ArticleMolecular and cellular biology2007
Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed, 84 citations in OpenAlex.
- GPATCH11 ortholog Sap34 regulates pre-mRNA splicing by interacting with early spliceosomal complexes in Schizosaccharomyces pombe.Scientific reports · 2026Article
- G-patch proteins: important regulators of pre-mRNA splicing and ribosome biogenesis.Frontiers in cell and developmental biology · 2026Review
- Structures of aberrant spliceosome intermediates on their way to disassembly.Nature structural & molecular biology · 2025Article
- Structural insights into spliceosome fidelity: DHX35-GPATCH1- mediated rejection of aberrant splicing substrates.Cell research · 2025Article
- Conformational dynamics of the RNA binding channel regulates loading and translocation of the DEAH-box helicase Prp43.Nucleic acids research · 2023Article
- Arresting Spliceosome Intermediates at Various Stages of the Splicing Pathway.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Defining the Functional Interactome of Spliceosome-Associated G-Patch Protein Gpl1 in the Fission YeastInternational journal of molecular sciences · 2022Article
- Functional recovery of the germ line following splicing collapse.Cell death and differentiation · 2022Article
- Auxiliary domains of the HrpB bacterial DExH-box helicase shape its RNA preferences.RNA biology · 2020Article
- Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Functional analysis of Cwc24 ZF-domain in 5' splice site selection.Nucleic acids research · 2019Article
- Termination of pre-mRNA splicing requires that the ATPase and RNA unwindase Prp43p acts on the catalytic snRNA U6.Genes & development · 2019Article
- Co-evolution of spliceosomal disassembly interologs: crowning J-protein component with moonlighting RNA-binding activity.Current genetics · 2019Article
- Molecular Mechanisms of pre-mRNA Splicing through Structural Biology of the Spliceosome.Cold Spring Harbor perspectives in biology · 2019Review
- Cwc23 is a component of the NTR complex and functions to stabilize Ntr1 and facilitate disassembly of spliceosome intermediates.Nucleic acids research · 2018Article
- Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2.Biophysical journal · 2018Article
- A new role for FBP21 as regulator of Brr2 helicase activity.Nucleic acids research · 2017Article
- Regulation of Prp43-mediated disassembly of spliceosomes by its cofactors Ntr1 and Ntr2.Nucleic acids research · 2017Article
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Saccharomyces cerevisiae splicing factors Ntr1 (also known as Spp382) and Ntr2 form a stable complex and can further associate with DExD/H-box RNA helicase Prp43 to form a functional complex, termed the NTR complex, which catalyzes spliceosome disassembly. We show that Prp43 interacts with Ntr1-Ntr2 in a dynamic manner. The Ntr1-Ntr2 complex can also bind to the spliceosome first, before recruiting Prp43 to catalyze disassembly. Binding of Ntr1-Ntr2 or Prp43 does not require ATP, but disassembly of the spliceosome requires hydrolysis of ATP. The NTR complex also dynamically interacts with U5 snRNP. Ntr2 interacts with U5 component Brr2 and is essential for both interactions of NTR with U5 and with the spliceosome. Ntr2 alone can also bind to U5 and to the spliceosome, suggesting a role of Ntr2 in mediating the binding of NTR to the spliceosome through its interaction with U5. Our results demonstrate that dynamic interactions of NTR with U5, through the interaction of Ntr2 with Brr2, and interactions of Ntr1 and Prp43 govern the recruitment of Prp43 to the spliceosome to mediate spliceosome disassembly.
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