Evidence map›Paper›PMID 22034500›Full record

ArticleNucleic acids research2012

Yeast mitochondrial RNase P, RNase Z and the RNA degradosome are part of a stable supercomplex.

Rachid Daoud, Lise Forget, B Franz Lang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. TheRNA (New York, N.Y.) · 2018
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Massive programmed translational jumping in mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Rachid DaoudRobert-Cedergren Centre for Bioinformatics and Genomics, Department of Biochemistry, Université de Montréal, 2900 Edouard-Montpetit, Montreal, Quebec H3T 1J4, Canada.
Lise Forget
B Franz Lang
Université de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initial steps in the synthesis of functional tRNAs require 5'- and 3'-processing of precursor tRNAs (pre-tRNAs), which in yeast mitochondria are achieved by two endonucleases, RNase P and RNase Z. In this study, using a combination of detergent-free Blue Native Gel Electrophoresis, proteomics and in vitro testing of pre-tRNA maturation, we reveal the physical association of these plus other mitochondrial activities in a large, stable complex of 136 proteins. It contains a total of seven proteins involved in RNA processing including RNase P and RNase Z, five out of six subunits of the mitochondrial RNA degradosome, components of the fatty acid synthesis pathway, translation, metabolism and protein folding. At the RNA level, there are the small and large rRNA subunits and RNase P RNA. Surprisingly, this complex is absent in an oar1Δ deletion mutant of the type II fatty acid synthesis pathway, supporting a recently published functional link between pre-tRNA processing and the FAS II pathway--apparently by integration into a large complex as we demonstrate here. Finally, the question of mt-RNase P localization within mitochondria was investigated, by GFP-tracing of a known protein subunit (Rpm2p). We find that about equal fractions of RNase P are soluble versus membrane-attached.

Indexed as

EndoribonucleasesFatty Acid SynthasesMitochondriaMitochondrial MembranesMitochondrial ProteinsProtein SubunitsRibonuclease PRNA Processing, Post-TranscriptionalRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionEndoribonucleasesFatty Acid SynthasesMitochondrial ProteinsProtein SubunitsRibonuclease PRNase ZRNA, TransferRPM2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22034500
PMCPMC3287206
OpenAlexW2152687754

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.