Evidence map›Paper›PMID 20512115›Full record

ArticleThe EMBO journal2010

Prp43p contains a processive helicase structural architecture with a specific regulatory domain.

Hélène Walbott, Saïda Mouffok, Régine Capeyrou, Simon Lebaron, Odile Humbert, Herman van Tilbeurgh, Yves Henry, Nicolas Leulliot

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Crystal structures of the DExH-box RNA helicase DHX9.Acta crystallographica. Section D, Structural biology · 2023
    Article
  8. Crystal structure of Prp16 in complex with ADP.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  9. Life (Basel, Switzerland) · 2023
    Article
  10. Article
  11. 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 · 2022
    Article
  12. Article
  13. Review
  14. Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021
    Article
  17. DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021
    Review
  18. Article
  19. Structural basis for DEAH-helicase activation by G-patch proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Article

29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Hélène WalbottInstitut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université de Paris-Sud, CNRS-UMR8619, IFR115, Orsay Cedex, France.
Saïda Mouffok
Régine Capeyrou
Simon Lebaron
Odile Humbert
Herman van Tilbeurgh
Yves Henry
Nicolas Leulliot
Centre National de la Recherche Scientifique · FRInstitut de Biochimie et Biophysique Moléculaire et Cellulaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DEAH/RNA helicase A (RHA) helicase family comprises proteins involved in splicing, ribosome biogenesis and transcription regulation. We report the structure of yeast Prp43p, a DEAH/RHA helicase remarkable in that it functions in both splicing and ribosome biogenesis. Prp43p displays a novel structural architecture with an unforeseen homology with the Ski2-like Hel308 DNA helicase. Together with the presence of a beta-hairpin in the second RecA-like domain, Prp43p contains all the structural elements of a processive helicase. Moreover, our structure reveals that the C-terminal domain contains an oligonucleotide/oligosaccharide-binding (OB)-fold placed at the entrance of the putative nucleic acid cavity. Deletion or mutations of this domain decrease the affinity of Prp43p for RNA and severely reduce Prp43p ATPase activity in the presence of RNA. We also show that this domain constitutes the binding site for the G-patch-containing domain of Pfa1p. We propose that the C-terminal domain, specific to DEAH/RHA helicases, is a central player in the regulation of helicase activity by binding both RNA and G-patch domain proteins.

Indexed as

Adenosine TriphosphateCrystallography, X-RayDEAD-box RNA HelicasesModels, MolecularProtein ConformationProtein Structure, TertiaryRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDEAD-box RNA HelicasesPFA1 protein, S cerevisiaePRP43 protein, S cerevisiaeRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID20512115
PMCPMC2905241
OpenAlexW2165906337

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.