ArticleNucleic acids research2014
The telomerase inhibitor Gno1p/PINX1 activates the helicase Prp43p during ribosome biogenesis.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 56 citations in OpenAlex.
- Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli.Genes & development · 2026Article
- G-patch proteins: important regulators of pre-mRNA splicing and ribosome biogenesis.Frontiers in cell and developmental biology · 2026Review
- DHX15 inhibits mouse APOBEC3 deamination.PLoS pathogens · 2025Article
- An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly.Nature communications · 2024Article
- PinX1 plays multifaceted roles in human cancers: a review and perspectives.Molecular biology reports · 2024Review
- The dual life of disordered lysine-rich domains of snoRNPs in rRNA modification and nucleolar compaction.Nature communications · 2024Article
- Unveiling the DHX15-G-patch interplay in retroviral RNA packaging.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- GPATCH4 regulates rRNA and snRNA 2'-O-methylation in both DHX15-dependent and DHX15-independent manners.Nucleic acids research · 2024Article
- Article
- Conformational dynamics of the RNA binding channel regulates loading and translocation of the DEAH-box helicase Prp43.Nucleic acids research · 2023Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- 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
- Rbp95 binds to 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation.Nucleic acids research · 2022Article
- Article
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
- DHX15-independent roles for TFIP11 in U6 snRNA modification, U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing fidelity.Nature communications · 2021Article
- DHX15 is required to control RNA virus-induced intestinal inflammation.Cell reports · 2021Article
- The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase.RNA biology · 2021Article
- Structural basis for DEAH-helicase activation by G-patch proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We provide evidence that a central player in ribosome synthesis, the ribonucleic acid helicase Prp43p, can be activated by yeast Gno1p and its human ortholog, the telomerase inhibitor PINX1. Gno1p and PINX1 expressed in yeast interact with Prp43p and the integrity of their G-patch domain is required for this interaction. Moreover, PINX1 interacts with human PRP43 (DHX15) in HeLa cells. PINX1 directly binds to yeast Prp43p and stimulates its adenosine triphosphatase activity, while alterations of the G patch abolish formation of the PINX1/Prp43p complex and the stimulation of Prp43p. In yeast, lack of Gno1p leads to a decrease in the levels of pre-40S and intermediate pre-60S pre-ribosomal particles, defects that can be corrected by PINX1 expression. We show that Gno1p associates with 90S and early pre-60S pre-ribosomal particles and is released from intermediate pre-60S particles. G-patch alterations in Gno1p or PINX1 that inhibit their interactions with Prp43p completely abolish their function in yeast ribosome biogenesis. Altogether, our results suggest that activation of Prp43p by Gno1p/PINX1 within early pre-ribosomal particles is crucial for their subsequent maturation.
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