Nucleic Acids Research · 2003 · 28 citations · 23 references
Life SciencesCell BiologyMolecular BiologyGene ExpressionProtein-protein InteractionsTranscriptional RegulationRna Polymerase FunctionRna Polymerase Ii TranscriptionRna-binding ProteinsRna-protein InteractionsSmall Nuclear Rna BiologyPhosphorylation MotifsPhosphorylation Of The Rna Polymerase Ii C-terminal DomainRna Polymerase Ii FunctionRna Polymerase Ii RegulationSmall Nucleolar RibonucleoproteinsSubunit AssemblyTranscription Elongation ComplexesTranscription Elongation Control
RNA polymerase II transcription is associated with cyclic phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II. To date, FCP1 is the only specific CTD phosphatase, which is required for general transcription and cell viability. To identify FCP1-associated proteins, we constructed a human cell line expressing epitope-tagged FCP1. In addition to RAP74, a previously identified FCP1 interacting factor, we determined that FCP1-affinity purified extracts contain RNAPII that has either a hyper- or a hypo-phosphorylated CTD. In addition, by mass spectrometry of affinity purified FCP1-associated factors, we identified a novel FCP1-interacting protein, named MEP50, a recently described component of the methylosome complex that binds to the snRNP's Sm proteins. We found that FCP1 specifically interacts with components of the spliceosomal U small nuclear ribonucleoproteins. These results suggest a putative role of FCP1 CTD-phosphatase in linking the transcription elongation with the splicing process.
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7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
Van Trung Nguyen, Tamás Kiss, Annemieke A. Michels et al. · Nature · 2001 · 706 citations
The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
Zhiyuan Yang, Qingwei Zhu, Kunxin Luo et al. · Nature · 2001 · 682 citations