ArticleNucleic acids research2017
Regulation of Prp43-mediated disassembly of spliceosomes by its cofactors Ntr1 and Ntr2.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- The G-patch protein Cwf28 interacts with the RNA helicase Cdc28 in catalytically active spliceosomes in Schizosaccharomyces pombe.PloS one · 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
- An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly.Nature communications · 2024Article
- How does the spliceosome dismantle itself?Nature · 2024Article
- Article
- Intron lariat spliceosomes convert lariats to true circles: implications for intron transposition.Genes & development · 2024Article
- Dysfunction of Gpl1-Gih35-Wdr83 Complex inInternational journal of molecular sciences · 2024Article
- Intron-lariat spliceosomes convert lariats to true circles: implications for intron transposition.bioRxiv : the preprint server for biology · 2024Article
- GPATCH4 regulates rRNA and snRNA 2'-O-methylation in both DHX15-dependent and DHX15-independent manners.Nucleic acids research · 2024Article
- Splicing factor Prp18p promotes genome-wide fidelity of consensus 3'-splice sites.Nucleic acids research · 2023Article
- Splicing quality control mediated by DHX15 and its G-patch activator SUGP1.Cell reports · 2023Article
- Conformational dynamics of the RNA binding channel regulates loading and translocation of the DEAH-box helicase Prp43.Nucleic acids research · 2023Article
- Maturation of small nucleolar RNAs: from production to function.RNA biology · 2023Review
- DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 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
- Tsukushi proteoglycan maintains RNA splicing and developmental signaling network in GFAP-expressing subventricular zone neural stem/progenitor cells.Frontiers in cell and developmental biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DEAH-box NTPase Prp43 disassembles spliceosomes in co-operation with the cofactors Ntr1/Spp382 and Ntr2, forming the NTR complex. How Prp43 is regulated by its cofactors to discard selectively only intron-lariat spliceosomes (ILS) and defective spliceosomes and to prevent disassembly of earlier and properly assembled/wild-type spliceosomes remains unclear. First, we show that Ntr1΄s G-patch motif (Ntr1GP) can be replaced by the GP motif of Pfa1/Sqs1, a Prp43΄s cofactor in ribosome biogenesis, demonstrating that the specific function of Ntr1GP is to activate Prp43 for spliceosome disassembly and not to guide Prp43 to its binding site in the spliceosome. Furthermore, we show that Ntr1΄s C-terminal domain (CTD) plays a safeguarding role by preventing Prp43 from disrupting wild-type spliceosomes other than the ILS. Ntr1 and Ntr2 can also discriminate between wild-type and defective spliceosomes. In both type of spliceosomes, Ntr1-CTD impedes Prp43-mediated disassembly while the Ntr1GP promotes disassembly. Intriguingly, Ntr2 plays a specific role in defective spliceosomes, likely by stabilizing Ntr1 and allowing Prp43 to enter a productive interaction with the GP motif of Ntr1. Our data indicate that Ntr1 and Ntr2 act as 'doorkeepers' and suggest that both cofactors inspect the RNP structure of spliceosomal complexes thereby targeting suboptimal spliceosomes for Prp43-mediated disassembly.
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