BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A

@article{Anderson1998BRCA1PI,
  title={BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A},
  author={Stephen F. Anderson and Brian P. Schlegel and Toshihiro Nakajima and Eric S. Wolpin and Jeffrey D. Parvin},
  journal={Nature Genetics},
  year={1998},
  volume={19},
  pages={254-256}
}
The breast cancer specific tumour suppressor protein, BRCA1 (refs 1,2), activates transcription when linked with a DNA-binding domain and is a component of the RNA polymerase II (Pol II) holoenzyme. We show here that RNA helicase A (RHA) protein links BRCA1 to the holoenzyme complex. The region of BRCA1 which interacts with RHA and, thus, the holoenzyme complex, corresponds to subregions of the BRCT domain of BRCA1 ( ref. 9). This interaction was shown to occur in yeast nuclei, and expression… 
BRCA1 Associates with Processive RNA Polymerase II*
TLDR
Preferential interaction with processive RNA pol II in undamaged cells places BRCA1 in position to link late events in transcription with repair processes in eukaryotic cells.
The BRCA1 and BARD1 association with the RNA polymerase II holoenzyme.
TLDR
Investigation of BRCA1-associated RING domain protein (BARD1) found that it is a component of the holo-pol complex and immunocytochemistry of expressed full-length and deletion mutants showed that the NH(2) terminus of B RCA1 is important for nuclear dot formation in S-phase.
The identification of a novel role for BRCA1 in regulating RNA polymerase I transcription
TLDR
BRCA1, a nuclear phosphoprotein, and a known tumour suppressor involved in variety of cellular processes such as DNA damage response, transcriptional regulation, cell cycle control and ubiquitylation, is associated with rDNA repeats, in particular with the regulatory regions of the rRNA gene.
BRCA1 interacts with components of the histone deacetylase complex.
  • R. Yarden, L. Brody
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
It is demonstrated that BRCA1 interacts with components of the histone deacetylase complex, and therefore may explain the involvement of BRC a1 in multiple processes such as transcription, DNA repair, and recombination.
BRCA1 cooperates with NUFIP and P-TEFb to activate transcription by RNA polymerase II
TLDR
The ubiquitous, stably expressed, nuclear protein NUFIP specifically stimulates activator-independent pol II transcription in vitro and in vivo and facilitates ATP-dependent dissociation of hyperphosphorylated pol II from open transcription complexes in vitro.
Casein kinase 2 binds to and phosphorylates BRCA1.
TLDR
Through a yeast two hybrid assay, it was found that the beta-subunit of casein kinase 2 (CK2) associated with a carboxy-terminal region of BRCA1, and this association was much weaker with the same fragment bearing a missense mutation that has been identified in breast tumors.
BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10α in activated transcription
TLDR
Two of the subunits of the Pol II enzyme, hRPB2 and h RPB10α, mediate the regulated stimulation of transcription and it is found that the transcriptional coactivator BRCA1 interacts directly with the core Pol II complex in vitro.
BRCA1 Can Modulate RNA Polymerase II Carboxy-Terminal Domain Phosphorylation Levels
TLDR
It is shown that the BRCA1 C-terminal region can negatively modulate phosphorylation levels of the RNA polymerase II CTD by the Cdk-activating kinase (CAK) in vitro.
Redistribution of BRCA1 among Four Different Protein Complexes following Replication Blockage*
TLDR
The HUIC was shown not to contain a number of holo-pol components or the Rad50-Mre11-Nbs1 complex but was associated with the BRCA1-associated RING domain protein BARD1, suggesting that the hydroxyurea-induced complex (HUIC) is involved with the response to DNA replication blockage.
BRCA1 Physically and Functionally Interacts with ATF1*
TLDR
It is demonstrated that BRCA1 and ATF1 can physically associate in vitro, in yeast, and in human cells, and implicate BRCa1 in transcriptional activation of ATF1 target genes, some of which are involved in the transcriptional response to DNA damage.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
A BRCA1 domain, which is deleted in about 90% of clinically relevant mutations, participates in binding to the holoenzyme complex in cells, consistent with recent data identifying transcription activation domains in the B RCA1 protein and link the BRC a1 tumor suppressor protein with the transcription process as a holoen enzyme-bound protein.
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TLDR
The presence of the p300 coactivator and the chromatin-modifying BRG1 protein support a role for the Pol II holoenzyme as a key target for regulation by enhancer binding proteins.
RNA Helicase A Mediates Association of CBP with RNA Polymerase II
TLDR
It is shown that complex formation between CBP and RNA polymerase II requires RNA helicase A (RHA), a nuclear DNA/RNA helicase that is related to the Drosophila male dosage compensation factor mle.
Human RNA helicase A is homologous to the maleless protein of Drosophila.
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TLDR
It is shown that the C-terminal region, comprising exons 16-24 (aa 1560-1863) of BRCA1 fused to GAL4 DNA binding domain can activate transcription both in yeast and mammalian cells.
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TLDR
A model is suggested in which the flanking domains influence and regulate the unwinding properties of NDH II, a full-length human nuclear DNA helicase II was cloned and overexpressed in a baculovirus-derived expression system.
BRCA1 regulates p53-dependent gene expression.
TLDR
Findings suggest a function of BRCA1 as a p53 coactivator, which stimulates artificial and genomic promoter constructs containing p53-responsive elements and coimmunoprecipitates with p53, in vitro and in vivo.
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TLDR
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TLDR
It is shown that BRCA1 transactivates expression of the cyclin-dependent kinase inhibitor p21WAF1/CIP1 in a p53-independent manner, and that B RCA1 inhibits cell-cycle progression into the S-phase following its transfection into human cancer cells.
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