. It has been shown that TLP is indispensable for p53-activated Transcription from an upstream TATA-less promoter of the p21 gene. We found that mutant TLPs having decreased TFIIA-binding ability exhibited weakened Transcriptional activation function for the upstream promoter. Activity of the upstream promoter was enhanced considerably by an increased amount of TFIIA in a p53-dependent manner, whereas activity of the TATA-containing downstream promoter was enhanced only slightly. TFIIA potentiated the upstream promoter additively with TLP. Although TFIIA is recruited to both promoters, activity of the upstream promoter was much more dependent on TFIIA. Recruitment of TFIIA and TLP to the upstream promoter was augmented in etoposide-treated cells, in which the amount of TFIIA–TLP complex is increased, and TFIIA-reactive TLP was required for the recruitment of both Factors. It was confirmed that etoposide-stimulated Transcription depends on TLP. We also found that TFIIA-reactive TLP acts to decrease cell growth rate, which can be explained by interaction of the p21 promoter with the Transcription Factors that we examined. The results of the present study suggest that the upstream TATA-less promoter of p21 needs TFIIA and TFIIA-reactive TLP for p53-dependent Transcriptional enhancement. Structured digital abstract TLP physically interacts with TFIIA beta and TFIIA alpha by anti tag coimmunoprecipitation (View interaction) TFIIA alpha/beta physically interacts with TLP by anti bait coip (View interaction)
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Chromosomal position, structure, expression, and requirement of genes for chicken Transcription Factor IIA.
Gene, 2007Co-Authors: Tomoko Mabuchi, Toshifumi Wakamatsu, Tomoyoshi Nakadai, Miho Shimada, Kazuhiko Yamada, Yoichi Matsuda, Taka-aki TamuraAbstract:Abstract Transcription Factor IIA (TFIIA) is one of the general Transcription Factors for RNA polymerase II and composed of three subunits, TFIIAα, TFIIAβ and TFIIAγ. TFIIAα and TFIIAβ are encoded by a single gene ( TFIIA αβ) and mature through internal cleavage of TFIIAαβ. In this study, we found that structures of TFIIAαβ and TFIIAγ are highly homologous with each mammalian counterpart. Exon–intron organizations of the human and chicken TFIIA genes were also homologous. The sequence of the cleavage region of the chicken TFIIAαβ precursor protein was fitted to the consensus cleavage recognition site. It was thus demonstrated that TFIIA is conserved in vertebrates. TFIIA proteins are present ubiquitously in chicken tissues. Fluorescent in situ hybridization revealed that TFIIA αβ and TFIIA γ genes are located in chromosome 5 and a mini-chromosome, respectively. We generated semi-knockout chicken DT40 cells for TFIIA αβ and TFIIA γ genes with high homologous recombination efficiencies, whereas we failed to establish double-knockout cells for each gene. It is thought that both genes for TFIIA are required in vertebrates. TFIIA siRNA resulted in deceleration of cell growth rate, suggesting that, consistent with those of knockout assays, TFIIA is associated with cell growth regulation.
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Chromosomal position, structure, expression, and requirement of genes for chicken Transcription Factor IIA.
Gene, 2007Co-Authors: Tomoko Mabuchi, Toshifumi Wakamatsu, Tomoyoshi Nakadai, Miho Shimada, Kazuhiko Yamada, Yoichi Matsuda, Taka-aki TamuraAbstract:Transcription Factor IIA (TFIIA) is one of the general Transcription Factors for RNA polymerase II and composed of three subunits, TFIIAalpha, TFIIAbeta and TFIIAgamma. TFIIAalpha and TFIIAbeta are encoded by a single gene (TFIIAalphabeta) and mature through internal cleavage of TFIIAalphabeta. In this study, we found that structures of TFIIAalphabeta and TFIIAgamma are highly homologous with each mammalian counterpart. Exon-intron organizations of the human and chicken TFIIA genes were also homologous. The sequence of the cleavage region of the chicken TFIIAalphabeta precursor protein was fitted to the consensus cleavage recognition site. It was thus demonstrated that TFIIA is conserved in vertebrates. TFIIA proteins are present ubiquitously in chicken tissues. Fluorescent in situ hybridization revealed that TFIIAalphabeta and TFIIAgamma genes are located in chromosome 5 and a mini-chromosome, respectively. We generated semi-knockout chicken DT40 cells for TFIIAalphabeta and TFIIAgamma genes with high homologous recombination efficiencies, whereas we failed to establish double-knockout cells for each gene. It is thought that both genes for TFIIA are required in vertebrates. TFIIA siRNA resulted in deceleration of cell growth rate, suggesting that, consistent with those of knockout assays, TFIIA is associated with cell growth regulation.
