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General transcription factor IIA, 2, 12kDa

Accurate transcription initiation on TATA-containing class II genes involves the ordered assembly of RNA polymerase II (POLR2A; MIM 180660) and the general initiation factors TFIIA, TFIIB (MIM 189963), TFIID (MIM 313650), TFIIE (MIM 189962), TFIIF (MIM 189968), TFIIG/TFIIJ, and TFIIH (MIM 189972). The first step involves recognition of the TATA element by the TATA-binding subunit (TBP; MIM 600075) and may be regulated by TFIIA, a factor that interacts with both TBP and a TBP-associated factor (TAF; MIM 600475) in TFIID. TFIIA has 2 subunits (43 and 12 kD) in yeast and 3 subunits in higher eukaryotes. In HeLa extracts, it consists of a 35-kD alpha subunit and a 19-kD beta subunit encoded by the N- and C-terminal regions of GTF2A1 (MIM 600520), respectively, and a 12-kD gamma subunit encoded by GTF2A2 (DeJong et al., 1995 [PubMed 7724559]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: TBP, POLYMERASE, CAN, IIa, STEP
Papers on TFIIA
Full trans-activation mediated by the immediate-early protein of equine herpesvirus 1 requires a consensus TATA box, but not its cognate binding sequence.
O'Callaghan et al., Shreveport, United States. In Virus Res, Feb 2016
Our data showed that the IEP directly interacted with transcription factor TFIIA, which is known to stabilize the binding of TBP and TFIID to the TATA box of core promoters.
TBP-like protein (TLP) interferes with Taspase1-mediated processing of TFIIA and represses TATA box gene expression.
Tamura et al., Chiba, Japan. In Nucleic Acids Res, Aug 2015
TBP-TFIIA interaction is involved in the potentiation of TATA box-driven promoters.
Unraveling the Activation Mechanism of Taspase1 which Controls the Oncogenic AF4-MLL Fusion Protein.
Marschalek et al., Frankfurt am Main, Germany. In Ebiomedicine, May 2015
The active enzyme cleaves only very few target proteins, e.g., MLL, MLL4 and TFIIA at their corresponding consensus cleavage sites (CSTasp1) as well as AF4-MLL in the case of leukemogenic translocation.
Taspase1 processing alters TFIIA cofactor properties in the regulation of TFIID.
Oelgeschläger et al., United Kingdom. In Transcription, 2014
TFIIA is an important positive regulator of TFIID, the primary promoter recognition factor of the basal RNA polymerase II transcription machinery.
Molecular Cloning of a cDNA Encoding for Taenia solium TATA-Box Binding Protein 1 (TsTBP1) and Study of Its Interactions with the TATA-Box of Actin 5 and Typical 2-Cys Peroxiredoxin Genes.
Landa et al., Mexico. In Plos One, 2014
In contrast, the TsTBP1 COOH-terminal domain is highly conserved among organisms, and contains the amino acids involved in interactions with the TATA-box, as well as with TFIIA and TFIIB.
More pieces to the puzzle: recent structural insights into class II transcription initiation.
Berger et al., Grenoble, France. In Curr Opin Struct Biol, 2014
Class II transcription initiation is a highly regulated process and requires the assembly of a pre-initiation complex (PIC) containing DNA template, RNA polymerase II (RNAPII), general transcription factors (GTFs) TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIH and Mediator.
The Mediator complex and transcription regulation.
Taatjes et al., Boulder, United States. In Crit Rev Biochem Mol Biol, 2013
Mediator and pol II function within the pre-initiation complex (PIC), which consists of Mediator, pol II, TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH and is approximately 4.0 MDa in size.
Structural visualization of key steps in human transcription initiation.
Nogales et al., Berkeley, United States. In Nature, 2013
Here we have used an in vitro reconstituted system to study the stepwise assembly of human TBP, TFIIA, TFIIB, Pol II, TFIIF, TFIIE and TFIIH onto promoter DNA using cryo-electron microscopy.
