Evidence map›Paper›PMID 26135751›Full record

ArticleRNA (New York, N.Y.)2015

Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.

Robert D Fagerlund, Anna Perederina, Igor Berezin, Andrey S Krasilnikov

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  3. Review
  4. Article
  5. Review
  6. The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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

4 authors at 1 institution in 1 country.

Robert D FagerlundDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Anna PerederinaDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Igor BerezinDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Andrey S KrasilnikovDepartment of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Pennsylvania State University · US

Funding

Proteins in RNA-Based EnzymesR01GM085149 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI KRASILNIKOV, ANDREY S. · 2008 to 2017
$2.9M
NIGMS NIH HHS GM085149NIGMS NIH HHS R01 GM085149
6 · The paper itself

Abstract

Ribonuclease (RNase) P and RNase MRP are closely related catalytic ribonucleoproteins involved in the metabolism of a wide range of RNA molecules, including tRNA, rRNA, and some mRNAs. The catalytic RNA component of eukaryotic RNase P retains the core elements of the bacterial RNase P ribozyme; however, the peripheral RNA elements responsible for the stabilization of the global architecture are largely absent in the eukaryotic enzyme. At the same time, the protein makeup of eukaryotic RNase P is considerably more complex than that of the bacterial RNase P. RNase MRP, an essential and ubiquitous eukaryotic enzyme, has a structural organization resembling that of eukaryotic RNase P, and the two enzymes share most of their protein components. Here, we present the results of the analysis of interactions between the largest protein component of yeast RNases P/MRP, Pop1, and the RNA moieties of the enzymes, discuss structural implications of the results, and suggest that Pop1 plays the role of a scaffold for the stabilization of the global architecture of eukaryotic RNase P RNA, substituting for the network of RNA-RNA tertiary interactions that maintain the global RNA structure in bacterial RNase P.

Indexed as

EndoribonucleasesModels, MolecularNucleic Acid ConformationProtein FootprintingRibonuclease PRibonucleasesRibonucleoproteinsRNA, CatalyticRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndoribonucleasesmitochondrial RNA-processing endoribonucleasePOP1 protein, S cerevisiaePOP4 protein, S cerevisiaeRibonuclease PRibonucleasesRibonucleoproteinsRNA, CatalyticRNA, FungalSaccharomyces cerevisiae ProteinsPop1ribonucleoproteinRNA foldingRNase MRPRNase PSaccharomyces cerevisiae

Identifiers

PMID26135751
PMCPMC4536320
OpenAlexW2106775444

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.