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Specific Interaction with Transcription Factor IIA and Localization of the Mammalian TATA-binding Protein-like Protein (TLP/TRF2/TLF)
Journal of Biological Chemistry, 2003Co-Authors: Tomoyoshi Nakadai, Miho Shimada, Daisuke Shima, Hiroshi Handa, Taka-aki TamuraAbstract:Abstract TBP-like protein (TLP) is structurally similar to the TATA-binding protein (TBP) and is thought to have a Transcriptional regulation function. Although TLP has been found to form a complex with Transcription Factor IIA (TFIIA), the in vivo functions of TFIIA for TLP are not clear. In this study, we analyzed the interaction between TLP and TFIIA. We determined the biophysical properties for the interaction of TLP with TFIIA. Dissociation constants of TFIIA versus TLP and TFIIA versus TBP were 1.5 and 10 nm, respectively. Moreover, the dissociation rate constant of TLP and TFIIA (1.2 × 10–4/m·s was significantly lower than that of TBP (2.1 × 10–3/m·s). These results indicate that TLP has a higher affinity to TFIIA than does TBP and that the TLP-TFIIA complex is much more stable than is the TBP-TFIIA complex. We found that TLP forms a dimer and a trimer and that these multimerizations are inhibited by TFIIA. Moreover, TLP mutimers were more stable than a TBP dimer. We determined the amounts of TLPs in the nucleus and cytoplasm of NIH3T3 cells and found that the molecular number of TLP in the nucleus was only 4% of that in the cytoplasm. Immunostaining of cells also revealed cytoplasmic localization of TLP. We established cells that stably express mutant TLP lacking TFIIA binding ability and identified the amino acids of TLP required for TFIIA binding (Ala-32, Leu-33, Asn-37, Arg-52, Lys-53, Lys-78, and Arg-86). Interestingly, the level of TFIIA binding defective mutant TLPs in the nucleus was much higher than that of the wild-type TLP and TFIIA-interactable mutant TLPs. Immunostaining analyses showed consistent results. These results suggest that the TFIIA binding ability of TLP is required for characteristic cytoplasmic localization of TLP. TFIIA may regulate the intracellular molecular state and the function of TLP through its property of binding to TLP.
Julius Brennecke - One of the best experts on this subject based on the ideXlab platform.
