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Mediator complex subunit 26

The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, CAN, TBP, TFIIS, SET
Papers on CRSP70
MED26 regulates the transcription of snRNA genes through the recruitment of little elongation complex.
Hatakeyama et al., Sapporo, Japan. In Nat Commun, 2014
Here we show that the human Mediator subunit MED26 plays a role in the recruitment of LEC to a subset of snRNA genes through direct interaction of EAF and the N-terminal domain (NTD) of MED26.
Reconstitution of active human core Mediator complex reveals a critical role of the MED14 subunit.
Roeder et al., New York City, United States. In Nat Struct Mol Biol, 2014
We further establish a conditional requirement for metazoan-specific MED26 that becomes evident in the presence of heterologous nuclear factors.
Characterization of the influence of mediator complex in HIV-1 transcription.
Esté et al., Badalona, Spain. In J Biol Chem, 2014
Knockdown of 9 out of 28 human MED proteins significantly impaired viral replication without affecting cell viability, including MED6, MED7, MED11, MED14, MED21, MED26, MED27, MED28, and MED30.
The metazoan-specific mediator subunit 26 (Med26) is essential for viability and is found at both active genes and pericentric heterochromatin in Drosophila melanogaster.
Marr et al., In Mol Cell Biol, 2014
Human MED26 was originally purified in the cofactor required for the Sp1 activation complex (CRSP) as a 70-kDa component named CRSP70.
Regulation of MYC expression and differential JQ1 sensitivity in cancer cells.
Roy et al., Boston, United States. In Plos One, 2013
Molecularly, these differences appear due to requirements of Brd4, the most active version of the Positive Transcription Elongation Factor B (P-TEFb) within the Super Elongation Complex (SEC), and transcription factors such as Gdown1, and MED26 and also other unknown cell specific factors.
Adenovirus L-E1A activates transcription through mediator complex-dependent recruitment of the super elongation complex.
Chinnadurai et al., Saint Louis, United States. In J Virol, 2013
In addition to MED23, mediator subunits such as MED14 and MED26 were also essential for the transcription of HAdv5 early genes.
Temporal association of herpes simplex virus ICP4 with cellular complexes functioning at multiple steps in PolII transcription.
DeLuca et al., Pittsburgh, United States. In Plos One, 2012
The form of Mediator copurifying with ICP4 was enriched for the kinase domain and also lacked the activator-specific component, Med26, suggesting that Mediator-ICP4 interactions may be involved in repression of viral transcription.
The Mediator complex in plants: structure, phylogeny, and expression profiling of representative genes in a dicot (Arabidopsis) and a monocot (rice) during reproduction and abiotic stress.
Tyagi et al., New Delhi, India. In Plant Physiol, 2011
Using Hidden Markov Model-based conserved motif searches, we have identified all the known yeast/metazoan Med components in one or more plant groups, including the Med26 subunits, which have not been reported so far for any plant species.
Human mediator subunit MED26 functions as a docking site for transcription elongation factors.
Conaway et al., Kansas City, United States. In Cell, 2011
MED26 can function as a molecular switch that interacts first with TFIID in the Pol II initiation complex and then exchanges TFIID for complexes containing ELL/EAF and P-TEFb to facilitate transition of Pol II into the elongation stage of transcription.
The TFIIS and TFIIS-like genes from Medicago truncatula are involved in oxidative stress response.
Carbonera et al., Pavia, Italy. In Gene, 2011
The N-terminal region of the MtTFIIS-like protein includes a LW motif, characterized by highly conserved leucine (L) and tryptophan (W) residues, also found in the canonical TFIIS protein, elongin A (transcription elongation factor S-III) and CRSP70 (cofactor required for Sp1 activation), while a proline-rich region is present in the C-terminal domain.
The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26.
Romier et al., Illkirch-Graffenstaden, France. In Embo J, 2011
Importantly, the ARM subdomain of Iws1 is conserved in several transcription factors, including TFIIS, Elongin A and Med26.
MED19 and MED26 are synergistic functional targets of the RE1 silencing transcription factor in epigenetic silencing of neuronal gene expression.
Boyer et al., San Antonio, United States. In J Biol Chem, 2009
findings identify MED19/MED26 as a probable composite REST interface in Mediator and further clarify the mechanistic basis by which Mediator facilitates REST-imposed epigenetic restrictions on neuronal gene expression
Characterization of transcription from TATA-less promoters: identification of a new core promoter element XCPE2 and analysis of factor requirements.
Takada et al., Houston, United States. In Plos One, 2008
Our results show that XCPE2-driven transcription uses at least TFIIB, either TFIID or free TBP, RNA polymerase II (RNA pol II) and the MED26-containing mediator complex but not Gcn5.
Enhancement of gene expression by a peptide p(CHWPR) produced by Bifidobacterium lactis BB-12.
Hirano et al., Niigata, Japan. In Microbiol Immunol, 2008
Furthermore, we found that p(CHWPR) also bound to a transcriptional avtivation subunit, CRSP70; this suggests that p(CHWPR), RORgamma, and CRSP70 in combination enhance transcription activity.
Human CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformation.
Tjian et al., United States. In Genes Dev, 2002
Human CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformation
The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1.
Tjian et al., Berkeley, United States. In Nature, 1999
CRSPs 34, 77 and 130 are new proteins, but the amino terminus of CRSP70 is homologous to elongation factor TFIIS. Immunodepletion studies confirm that these subunits have an essential cofactor function.
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