Evidence map›Paper›PMID 23925311›Full record

ReviewRNA biology2013

PPR proteins shed a new light on RNase P biology.

Franziska Pinker, Géraldine Bonnard, Anthony Gobert, Bernard Gutmann, Kamel Hammani, Claude Sauter, Peter A Gegenheimer, Philippe Giegé

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. TheRNA (New York, N.Y.) · 2018
    Article
  11. Article
  12. Review
  13. Biophysical analysis ofThe Journal of biological chemistry · 2017
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  19. Article
  20. Review
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 4 institutions in 2 countries.

Franziska PinkerInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France; Institut de Biologie Moléculaire et Cellulaire du CNRS; Architecture et Réactivité de l'ARN; Université de Strasbourg; Strasbourg, France.
Géraldine BonnardInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Anthony GobertInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Bernard GutmannInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Kamel HammaniInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Claude SauterInstitut de Biologie Moléculaire et Cellulaire du CNRS; Architecture et Réactivité de l'ARN; Université de Strasbourg; Strasbourg, France.
Peter A GegenheimerDepartment of Molecular Biosciences; University of Kansas;Lawrence, KS USA.
Philippe GiegéInstitut de Biologie Moléculaire des Plantes du CNRS; Université de Strasbourg; Strasbourg, France.
Université de Strasbourg · FRArchitecture et Réactivité de l'arN · FRInstitut de Biologie Moléculaire des Plantes · FRUniversity of Kansas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and organelles. RNase P is the endonucleolytic activity that removes 5' leader sequences from tRNA precursors and is thus essential for translation. Before the characterization of PRORP, RNase P enzymes were thought to occur universally as ribonucleoproteins, although some evidence implied that some eukaryotes or cellular compartments did not use RNA for RNase P activity. The characterization of PRORP reveals a two-domain enzyme, with an N-terminal domain containing multiple PPR motifs and assumed to achieve target specificity and a C-terminal domain holding catalytic activity. The nature of PRORP interactions with tRNAs suggests that ribonucleoprotein and protein-only RNase P enzymes share a similar substrate binding process.

Indexed as

Arabidopsis ProteinsCell NucleusChloroplastsEukaryotic CellsHumansMitochondriaPlant ProteinsProtein ConformationProtein Structure, TertiaryRibonuclease PRNA-Binding ProteinsRNA PrecursorsRNA, TransferTrypanosoma brucei bruceiArabidopsis ProteinsPlant ProteinsPRORP1 protein, ArabidopsisRibonuclease PRNA-Binding ProteinsRNA PrecursorsRNA, Transferevolutionpentatricopeptide repeatRNA binding proteinRNase PtRNA maturation

Identifiers

PMID23925311
PMCPMC3858429
OpenAlexW2094090797

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.