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RPO21 Rpo21p

Rpb1, RNA polymerase II subunit, RPO21, POLR2A
This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, RPB2, CAN, ACID, HAD
Papers using Rpb1 antibodies
p38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation. Participation of the Mef2c transcription factor
Supplier
Dilworth Francis Jeffrey et al., In The EMBO Journal, 1998
... antibody (Millipore 06-755), Myog (Santa Cruz SC-576), Suz12 (Abcam ab12073), Mef2 (Santa Cruz sc-17785, sc-13917), RPB1 (Abcam ab5408), and Ezh2 (Zymed ...
Papers on Rpb1
TP53 Loss Creates Susceptibility to Anti-Pol II Therapy in Colorectal Cancer.
New
In Cancer Discov, 07 Jun 2015
UNASSIGNED: TP53 loss coincides with hemizygous POLR2A deletion, sensitizing cells to POLR2A inhibition.
TP53 loss creates therapeutic vulnerability in colorectal cancer.
New
Impact
Lu et al., Houston, United States. In Nature, 30 May 2015
POLR2A is identified as such a gene that is almost always co-deleted with TP53 in human cancers.
Abnormal expression of RNA polymerase II associated proteins in muscle of patients with myofibrillar myopathies.
New
Vattemi et al., Verona, Italy. In Histopathology, 17 May 2015
Our data demonstrated that RPAP2, and to a lesser extent GPN1/RPAP4, are focally accumulated in the cytoplasm of MFMs muscle fibers in which they colocalize with POLR2A/RPB1, the largest subunit of RNAPII, and correspond to αB-cystallin deposits in distribution and staining intensity.
Systematics of the Cosmospora viliuscula species complex.
New
Chaverri et al., Viçosa, Brazil. In Mycologia, 23 Apr 2015
A phylogeny was generated with maximum likelihood and Bayesian inference methods applied to a three-partition dataset (ITS, 28S, MCM7-RPB1-TUB2).
Application of the phylogenetic species concept to Wallemia sebi from house dust and indoor air revealed by multi-locus genealogical concordance.
New
Seifert et al., Ottawa, Canada. In Plos One, Dec 2014
The ITS and four protein-coding genes (MCM7, RPB1, RPB2, and TSR1) were sequenced for 85 isolates.
Coalescent-based species delimitation approach uncovers high cryptic diversity in the cosmopolitan lichen-forming fungal genus protoparmelia (lecanorales, ascomycota).
New
Schmitt et al., Frankfurt am Main, Germany. In Plos One, Dec 2014
In this study, we inferred the phylogeny of 18 species currently assigned to this genus based on 160 specimens and six markers: mtSSU, nuLSU, ITS, RPB1, MCM7, and TSR1.
Evolution of lysine acetylation in the RNA polymerase II C-terminal domain.
New
Capra et al., Nashville, United States. In Bmc Evol Biol, Dec 2014
BACKGROUND: RPB1, the largest subunit of RNA polymerase II, contains a highly modifiable C-terminal domain (CTD) that consists of variations of a consensus heptad repeat sequence (Y1S2P3T4S5P6S7).
Multigene assessment of the species boundaries and sexual status of the basidiomycetous yeasts Cryptococcus flavescens and C. terrestris (Tremellales).
New
Fonseca et al., Braunschweig, Germany. In Plos One, Dec 2014
The following five loci were chosen for MLS: the rDNA ITS-LSU region, the rDNA IGS1 spacer, and fragments of the genes encoding the largest subunit of RNA polymerase II (RPB1), the translation elongation factor 1 alpha (TEF1) and the p21-activated protein kinase (STE20).
The super elongation complex (SEC) family in transcriptional control.
Impact
GeneRIF
Shilatifard et al., Kansas City, United States. In Nat Rev Mol Cell Biol, 2012
Studies indicate that the super elongation complex (SEC) consisting of ELL, P-TEFb (CDK9) and MLL required for rapid transcriptional induction in the presence or absence of paused RNA polymerase II (Pol II).
Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
GeneRIF
Lewis et al., Bethesda, United States. In J Biol Chem, 2012
Results indicate roles for both the RNA polymerase II C-terminal domain (CTD) and O-GlcNAc in the regulation of transcription initiation.
Separate domains of fission yeast Cdk9 (P-TEFb) are required for capping enzyme recruitment and primed (Ser7-phosphorylated) Rpb1 carboxyl-terminal domain substrate recognition.
GeneRIF
Fisher et al., New York City, United States. In Mol Cell Biol, 2012
Separate domains of Cdk9 (P-TEFb) are required for capping enzyme recruitment and primed (Ser7-phosphorylated) Rpb1 carboxyl-terminal domain substrate recognition.
Threonine-4 of mammalian RNA polymerase II CTD is targeted by Polo-like kinase 3 and required for transcriptional elongation.
GeneRIF
Eick et al., München, Germany. In Embo J, 2012
Here, the authors report phosphorylation of Thr4 by Polo-like kinase 3 in mammalian cells.
Activator-mediator binding stabilizes RNA polymerase II orientation within the human mediator-RNA polymerase II-TFIIF assembly.
GeneRIF
Taatjes et al., Boulder, United States. In J Mol Biol, 2012
These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly.
A phylogenetic overview of the Agaricomycotina.
Review
Hibbett, Worcester, United States. In Mycologia, 2006
Recent phylogenetic analyses by P. Matheny and colleagues combining nuclear rRNA genes with the protein-coding genes rpb1, rpb2 and tef1 support the division of Agaricomycotina into Tremellomycetes, Dacrymycetes and Agaricomycetes.
Evolutionary relationships among basal fungi (Chytridiomycota and Zygomycota): Insights from molecular phylogenetics.
Review
Sugiyama et al., Ibaraki, Japan. In J Gen Appl Microbiol, 2005
Evolutionary relationships of the two basal fungal phyla Chytridiomycota and Zygomycota are reviewed in light of recent molecular phylogenetic investigation based on rDNA (nSSU, nLSU rDNA), entire mitochondrial genomes, and nuclear protein coding gene sequences (e.g., EF-1alpha, RPB1).
CTD phosphatase: role in RNA polymerase II cycling and the regulation of transcript elongation.
Review
Dahmus et al., In Prog Nucleic Acid Res Mol Biol, 2001
The repetitive C-terminal domain (CTD) of the largest RNA polymerase II subunit plays a critical role in the regulation of gene expression.
Complementary DNA sequencing: expressed sequence tags and human genome project.
Impact
Moreno et al., Bethesda, United States. In Science, 1991
Of the sequences generated, 337 represent new genes, including 48 with significant similarity to genes from other organisms, such as a yeast RNA polymerase II subunit; Drosophila kinesin, Notch, and Enhancer of split; and a murine tyrosine kinase receptor.
RNA polymerase II: subunit structure and function.
Review
Young et al., Cambridge, United States. In Trends Biochem Sci, 1990
Epitope tagging and other experiments made possible by the cloning of these genes have provided a clearer picture of RNA polymerase II subunit composition, stoichiometry and function, and set the stage for further investigating the dialogue between RNA polymerase II and transcription factors.
A suppressor of a HIS4 transcriptional defect encodes a protein with homology to the catalytic subunit of protein phosphatases.
Impact
Fink et al., Cambridge, United States. In Cell, 1989
Two of these suppressors, SIT1 and SIT2, are encoded by RPB1 and RPB2, the genes for the two largest subunits of RNA polymerase II.
Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases.
Impact
Ingles et al., In Cell, 1985
We have determined the nucleotide sequence of two yeast RNA polymerase genes, RPO21 and RPO31, which encode the largest subunits of RNA polymerases II and III, respectively.
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