ArticleNucleic acids research2017
Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.
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 16 papers.
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16 citing papers in PubMed, 39 citations in OpenAlex.
- An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly.Nature communications · 2024Article
- 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
- Conformational dynamics of the RNA binding channel regulates loading and translocation of the DEAH-box helicase Prp43.Nucleic acids research · 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
- A model for DHX15 mediated disassembly of A-complex spliceosomes.RNA (New York, N.Y.) · 2022Article
- The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase.RNA biology · 2021Article
- Sgd1 is an MIF4G domain-containing cofactor of the RNA helicase Fal1 and associates with the 5' domain of the 18S rRNA sequence.RNA biology · 2020Article
- Structural basis for DEAH-helicase activation by G-patch proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The DEAH-box RNA helicase Dhr1 contains a remarkable carboxyl terminal domain essential for small ribosomal subunit biogenesis.Nucleic acids research · 2019Article
- Identification of proteins associated with splicing factors Ntr1, Ntr2, Brr2 and Gpl1 in the fission yeastCell cycle (Georgetown, Tex.) · 2019Article
- Molecular mechanism of the RNA helicase DHX37 and its activation by UTP14A in ribosome biogenesis.RNA (New York, N.Y.) · 2019Article
- Human RNA cap1 methyltransferase CMTr1 cooperates with RNA helicase DHX15 to modify RNAs with highly structured 5' termini.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018Article
- DHX15 regulates CMTR1-dependent gene expression and cell proliferation.Life science alliance · 2018Article
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Authors and funding
12 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DEAH box helicase Prp43 is a bifunctional enzyme from the DEAH/RHA helicase family required both for the maturation of ribosomes and for lariat intron release during splicing. It interacts with G-patch domain containing proteins which activate the enzymatic activity of Prp43 in vitro by an unknown mechanism. In this work, we show that the activation by G-patch domains is linked to the unique nucleotide binding mode of this helicase family. The base of the ATP molecule is stacked between two residues, R159 of the RecA1 domain (R-motif) and F357 of the RecA2 domain (F-motif). Using Prp43 F357A mutants or pyrimidine nucleotides, we show that the lack of stacking of the nucleotide base to the F-motif decouples the NTPase and helicase activities of Prp43. In contrast the R159A mutant (R-motif) showed reduced ATPase and helicase activities. We show that the Prp43 R-motif mutant induces the same phenotype as the absence of the G-patch protein Gno1, strongly suggesting that the processing defects observed in the absence of Gno1 result from a failure to activate the Prp43 helicase. Overall we propose that the stacking between the R- and F-motifs and the nucleotide base is important for the activity and regulation of this helicase family.
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