ArticleGenes & development2000
ATP can be dispensable for prespliceosome formation in yeast.
Article in Genes & development, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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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
44 citing papers in PubMed, 70 citations in OpenAlex.
- Coordinated alternative splicing decisions via stepwise exon definition.Nucleic acids research · 2026Article
- New mechanistic insights into prespliceosome formation-roles of DEAD-box proteins Prp5 and Sub2.RNA (New York, N.Y.) · 2025Article
- Branch site recognition by the spliceosome.RNA (New York, N.Y.) · 2024Review
- Transcriptomic Analysis Provides New Insights into the Tolerance Mechanisms of Green MacroalgaeBiology · 2024Article
- Inefficient recruitment of DDX39B impedes pre-spliceosome assembly onRNA (New York, N.Y.) · 2024Article
- Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP assembly.Nature communications · 2023Article
- Attacking a DEAD problem: The role of DEAD-box ATPases in ribosome assembly and beyond.Methods in enzymology · 2022Article
- Prp5-Spt8/Spt3 interaction mediates a reciprocal coupling between splicing and transcription.Nucleic acids research · 2020Article
- Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019Review
- 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
- The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface.The Journal of biological chemistry · 2019Article
- SF3b1 mutations associated with myelodysplastic syndromes alter the fidelity of branchsite selection in yeast.Nucleic acids research · 2017Article
- Stoichiometries of U2AF35, U2AF65 and U2 snRNP reveal new early spliceosome assembly pathways.Nucleic acids research · 2017Article
- Conformational dynamics of stem II of the U2 snRNA.RNA (New York, N.Y.) · 2016Article
- Functional roles of DExD/H-box RNA helicases in Pre-mRNA splicing.Journal of biomedical science · 2015Review
- A novel mechanism for Prp5 function in prespliceosome formation and proofreading the branch site sequence.Genes & development · 2015Article
- A splicing-dependent transcriptional checkpoint associated with prespliceosome formation.Molecular cell · 2014Article
- Using yeast genetics to study splicing mechanisms.Methods in molecular biology (Clifton, N.J.) · 2014Article
- A high-throughput splicing assay identifies new classes of inhibitors of human and yeast spliceosomes.Journal of biomolecular screening · 2013Article
- Functional roles of protein splicing factors.Bioscience reports · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The first ATP-dependent step in pre-mRNA splicing involves the stable binding of U2 snRNP to form the prespliceosome. We show that a prespliceosome-like complex forms in the absence of ATP in yeast extracts lacking the U2 suppressor protein CUS2. These complexes display the same pre-mRNA and U snRNA requirements as authentic prespliceosomes and can be chased through the splicing pathway, indicating that they are a functional intermediate in the spliceosome assembly pathway. ATP-independent prespliceosome-like complexes are also observed in extracts containing a mutant U2 snRNA. Loss of CUS2 does not bypass the role of PRP5, an RNA helicase family member required for ATP-dependent prespliceosome formation. Genetic interactions between CUS2 and a heat-sensitive prp5 allele parallel those observed between CUS2 and U2, and suggest that CUS2 mediates functional interactions between U2 RNA and PRP5. We propose that CUS2 enforces ATP dependence during formation of the prespliceosome by brokering an interaction between PRP5 and the U2 snRNP that depends on correct U2 RNA structure.
Indexed as
Identifiers
10640279PMC316341W1958447102What OpenQuestion holds
Registered trials
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.