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General transcription factor IIIC, polypeptide 1, alpha 220kDa

Top mentioned proteins: POLYMERASE, IRF, CAN, TBP, V1a
Papers on TFIIIC
PRC2 regulates RNA polymerase III transcribed non-translated RNA gene transcription through EZH2 and SUZ12 interaction with TFIIIC complex.
Zhang et al., Beijing, China. In Nucleic Acids Res, Aug 2015
Here we present a paradigm that EZH2 is involved in the repression of Pol III transcription via interaction with transcriptional factor complex IIIC (TFIIIC).
Argonaute 2 Binds Directly to tRNA Genes and Promotes Gene Repression in cis.
Giles et al., In Mol Cell Biol, Jul 2015
AGO2 chromatin binding was not observed at non-TFIIIC-dependent RNA polymerase III (Pol III) genes or at extra-TFIIIC (ETC) sites, indicating that the interaction is specific for TFIIIC-dependent Pol III genes.
Intrinsic Toxicity of Unchecked Heterochromatin Spread Is Suppressed by Redundant Chromatin Boundary Functions in Schizosacchromyces pombe.
Madhani et al., San Francisco, United States. In G3 (bethesda), Jul 2015
In the fission yeast Schizosacchromyces pombe, two factors/elements required for boundary function have been described, the jmjC protein Epe1 and binding sites for the RNA polymerase III transcription factor TFIIIC.
Biochemical analysis of transcription termination by RNA polymerase III from yeast Saccharomyces cerevisiae.
Maraia et al., Bethesda, United States. In Methods Mol Biol, 2014
Only two transcription factor complexes, TFIIIB and TFIIIC, are required to faithfully initiate and direct multiple rounds of transcription by pol III.
Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly.
Müller et al., Heidelberg, Germany. In Nat Commun, 2014
TFIIIC has been described as a conserved, multi-subunit protein complex composed of two subcomplexes, called τA and τB.
TFIIIC bound DNA elements in nuclear organization and insulation.
Kamakaka et al., Santa Cruz, United States. In Biochim Biophys Acta, 2013
tDNAs also play a role in genome organization by clustering at sites in the nucleus and both of these functions are dependent on the transcription factor TFIIIC.
RNA polymerase III transcription - regulated by chromatin structure and regulator of nuclear chromatin organization.
Teichmann et al., Pessac, France. In Subcell Biochem, 2012
In yeast, the ability of the Pol III transcription system to contribute to nuclear organization seems to be dependent on direct interactions of Pol III genes and/or its transcription factors TFIIIC and TFIIIB with the structural maintenance of chromatin (SMC) protein-containing complexes cohesin and condensin.
tDNA insulators and the emerging role of TFIIIC in genome organization.
Corces et al., Atlanta, United States. In Transcription, 2012
TFIIIC, a transcription factor that interacts with the B-box in tDNAs as well as thousands of ETC sites in the genome, is responsible for insulator function.
Extra-transcriptional functions of RNA Polymerase III complexes: TFIIIC as a potential global chromatin bookmark.
Donze, Baton Rouge, United States. In Gene, 2012
Pol III transcription at tRNA genes (tDNAs) requires the binding of two transcription factor complexes, TFIIIC and TFIIIB.
RNA polymerase III transcription control elements: themes and variations.
Dieci et al., Parma, Italy. In Gene, 2012
The highly selective, efficient and localized action of Pol III at its minute genomic targets is made possible by a handful of cis-acting regulatory elements, located within the transcribed region (where they are bound by the multisubunit assembly factor TFIIIC) and/or upstream of the transcription start site.
mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1.
White et al., Glasgow, United Kingdom. In Proc Natl Acad Sci U S A, 2010
Maf1, a repressor that binds and inhibits pol III, is phosphorylated in a mTOR-dependent manner both in vitro and in vivo at serine 75, a site that contributes to its function as a transcriptional inhibitor.
Different functional modes of p300 in activation of RNA polymerase III transcription from chromatin templates.
Roeder et al., New York City, United States. In Mol Cell Biol, 2008
Results identify TFIIIC as a recruitment factor for p300 and thus may have important implications for the emerging concept that tRNA genes or TFIIIC binding sites act as chromatin barriers to prohibit spreading of silenced heterochromatin domains.
Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC.
Teichmann et al., Pessac, France. In J Biol Chem, 2007
TFIIIC is composed of six subunits, five of which are conserved in humans. We report the identification, molecular cloning, and characterization of the sixth subunit of human TFIIIC, TFIIIC35
A role for TFIIIC transcription factor complex in genome organization.
Grewal et al., Bethesda, United States. In Cell, 2006
We show that inverted repeat (IR) boundary elements flanking the fission yeast mating-type heterochromatin domain contain B-box sequences, which prevent heterochromatin from spreading into neighboring euchromatic regions by recruiting transcription factor TFIIIC complex without RNA polymerase III (Pol III).
TFIIIC boxes in the genome.
Geyer et al., Iowa City, United States. In Cell, 2006
In this issue of Cell, Noma et al. (2006) show that B-boxes and TFIIIC limit the spread of heterochromatin at the silent mat region in the fission yeast genome.
The activity of transcription factor IIIC1 is impaired during differentiation of F9 cells.
Seifart et al., Marburg an der Lahn, Germany. In J Biol Chem, 2002
The partial purification of pol III transcription factors from PE and EC cells revealed that TFIIIC2 activity could be purified from both cell types, whereas TFIIIC1 activity was dramatically reduced in extracts from PE cells.
Facilitated recycling pathway for RNA polymerase III.
Sentenac et al., Gif-sur-Yvette, France. In Cell, 1996
Kinetic analysis shows that RNA polymerase recycling on preassembled tDNA.TFIIIC.TFIIIB complexes is much faster than the initial transcription cycle.
Requirement of RNA polymerase III transcription factors for in vitro position-specific integration of a retroviruslike element.
Sandmeyer et al., Irvine, United States. In Science, 1995
Integration was position-specific and required Ty3 integrase, Pol III transcription factor (TF) IIIB-, TFIIIC-, and Pol III-containing fractions showed that TFIIIB and TFIIIC, together, were sufficient for position-specific Ty3 integration, but not for transcription.
TFIIIC relieves repression of U6 snRNA transcription by chromatin.
Sentenac et al., Gif-sur-Yvette, France. In Nature, 1993
Here we report that, after nucleosome reconstitution or chromatin assembly, U6 snRNA synthesis becomes dependent on TFIIIC and on the integrity of the B-block element.
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