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Study reports 2.53 A atomic structures of both the human PAF1/CTR9 and yeast Paf1/Ctr9 heterodimers. Results clearly reveal that the heterodimer of PAF1/CTR9 or Paf1/Ctr9 is the core component of evolutionarily conserved multifunctional polymerase-associated factor 1 complex (Paf1C) and is important for human PAF1C or yeast Paf1C assembly, yeast viability, and Paf1C-mediated histone modifications.
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a subset of enhancers can primarily modulate gene expression by controlling the release of paused Pol II in a PAF1-dependent manner.
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These results reveal ubiquitin-proteasome system regulation of Paf1 and suggest downregulation of ubiquitin-proteasome system in elevating Paf1's abundance in poorly differentiated cancers.
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The various functions of Paf1C, such as the regulation of promoter-proximal pausing and development in higher eukaryotes, are complex and context dependent.
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High PAF1 expression is associated with ovarian cancer.
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Overexpression of PD2 leads to increased tumorigenicity and metastasis in pancreatic ductal adenocarcinoma.
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Propose that degradation of MYC limits the accumulation of MYC/PAF1C complexes during transcriptional activation.
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Mechanistic studies indicated that PAF1C could promote lung cancer cell proliferation through regulating c-MYC transcription.
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CNOT4 controls the degradation of chromatin-unbound PAF1 via the 26S proteasome.
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this study found that Pol II-associated factor 1 (PAF1) is a critical regulator of paused Pol II release, that positive transcription elongation factor b (P-TEFb) directly regulates the initial recruitment of PAF1 complex (PAF1C) to genes, and that the subsequent recruitment of CDK12 is dependent on PAF1C.
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This study reveals an evolutionarily conserved role for PAF1 as a regulator of promoter-proximal pausing by RNA Pol II in all metazoans, including human.
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PD2 is a novel cancer stem cell (CSC) maintenance protein, loss of which renders the CSCs more susceptible to drug-induced cell death.
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Together, these results indicate that human adenovirus E1A uses hBre1 to recruit the hPaf1 complex in order to optimally activate viral early transcription by enhancing transcriptional elongation.
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The results show that the Paf1/Leo1 heterodimer is necessary for its binding to histone H3, the histone octamer, and nucleosome in vitro.
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E1A changes the function of hBre1 from a ubiquitin ligase involved in substrate selection to a scaffold which recruits hPaf1 as a means to stimulate transcription and transcription-coupled histone modifications.
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Data indicate that the Plus3 domain of the Rtf1 subunit mediates Paf1C recruitment to genes by binding a repeating domain within the phosphorylated elongation factor Spt5.
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Data show that activation-induced deaminase (AID) associates with RNA polymerase-associated factor 1 (PAF1) through its N-terminal domain.
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PAF1c acts as an arginine methyl histone effector that is recruited to promoters and activates a subset of genes, including targets of estrogen signaling.
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that hPaf1/PD2 in association with MLL1 regulates methylation of H3K4 residues, as well as interacts and regulates nuclear shuttling of chromatin remodeling protein CHD1, facilitating its function in pancreatic cancer cells
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Interaction between the Polymerase Associated Factor complex and Mixed Lineage Leukemia is critical for gene rearranged leukemogenesis.
