ArticleNucleic acids research1995
The nuclear matrix phosphoprotein p255 associates with splicing complexes as part of the [U4/U6.U5] tri-snRNP particle.
Article in Nucleic acids research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
- A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression.The EMBO journal · 2010Article
- DNA methylation and methyl-CpG binding proteins: developmental requirements and function.Chromosoma · 2009Review
- 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
- Association of the 72/74-kDa proteins, members of the heterogeneous nuclear ribonucleoprotein M group, with the pre-mRNA at early stages of spliceosome assembly.The Biochemical journal · 2002Article
- A human RNA polymerase II-containing complex associated with factors necessary for spliceosome assembly.The Journal of biological chemistry · 2002Article
- Participation of the C-terminal domain of RNA polymerase II in exon definition during pre-mRNA splicing.Molecular and cellular biology · 2000Article
- Topological localization of the carboxyl-terminal domain of RNA polymerase II in the initiation complex.The Journal of biological chemistry · 1999Article
- Phosphorylated RNA polymerase II stimulates pre-mRNA splicing.Genes & development · 1999Article
- Transcriptional termination in the Balbiani ring 1 gene is closely coupled to 3'-end formation and excision of the 3'-terminal intron.Genes & development · 1998Article
- Localization of human cytomegalovirus structural proteins to the nuclear matrix of infected human fibroblasts.Journal of virology · 1998Article
- A nuclear matrix protein interacts with the phosphorylated C-terminal domain of RNA polymerase II.Molecular and cellular biology · 1998Article
- Nuclear translocation and carboxyl-terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos.The EMBO journal · 1997Article
- Heat-shock inactivation of the TFIIH-associated kinase and change in the phosphorylation sites on the C-terminal domain of RNA polymerase II.Nucleic acids research · 1997Article
- The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes.Nucleic acids research · 1996Article
- A connection between pre-mRNA splicing and the cell cycle in fission yeast: cdc28+ is allelic with prp8+ and encodes an RNA-dependent ATPase/helicase.Molecular biology of the cell · 1996Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The monoclonal antibody CC3 recognizes a phosphorylated epitope present on an interphase protein of 255 kDa. Previous work has shown that p255 is localized mainly to nuclear speckles and remains associated with the nuclear matrix scaffold following extraction with non-ionic detergents, nucleases and high salt. The association of p255 with splicing complexes is suggested by the finding that mAb CC3 can inhibit in vitro splicing and immunoprecipitate pre-messenger RNA and splicing products. Small nuclear RNA immunoprecipitation assays show that p255 is a component of the U5 small nuclear ribonucleoprotein (snRNP) and the [U4/U6.U5] tri-snRNP complex. In RNase protection assays, mAb CC3 immunoprecipitates fragments containing branch site and 3' splice site sequences. As predicted for a [U4/U6.U5]-associated component, the recovery of the branch site-protected fragment requires binding of U2 snRNP and is inhibited by EDTA. p255 may correspond to the previously identified p220 protein, the mammalian analogue of the yeast PRP8 protein. Our results suggest that changes in the phosphorylation of p255 may be part of control mechanisms that interface splicing activity with nuclear organization.
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