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TAF11 RNA polymerase II, TATA box binding protein

Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes a small subunit of TFIID that is present in all TFIID complexes and interacts with TBP. This subunit also interacts with another small subunit, TAF13, to form a heterodimer with a structure similar to the histone core structure. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: TBP, TAF, POLYMERASE, CAN, Histone
Papers on TAFII
[Classification and therapeutic strategy for chronic tonsillitis].
Pal'chun, In Vestn Otorinolaringol, 2012
simple and toxico-allergic (TAF) CT, the latter being subdivided into two variants differing in the character of manifestations (TAF-1 and TAF-II).
[Conservative therapy and surgical treatment of chronic tonsillitis in the children].
Tovmasian et al., In Vestn Otorinolaringol, 2012
At the same time, the number of such patients undergoing surgery for the treatment of toxico-allergic forms (TAF-I and TAF-II) decreased from 26.7 to 8.7-11.6% of their total number admitted to the department for the treatment of pharyngeal pathology.
Involvement of template-activating factor I/SET in transcription of adenovirus early genes as a positive-acting factor.
Nagata et al., Tsukuba, Japan. In J Virol, 2006
We identified host acidic proteins, template-activating factor I (TAF-I), TAF-II, and TAF-III as stimulatory factors for replication from the adenovirus DNA-protein VII complex.
Isolation and identification of a new thymic peptide from calf thymus.
He et al., Beijing, China. In Biochemistry (mosc), 2004
We isolated a new peptide from calf thymus and named it thymus activity factor II (TAF-II).
Role of TAFII-17, a VDR binding protein, in the increased osteoclast formation in Paget's Disease.
Roodman et al., Pittsburgh, United States. In J Bone Miner Res, 2004
Using a GST-VDR chimeric protein, we identified TAFII-17 as VDR binding protein expressed by pagetic OCL precursors and MVNP transduced normal OCL precursors.
The TBN protein, which is essential for early embryonic mouse development, is an inducible TAFII implicated in adipogenesis.
Roeder et al., New York City, United States. In Mol Cell, 2003
Human TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (hTAFs) that have been shown to play important roles, within TFIID, both in core promoter recognition and as coactivators.
A role of the TATA box and the general co-activator hTAF(II)130/135 in promoter-specific trans-activation by simian virus 40 small t antigen.
Moens et al., Tromsø, Norway. In J Gen Virol, 2003
Overexpressing the general transcription factor hTAF(II)130/135, but not hTAF(II)28 or hTAF(II)80, stimulated the activity of promoters in a consensus TATA box-dependent mode.
Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis.
Van Dorsselaer et al., Strasbourg, France. In Proteomics, 2003
Initiation of transcription of protein-encoding genes by RNA polymerase II was thought to require the transcription factor II D (TF(II)D), a complex comprising the TATA binding protein (TBP) and TBP-associated factors.
NF-Y recruitment of TFIID, multiple interactions with histone fold TAF(II)s.
Mantovani et al., Modena, Italy. In J Biol Chem, 2002
hTAF(II)20, hTAF(II)28, and hTAF(II)18-hTAF(II)28 bind to the NF-Y B-NF-YC histone fold dimer; hTAF(II)80 and hTAF(II)31-hTAF(II)80 interact with the trimer but not with the NF-YB-NF-YC dimer.
IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff.
Levy et al., New York City, United States. In Nat Cell Biol, 2002
The TFIID component TAF(II)130 potentiates STAT2 function, but TAF(II)28 or the HAT activity of TAF(II)250 do not, and transcriptional induction can proceed independently of the TATA-binding protein, TBP.
Requirement of tissue-selective TBP-associated factor TAFII105 in ovarian development.
Tjian et al., Berkeley, United States. In Science, 2001
Transcription factor TFIID, composed of TBP and TAFII subunits, is a central component of the RNA polymerase II machinery.
Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC.
Schultz et al., Strasbourg, France. In Science, 2000
TBP (TATA-binding protein)-associated factors (TAF(II)s) are components of large multiprotein complexes such as TFIID, TFTC, STAGA, PCAF/GCN5, and SAGA, which play a key role in the regulation of gene expression by RNA polymerase II.
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
Moras et al., Strasbourg, France. In Cell, 1998
The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences.
Functional and structural analysis of the subunits of human transcription factor TFIID.
Moras et al., Strasbourg, France. In Cold Spring Harb Symp Quant Biol, 1997
The past few years have brought many new insights concerning the structure and function of TAFII proteins.
Human TAFII 105 is a cell type-specific TFIID subunit related to hTAFII130.
Tjian et al., Berkeley, United States. In Cell, 1996
We previously characterized Drosophila and human TAF subunits that make up the core TFIID complex found in all cells.
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