Evidence map›Paper›PMID 20075859›Full record

ArticleThe EMBO journal2010

Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain.

Anna Perederina, Olga Esakova, Chao Quan, Elena Khanova, Andrey S Krasilnikov

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
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  14. Review
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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

5 authors at 1 institution in 1 country.

Anna PerederinaDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Olga Esakova
Chao Quan
Elena Khanova
Andrey S Krasilnikov
Pennsylvania State University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Proteins in RNA-Based EnzymesR01GM085149 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI KRASILNIKOV, ANDREY S. · 2008 to 2017
$2.9M
Macromolecular X-Ray Crystallography InstrumentS10RR023439 · NCRR · PENNSYLVANIA STATE UNIVERSITY, THE · PI YENNAWAR, NEELA H. · 2007 to 2007
$500k
NCRR NIH HHS S10 RR023439NCRR NIH HHS S10RR023439NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM085149NIGMS NIH HHS R01 GM085149
6 · The paper itself

Abstract

Ribonuclease (RNase) P is a site-specific endoribonuclease found in all kingdoms of life. Typical RNase P consists of a catalytic RNA component and a protein moiety. In the eukaryotes, the RNase P lineage has split into two, giving rise to a closely related enzyme, RNase MRP, which has similar components but has evolved to have different specificities. The eukaryotic RNases P/MRP have acquired an essential helix-loop-helix protein-binding RNA domain P3 that has an important function in eukaryotic enzymes and distinguishes them from bacterial and archaeal RNases P. Here, we present a crystal structure of the P3 RNA domain from Saccharomyces cerevisiae RNase MRP in a complex with RNase P/MRP proteins Pop6 and Pop7 solved to 2.7 A. The structure suggests similar structural organization of the P3 RNA domains in RNases P/MRP and possible functions of the P3 domains and proteins bound to them in the stabilization of the holoenzymes' structures as well as in interactions with substrates. It provides the first insight into the structural organization of the eukaryotic enzymes of the RNase P/MRP family.

Indexed as

Amino Acid SequenceBase SequenceCrystallography, X-RayEndoribonucleasesHoloenzymesMacromolecular SubstancesModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein Structure, TertiaryRibonuclease PRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsEndoribonucleasesHoloenzymesMacromolecular Substancesmitochondrial RNA-processing endoribonucleaseRibonuclease PRNA, FungalSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID20075859
PMCPMC2829168
OpenAlexW2123066271

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.