Human TFIID binds to core promoter DNA in a reorganized structural state.
Nogales et al., Berkeley, United States. In Cell, 2013
This analysis revealed that TFIID coexists in two predominant and distinct structural states that differ by a 100 Å translocation of TFIID's lobe A. The transition between these structural states is modulated by TFIIA, as the presence of TFIIA and promoter DNA facilitates the formation of a rearranged state of TFIID that enables promoter recognition and binding.
Genome-wide structure and organization of eukaryotic pre-initiation complexes.
Pugh et al., United States. In Nature, 2012
PICs, including RNA polymerase II and protein complexes TFIIA, TFIIB, TFIID (or TBP), TFIIE, TFIIF, TFIIH and TFIIK were positioned within promoters and excluded from coding regions.
New insights into the function of transcription factor TFIID from recent structural studies.
Schultz et al., Illkirch-Graffenstaden, France. In Curr Opin Genet Dev, 2011
The structural analysis of functional transcription complexes formed by TFIID, TFIIA, activators and/or promoter DNA illuminates the faculty of TFIID to adjust to various promoter architectures and highlights its role as a platform for preinitiation complex assembly.
TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation.
Schultz et al., Illkirch-Graffenstaden, France. In Nature, 2010
Transcription of eukaryotic messenger RNA (mRNA) encoding genes by RNA polymerase II (Pol II) is triggered by the binding of transactivating proteins to enhancer DNA, which stimulates the recruitment of general transcription factors (TFIIA, B, D, E, F, H) and Pol II on the cis-linked promoter, leading to pre-initiation complex formation and transcription.
Identification of candidate epigenetic biomarkers for ovarian cancer detection.
Lin et al., Columbus, United States. In Oncol Rep, 2009
GTF2A1 alone, or GTF2A1 plus HAAO are excellent candidate biomarkers for detecting Ovarian cancer
Specific variants of general transcription factors regulate germ cell development in diverse organisms.
Freiman, Providence, United States. In Biochim Biophys Acta, 2009
One surprising germ cell development mechanism utilizes variation of the global transcriptional machinery, such as TFIID and TFIIA.
TFIIA changes the conformation of the DNA in TBP/TATA complexes and increases their kinetic stability.
Goodrich et al., Boulder, United States. In J Mol Biol, 2007
TFIIA induces a conformational change within the TBP/TATA complex that enhances its stability under both in vitro and physiological salt conditions.
A facelift for the general transcription factor TFIIA.
Stunnenberg et al., Nijmegen, Netherlands. In Biochim Biophys Acta, 2007
TFIIA was classified as a general transcription factor when it was first identified.
Uncleaved TFIIA is a substrate for taspase 1 and active in transcription.
Stunnenberg et al., Nijmegen, Netherlands. In Mol Cell Biol, 2006
Transfected taspase 1 enhances cleavage of TFIIA, and RNA interference knockdown of endogenous taspase 1 diminishes cleavage of TFIIA in vivo.
Specific interaction with transcription factor IIA and localization of the mammalian TATA-binding protein-like protein (TLP/TRF2/TLF).
Tamura et al., Chiba, Japan. In J Biol Chem, 2004
transcription factor IIA may regulate the intracellular molecular state and the function of TATA-binding protein-like protein (TLP) through its property of binding to TLP
Novel interactions between the components of human and yeast TFIIA/TBP/DNA complexes.
Richmond et al., Zürich, Switzerland. In J Mol Biol, 2003
Results present the X-ray structures of human and yeast TATA box-binding protein /transcription factor IIA/DNA complexes at 2.1A and 1.9A resolution, respectively
A transcription reinitiation intermediate that is stabilized by activator.
Hahn et al., Seattle, United States. In Nature, 2000
Here we describe the isolation of a reinitiation intermediate that includes transcription factors TFIID, TFIIA, TFIIH, TFIIE and Mediator.
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