ArticleNucleic acids research1996
The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 87 citations in OpenAlex.
- Article
- Chromatin remodelers: We are the drivers!!Nucleus (Austin, Tex.) · 2016Review
- Interconnections Between RNA-Processing Pathways Revealed by a Sequencing-Based Genetic Screen for Pre-mRNA Splicing Mutants in Fission Yeast.G3 (Bethesda, Md.) · 2016Article
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
- Co-transcriptional regulation of alternative pre-mRNA splicing.Biochimica et biophysica acta · 2012Review
- The in vivo kinetics of RNA polymerase II elongation during co-transcriptional splicing.PLoS biology · 2011Article
- Transcription factories are nuclear subcompartments that remain in the absence of transcription.Genes & development · 2008Article
- In vivo commitment to yeast cotranscriptional splicing is sensitive to transcription elongation mutants.Genes & development · 2006Article
- Role for PSF in mediating transcriptional activator-dependent stimulation of pre-mRNA processing in vivo.Molecular and cellular biology · 2005Article
- Prp8 protein: at the heart of the spliceosome.RNA (New York, N.Y.) · 2005Review
- The C-terminal domain of RNA polymerase II functions as a phosphorylation-dependent splicing activator in a heterologous protein.Molecular and cellular biology · 2005Article
- NMPdb: Database of Nuclear Matrix Proteins.Nucleic acids research · 2005Article
- p54(nrb) associates with the 5' splice site within large transcription/splicing complexes.The EMBO journal · 2004Article
- Splicing and transcription-associated proteins PSF and p54nrb/nonO bind to the RNA polymerase II CTD.RNA (New York, N.Y.) · 2002Article
- A human RNA polymerase II-containing complex associated with factors necessary for spliceosome assembly.The Journal of biological chemistry · 2002Article
- High-copy-number expression of Sub2p, a member of the RNA helicase superfamily, suppresses hpr1-mediated genomic instability.Molecular and cellular biology · 2001Article
- Capping, splicing, and 3' processing are independently stimulated by RNA polymerase II: different functions for different segments of the CTD.Genes & development · 2001Article
- Trichinella spiralis-infected muscle cells: abundant RNA polymerase II in nuclear speckle domains colocalizes with nuclear antigens.Infection and immunity · 2001Article
- TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins.Molecular and cellular biology · 2000Article
- Three-dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles.The Journal of cell biology · 1999Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The monoclonal antibody CC-3 recognizes a phosphodependent epitope on a 255 kDa nuclear matrix protein (p255) recently shown to associate with splicing complexes as part of the [U4/U6.U5] tri-snRNP particle [Chabot et al. (1995) Nucleic Acids Res. 23, 3206-3213]. In mouse and Drosophila cultured cells the electrophoretic mobility of p255, faster in the latter species, was identical to that of the hyperphosphorylated form of RNA polymerase II largest subunit (IIo). The CC-3 immunoreactivity of p255 was abolished by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, which is known to cause the dephosphorylation of the C-terminal domain of subunit IIo by inhibiting the TFIIH-associated kinase. The identity of p255 was confirmed by showing that CC-3-immunoprecipitated p255 was recognized by POL3/3 and 8WG16, two antibodies specific to RNA polymerase II largest subunit. Lastly, the recovery of RNA polymerase II largest subunit from HeLa splicing mixtures was compromised by EDTA, which prevents the interaction of p255 with splicing complexes and inhibits splicing. Our results indicate that p255 represents a highly phosphorylated form of RNA polymerase II largest subunit physically associated with spliceosomes and possibly involved in coupling transcription to RNA processing.
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