ArticleMolecular and cellular biology2000
Functional Cus1p is found with Hsh155p in a multiprotein splicing factor associated with U2 snRNA.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
- Evolutionarily conserved spliceosome-exosome pathway in nuclear mRNA surveillance.Genes & development · 2026Article
- The SF3b Complex is an Integral Component of the Spliceosome and Targeted by Natural Product-Based Inhibitors.Sub-cellular biochemistry · 2021Review
- Arabidopsis JANUS Regulates Embryonic Pattern Formation through Pol II-Mediated Transcription of WOX2 and PIN7.iScience · 2019Article
- Cus2 enforces the first ATP-dependent step of splicing by binding to yeast SF3b1 through a UHM-ULM interaction.RNA (New York, N.Y.) · 2019Article
- Structure of a pre-catalytic spliceosome.Nature · 2017Article
- Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.RNA (New York, N.Y.) · 2017Article
- Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment.Protein science : a publication of the Protein Society · 2017Article
- SF3B1 is a stress-sensitive splicing factor that regulates both HSF1 concentration and activity.PloS one · 2017Article
- Identification of Putative Mek1 Substrates during Meiosis in Saccharomyces cerevisiae Using Quantitative Phosphoproteomics.PloS one · 2016Article
- Structural and functional characterization of the N terminus of Schizosaccharomyces pombe Cwf10.Eukaryotic cell · 2013Article
- Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.PeerJ · 2013Article
- Spliceostatin A inhibits spliceosome assembly subsequent to prespliceosome formation.Nucleic acids research · 2010Article
- Predicting co-complexed protein pairs from heterogeneous data.PLoS computational biology · 2008Article
- Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145.Molecular and cellular biology · 2006Article
- Interactions of the yeast SF3b splicing factor.Molecular and cellular biology · 2005Article
- Mer1p is a modular splicing factor whose function depends on the conserved U2 snRNP protein Snu17p.Nucleic acids research · 2004Article
- Spatial organization of protein-RNA interactions in the branch site-3' splice site region during pre-mRNA splicing in yeast.Molecular and cellular biology · 2003Article
- Systematic identification of novel protein domain families associated with nuclear functions.Genome research · 2002Article
- The ATP requirement for U2 snRNP addition is linked to the pre-mRNA region 5' to the branch site.RNA (New York, N.Y.) · 2001Article
- A novel U2 and U11/U12 snRNP protein that associates with the pre-mRNA branch site.The EMBO journal · 2001Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
To explore the dynamics of snRNP structure and function, we have studied Cus1p, identified as a suppressor of U2 snRNA mutations in budding yeast. Cus1p is homologous to human SAP145, a protein present in the 17S form of the human U2 snRNP. Here, we define the Cus1p amino acids required for function in yeast. The segment of Cus1p required for binding to Hsh49p, a homolog of human SAP49, is contained within an essential region of Cus1p. Antibodies against Cus1p coimmunoprecipitate U2 snRNA, as well as Hsh155p, a protein homologous to human SAP155. Biochemical fractionation of splicing extracts and reconstitution of heat-inactivated splicing extracts from strains carrying a temperature-sensitive allele of CUS1 indicate that Cus1p and Hsh155p reside in a functional, high-salt-stable complex that is salt-dissociable from U2 snRNA. We propose that Cus1p, Hsh49p, and Hsh155p exist in a stable protein complex which can exchange with a core U2 snRNP and which is necessary for U2 snRNP function in prespliceosome assembly. The Cus1p complex shares functional as well as structural similarities with human SF3b.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.