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DR1-associated protein 1

DRAP1, NC2alpha
Transcriptional repression is a general mechanism for regulating transcriptional initiation in organisms ranging from yeast to humans. Accurate initiation of transcription from eukaryotic protein-encoding genes requires the assembly of a large multiprotein complex consisting of RNA polymerase II and general transcription factors such as TFIIA, TFIIB, and TFIID. DR1 is a repressor that interacts with the TATA-binding protein (TBP) of TFIID and prevents the formation of an active transcription complex by precluding the entry of TFIIA and/or TFIIB into the preinitiation complex. The protein encoded by this gene is a corepressor of transcription that interacts with DR1 to enhance DR1-mediated repression. The interaction between this corepressor and DR1 is required for corepressor function and appears to stabilize the TBP-DR1-DNA complex. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DRB1, TBP, POLYMERASE, CAN, Histone
Papers on DRAP1
Evaluation of housekeeping genes for normalizing real-time quantitative PCR assays in pig skeletal muscle at multiple developmental stages.
Lei et al., Wuhan, China. In Gene, Aug 2015
Our results indicated that DRAP1 and RNF7 were the most appropriate combination to normalize gene expression in the Yorkshire samples, the combination of DRAP1 and WSB2 were appropriate in the Tongcheng samples, H3F3A and DRAP1 in prenatal periods, DRAP1 and RNF7 in postnatal periods, and the combination of DRAP1 and WSB2 was most suitable for accurate normalization in whole samples.
Dr1 (NC2) is present at tRNA genes and represses their transcription in human cells.
White et al., Glasgow, United Kingdom. In Nucleic Acids Res, 2010
In contrast, we demonstrate that endogenous Dr1 is present at pol III templates in human cells, as is its dimerization partner DRAP1 (also called NC2alpha).
To bleed or not to bleed. A prediction based on individual gene profiling combined with dose-volume histogram shapes in prostate cancer patients undergoing three-dimensional conformal radiation therapy.
Gariboldi et al., Milano, Italy. In Int J Radiat Oncol Biol Phys, 2009
Four genes were significantly upregulated in the high-risk nonbleeder group than in the other groups: DDX17 (p = 0.048), DRAP1 (p = 0.0025), RAD23 (p = 0.015), and SRF (p = 0.024).
Regulation of nuclear import and export of negative cofactor 2.
Doenecke et al., Göttingen, Germany. In J Biol Chem, 2009
heterodimerization with NC2alpha masks the nuclear localization signal in NC2beta, which prevents nuclear export of the NC2 complex
Nonradioactive, ultrasensitive site-specific protein-protein photocrosslinking: interactions of alpha-helix 2 of TATA-binding protein with general transcription factor TFIIA and transcriptional repressor NC2.
Ebright et al., United States. In Nucleic Acids Res, 2008
We further have found that TBP H2 can be crosslinked to NC2 in the NC2-TBP-DNA complex, and we have mapped the crosslink to the C-terminal 'tail' of the NC2 alpha-subunit (NC2alpha).
Cooperative action of NC2 and Mot1p to regulate TATA-binding protein function across the genome.
Timmers et al., Utrecht, Netherlands. In Genes Dev, 2008
Relative binding of NC2alpha and Mot1p is higher at TATA promoters, whereas NC2beta has a preference for TATA-less promoters.
The dual control of TFIIB recruitment by NC2 is gene specific.
Collart et al., Genève, Switzerland. In Nucleic Acids Res, 2008
Negative co-factor 2 (NC2) is a conserved eukaryotic complex composed of two subunits, NC2alpha (Drap1) and NC2beta (Dr1) that associate through a histone-fold motif.
Involvement of GTA protein NC2beta in neuroblastoma pathogenesis suggests that it physiologically participates in the regulation of cell proliferation.
Purrello et al., Catania, Italy. In Mol Cancer, 2007
respectively) were also reduced, whereas we didn't detect any quantitative alteration of the mRNAs from GTF2B and NC2alpha (localized at 1p22-p21 and 11q13.3,
NC2 mobilizes TBP on core promoter TATA boxes.
Meisterernst et al., München, Germany. In Nat Struct Mol Biol, 2007
provide evidence that negative cofactor-2 (NC2) induces dynamic conformational changes in the TBP-DNA complex that allow it to escape and return to TATA-binding mode
The initiator core promoter element antagonizes repression of TATA-directed transcription by negative cofactor NC2.
Oelgeschläger et al., United Kingdom. In J Biol Chem, 2007
Here we report that a functional INR provides resistance to NC2 (Dr1/DRAP1), a general repressor of TATA promoters.
Global distribution of negative cofactor 2 subunit-alpha on human promoters.
Meisterernst et al., München, Germany. In Proc Natl Acad Sci U S A, 2007
The global distribution of DRAP1 on promoters was determined.
NC2alpha interacts with BTAF1 and stimulates its ATP-dependent association with TATA-binding protein.
Timmers et al., Utrecht, Netherlands. In Mol Cell Biol, 2004
physical cooperation between BTAF1 and NC2alpha in TBP regulation
Hypoxia actively represses transcription by inducing negative cofactor 2 (Dr1/DrAP1) and blocking preinitiation complex assembly.
Barton et al., Stanford, United States. In J Biol Chem, 2003
Hypoxia actively represses transcription by inducing this protein and blocking preinitiation complex assembly.
Inhibition of excess nodal signaling during mouse gastrulation by the transcriptional corepressor DRAP1.
Shen et al., United States. In Science, 2003
Here we show that the transcriptional corepressor DRAP1 has a very specific role in regulation of Nodal activity during mouse embryogenesis.
Nodal signaling in vertebrate development.
Schier, New York City, United States. In Annu Rev Cell Dev Biol, 2002
Additional modulators of Nodal signaling include convertases that regulate the generation of the mature signal, and factors such as Arkadia and DRAP1 that regulate the cellular responses to the signal.
The DPE, a core promoter element for transcription by RNA polymerase II.
Kadonaga, San Diego, United States. In Exp Mol Med, 2002
For instance, NC2/Dr1-Drap1 is a repressor of TATA-dependent transcription and an activator of DPE-dependent transcription.
Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.
Burley et al., New York City, United States. In Cell, 2001
The N termini of NC2 alpha and beta resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions.
A basal transcription factor that activates or represses transcription.
Kadonaga et al., San Diego, United States. In Science, 2000
The purified factor was found to be the Drosophila homolog of the transcriptional repressor known as NC2 or Dr1-Drap1.
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