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A heterochromatin-dependent Transcription machinery drives piRNA expression
Nature, 2017Co-Authors: Peter Refsing Andersen, Laszlo Tirian, Milica Vunjak, Julius BrenneckeAbstract:Transcription of Drosophila PIWI-interacting RNA (piRNA) clusters is enforced through RNA polymerase II pre-initiation complex formation within repressive heterochromatin, accomplished through the Transcription Factor IIA subunit paralogue Moonshiner. Nuclear small RNA pathways safeguard genome integrity by establishing Transcription-repressing heterochromatin at transposable elements. This inevitably also targets the transposon-rich source loci of the small RNAs themselves. How small RNA source loci are efficiently transcribed while transposon promoters are potently silenced is not understood. Here we show that, in Drosophila , Transcription of PIWI-interacting RNA (piRNA) clusters—small RNA source loci in animal gonads—is enforced through RNA polymerase II pre-initiation complex formation within repressive heterochromatin. This is accomplished through Moonshiner, a paralogue of a basal Transcription Factor IIA (TFIIA) subunit, which is recruited to piRNA clusters via the heterochromatin protein-1 variant Rhino. Moonshiner triggers Transcription initiation within piRNA clusters by recruiting the TATA-box binding protein (TBP)-related Factor TRF2, an animal TFIID core variant. Thus, Transcription of heterochromatic small RNA source loci relies on direct recruitment of the core Transcriptional machinery to DNA via histone marks rather than sequence motifs, a concept that we argue is a recurring theme in evolution. The PIWI-interacting RNA (piRNA) pathway is important for genome stability in the germline by establishing repressive heterochromatin at transposons. How piRNAs are transcribed from their loci within transposons that are Transcriptionally silenced is not understood. Here Julius Brennecke and colleagues show that Transcription initiation of Drosophila piRNA precursors involves a germline-specific TFIIA-L paralogue which they name Moonshiner. This protein is recruited to piRNA clusters in heterochromatin via an HP1 paralogue, Rhino, and couples to the core RNA polymerase II Transcription machinery. Moonshiner therefore enables active piRNA Transcription in a repressive heterochromatin environment.
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A heterochromatin-dependent Transcription machinery drives piRNA expression
Nature, 2017Co-Authors: Peter Refsing Andersen, Laszlo Tirian, Milica Vunjak, Julius BrenneckeAbstract:Nuclear small RNA pathways safeguard genome integrity by establishing Transcription-repressing heterochromatin at transposable elements. This inevitably also targets the transposon-rich source loci of the small RNAs themselves. How small RNA source loci are efficiently transcribed while transposon promoters are potently silenced is not understood. Here we show that, in Drosophila, Transcription of PIWI-interacting RNA (piRNA) clusters-small RNA source loci in animal gonads-is enforced through RNA polymerase II pre-initiation complex formation within repressive heterochromatin. This is accomplished through Moonshiner, a paralogue of a basal Transcription Factor IIA (TFIIA) subunit, which is recruited to piRNA clusters via the heterochromatin protein-1 variant Rhino. Moonshiner triggers Transcription initiation within piRNA clusters by recruiting the TATA-box binding protein (TBP)-related Factor TRF2, an animal TFIID core variant. Thus, Transcription of heterochromatic small RNA source loci relies on direct recruitment of the core Transcriptional machinery to DNA via histone marks rather than sequence motifs, a concept that we argue is a recurring theme in evolution.
Timothy J. Richmond - One of the best experts on this subject based on the ideXlab platform.
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Crystal structure of a yeast TFIIA/TBP/DNA complex
Nature, 1996Co-Authors: Song Tan, Yvonne Hunziker, David F. Sargent, Timothy J. RichmondAbstract:The X-ray crystal structure of the Transcription Factor IIA (TFIIA)in complex with the TATA-box-binding protein (TBP) and TATA-element DNA is presented at 2.5 Å resolution. TFIIA is composed of a β-barrel and a four-helix bundle motif that together have a boot-like appearance. The β-barrel extends the TBP β-sheet and bridges over the DNA major groove immediately upstream of the TATA box. The four-helix bundle contributes substantially to the surface of the complex available for interaction with additional Transcription Factors.
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Crystal structure of a yeast TFIIA/TBP/DNA complex.
Nature, 1996Co-Authors: Song Tan, Yvonne Hunziker, David F. Sargent, Timothy J. RichmondAbstract:The X-ray crystal structure of the Transcription Factor IIA (TFIIA) in complex with the TATA-box-binding protein (TBP) and TATA-element DNA is presented at 2.5 A resolution. TFIIA is composed of a beta-barrel and a four-helix bundle motif that together have a boot-like appearance. The beta-barrel extends the TBP beta-sheet and bridges over the DNA major groove immediately upstream of the TATA box. The four-helix bundle contributes substantially to the surface of the complex available for interaction with additional Transcription Factors.