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RPB9 Rpb9p

Rpb9, contacts DNA
This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit, in combination with two other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. The product of this gene has two zinc finger motifs with conserved cysteines and the subunit does possess zinc binding activity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, CAN, ACID, HAD, TFIIS
Papers on Rpb9
Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage.
Biertümpfel et al., Martinsried, Germany. In Elife, Jan 2016
The GEN1 chromodomain directly contacts DNA and its truncation severely hampers GEN1's catalytic activity.
DNA recognition for virus assembly through multiple sequence-independent interactions with a helix-turn-helix motif.
Antson et al., Eugene, United States. In Nucleic Acids Res, Jan 2016
Nuclear magnetic resonance chemical shift perturbation studies with an arbitrary single-site substrate suggest that the HTH motif contacts DNA similarly to how certain HTH proteins contact DNA non-specifically.
Association of condensin with chromosomes depends on DNA binding by its HEAT-repeat subunits.
Haering et al., Heidelberg, Germany. In Nat Struct Mol Biol, 2014
Previous work has suggested that condensin, in addition to encircling chromatin fibers topologically within the ring-shaped structure formed by its SMC and kleisin subunits, contacts DNA directly.
Identification of new residues involved in intramolecular signal transmission in a prokaryotic transcriptional repressor.
Ramos et al., Granada, Spain. In J Bacteriol, 2014
TtgV contacts DNA mainly through a canonical recognition helix, but its three-dimensional structure bound to DNA revealed that two residues, R19 and S35, outside the HTH motif, directly contact DNA.
The multi-zinc finger protein ZNF217 contacts DNA through a two-finger domain.
Crossley et al., Sydney, Australia. In J Biol Chem, 2011
Classical C2H2 zinc finger proteins are among the most abundant transcription factors found in eukaryotes, and the mechanisms through which they recognize their target genes have been extensively investigated.
Transcription by the multifunctional RNA polymerase I in Trypanosoma brucei functions independently of RPB7.
Günzl et al., Farmington, United States. In Mol Biochem Parasitol, 2011
Interestingly, RPB7 did crosslink to the RRNA promoter but so did the RNA pol II-specific subunit RPB9 suggesting that RNA pol II is recruited to this promoter.
p53 binding to nucleosomes within the p21 promoter in vivo leads to nucleosome loss and transcriptional activation.
Prives et al., New York City, United States. In Proc Natl Acad Sci U S A, 2011
It is well established that p53 contacts DNA in a sequence-dependent manner in order to transactivate its myriad target genes.
Rpb9 subunit controls transcription fidelity by delaying NTP sequestration in RNA polymerase II.
Kashlev et al., Frederick, United States. In J Biol Chem, 2009
Rpb9 is a small non-essential subunit of yeast RNA polymerase II located on the surface on the enzyme.
Nuclear signalling by tumour-associated antigen EpCAM.
Gires et al., München, Germany. In Nat Cell Biol, 2009
Released EpICD associates with FHL2, beta-catenin and Lef-1 to form a nuclear complex that contacts DNA at Lef-1 consensus sites, induces gene transcription and is oncogenic in immunodeficient mice.
Yeast Rpb9 plays an important role in ubiquitylation and degradation of Rpb1 in response to UV-induced DNA damage.
Li et al., Baton Rouge, United States. In Mol Cell Biol, 2007
In response to ultraviolet radiation, Rpb9 also functions in promoting ubiquitylation and degradation of Rpb1, the largest subunit of Pol II.
Stimulation of RNA polymerase II transcript cleavage activity contributes to maintain transcriptional fidelity in yeast.
Sekimizu et al., Tokyo, Japan. In Genes Cells, 2007
both S-II and Rpb9 maintain transcriptional fidelity by stimulating the cleavage activity intrinsic to RNA polymerase II
Modulation of Rad26- and Rpb9-mediated DNA repair by different promoter elements.
Smerdon et al., Baton Rouge, United States. In J Biol Chem, 2007
Rad26-mediated repair can be either transcription-coupled or transcription-independent; Rpb9-mediated repair is strictly transcription-coupled and is efficient only when the transcription level is high
Evidence that the transcription elongation function of Rpb9 is involved in transcription-coupled DNA repair in Saccharomyces cerevisiae.
Chen et al., Baton Rouge, United States. In Mol Cell Biol, 2006
The transcription elongation function of Rpb9 is involved in transcription-coupled DNA repair.
RNA polymerase II subunit Rpb9 is important for transcriptional fidelity in vivo.
Hawley et al., Eugene, United States. In Proc Natl Acad Sci U S A, 2006
Rpb9 plays an important role in maintaining transcriptional fidelity, whereas TFIIS may serve a different primary purpose
Aromatic Ring Currents at a Protein Surface: Use of (1)H-NMR Chemical Shifts to Refine the Structure of a Naked β Sheet.
Weiss et al., Chicago, United States. In J Biomol Struct Dyn, 1999
A model is provided by an archaeal Zn ribbon homologous to eukaryotic RNA polymerase II subunit 9 (RPB9).
DNA recognition by beta-sheets.
Suzuki et al., Tsukuba, Japan. In Biopolymers, 1996
Upon following the major groove a two-stranded antiparallel beta-sheet dives into the groove and contacts DNA bases with its convex side facing the DNA, while upon following the minor groove, it binds around the sugar-phosphate backbones, with its opposite concave side shielding the DNA.
Muscle: the regulation of myogenesis.
Buckingham, Paris, France. In Curr Opin Genet Dev, 1994
At the molecular level, crystallographic studies have led to a structural model of the actinomyosin complex and also to information about how MyoD contacts DNA.
Altered specificity of DNA-binding proteins with transition metal dimerization domains.
Schepartz et al., New Haven, United States. In Science, 1993
The bZIP motif is characterized by a leucine zipper domain that mediates dimerization and a basic domain that contacts DNA.
Sequence-specific DNA binding by a short peptide dimer.
Kim et al., Cambridge, United States. In Science, 1990
A recently described class of DNA binding proteins is characterized by the "bZIP" motif, which consists of a basic region that contacts DNA and an adjacent "leucine zipper" that mediates protein dimerization.
Changing fos oncoprotein to a jun-independent DNA binding protein with GCN4 dimerization specificity by swapping "leucine zippers".
Struhl et al., Boston, United States. In Nature, 1989
These results indicate that the leucine zipper is sufficient to confer dimerization specificity and strongly suggest that Fos contacts DNA directly.
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