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MED7 Med7p

Med7, CRSP9
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. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, Srb7, L-6, CAN, MED6
Papers on Med7
A functional portrait of Med7 and the mediator complex in Candida albicans.
Whiteway et al., Montréal, Canada. In Plos Genet, 2014
Intriguingly, while the Med4, 8, 10, 11, 14, 17, 21 and 22 subunits were essential in both fungi, the structurally highly conserved Med7 subunit was apparently non-essential in C. albicans.
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.
Model of the Mediator middle module based on protein cross-linking.
Cramer et al., Victoria, Canada. In Nucleic Acids Res, 2013
The model contains a central tetramer formed by the heterodimers Med4/Med9 and Med7/Med21.
Role of Mediator in regulating Pol II elongation and nucleosome displacement in Saccharomyces cerevisiae.
Gross et al., Shreveport, United States. In Genetics, 2012
We find that ewe (expression without heat shock element) mutations in conserved Mediator subunits Med7, Med14, Med19, and Med21-all located within or adjacent to the middle module-severely diminish heat-shock-induced expression of the Hsf1-regulated HSP82 gene.
MC EMiNEM maps the interaction landscape of the Mediator.
Tresch et al., München, Germany. In Plos Comput Biol, 2011
We identify the N-terminus of Med7 as a peripheral entity, entailing only local structural changes upon perturbation, while the C-terminus of Med7 and Med19 appear to play a central role.
Genome-wide profiling of pluripotent cells reveals a unique molecular signature of human embryonic germ cells.
Kerr et al., Baltimore, United States. In Plos One, 2011
These include IPO7, MED7, RBM26, HSPD1, and KRAS which were upregulated in EGCs along with other pluripotent stem cells when compared to PGCs.
Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization.
Cramer et al., München, Germany. In Nucleic Acids Res, 2011
The bundle domain fold is also present in the Mediator middle module subcomplex Med7/21 and is predicted in the Mediator heterodimers Med2/3, Med4/9, Med10/14 and Med28/30.
Mediator influences telomeric silencing and cellular life span.
Gustafsson et al., Göteborg, Sweden. In Mol Cell Biol, 2011
Loss of the Mediator Med5 subunit or mutations in Med7 cause a depletion of the complex from regions located near subtelomeric X elements, which leads to a change in the balance between the Sir2 and Sas2 proteins.
Preparation and topology of the Mediator middle module.
Cramer et al., München, Germany. In Nucleic Acids Res, 2010
Protein-protein interaction assays combined with previously published data suggest that the Med7 and Med4 subunits serve as a binding platform to form the three heterodimeric subcomplexes, Med7N/21, Med7C/31 and Med4/9.
Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation.
Niedenthal et al., Hannover, Germany. In Nucleic Acids Res, 2009
When FKBP fusion proteins of STAT1, p53, CRSP9, FOS, CSNK2B, HES1, TCF21 and MYF6 are coexpressed with Ubc9-FRB, treatment of HEK293 cells with the rapamycin-related dimerizer compound AP21967 induces SUMOylation of these proteins in vivo.
Identification, structure, and functional requirement of the Mediator submodule Med7N/31.
Cramer et al., München, Germany. In Embo J, 2009
Here, we show that the middle module of the Mediator core contains a submodule of unique structure and function that comprises the N-terminal part of subunit Med7 (Med7N) and the highly conserved subunit Med31 (Soh1).
Saccharomyces cerevisiae Med9 comprises two functionally distinct domains that play different roles in transcriptional regulation.
Kokubo et al., Yokohama, Japan. In Genes Cells, 2009
In contrast, the well-conserved carboxy-terminal half (aa 64-149) has a more fundamental function involved in direct binding to the amino-terminal portions of Med4 and Med7 and the assembly of Med9 into the Middle module.
Malleable machines in transcription regulation: the mediator complex.
Fuxreiter et al., Budapest, Hungary. In Plos Comput Biol, 2008
In Saccharomyces cerevisiae, the functional roles of 11 MoRFs have been experimentally verified, and those in the Med8/Med18/Med20 and Med7/Med21 complexes were structurally confirmed.
Isolation of dieldrin- and endrin-degrading bacteria using 1,2-epoxycyclohexane as a structural analog of both compounds.
Oyaizu et al., Hachiōji, Japan. In Appl Microbiol Biotechnol, 2008
strain MED-7 and Cupriavidus sp.
The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1.
Tjian et al., Berkeley, United States. In Nature, 1999
Cloning of genes encoding CRSP subunits reveals that CRSP33 is a homologue of the yeast mediator subunit Med7, whereas CRSP150 contains a domain conserved in yeast mediator subunit Rgr1.
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