Evidence map›Paper›PMID 25181249›Full record

ArticleRNA biology2014

The Pet309 pentatricopeptide repeat motifs mediate efficient binding to the mitochondrial COX1 transcript in yeast.

Angélica Zamudio-Ochoa, Yolanda Camacho-Villasana, Aldo E García-Guerrero, Xochitl Pérez-Martínez

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024
    Review
  5. Article
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  8. Molecular biology of the cell · 2021
    Article
  9. Molecular and cellular biology · 2021
    Article
  10. Review
  11. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  12. Article
  13. Article
  14. The Cox1 C-terminal domain is a central regulator of cytochromeThe Journal of biological chemistry · 2017
    Article
  15. Article
  16. Article
  17. Tissue- and Condition-Specific Isoforms of Mammalian CytochromeOxidative medicine and cellular longevity · 2017
    Review
  18. Article
  19. 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.

Angélica Zamudio-OchoaDepartamento de Genética Molecular; Instituto de Fisiología Celular; Universidad Nacional Autónoma de México; México.
Yolanda Camacho-VillasanaDepartamento de Genética Molecular; Instituto de Fisiología Celular; Universidad Nacional Autónoma de México; México.
Aldo E García-GuerreroDepartamento de Genética Molecular; Instituto de Fisiología Celular; Universidad Nacional Autónoma de México; México.
Xochitl Pérez-MartínezDepartamento de Genética Molecular; Instituto de Fisiología Celular; Universidad Nacional Autónoma de México; México.
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial synthesis of Cox1, the largest subunit of the cytochrome c oxidase complex, is controlled by Mss51 and Pet309, two mRNA-specific translational activators that act via the COX1 mRNA 5'-UTR through an unknown mechanism. Pet309 belongs to the pentatricopeptide repeat (PPR) protein family, which is involved in RNA metabolism in mitochondria and chloroplasts, and its sequence predicts at least 12 PPR motifs in the central portion of the protein. Deletion of these motifs selectively disrupted translation but not accumulation of the COX1 mRNA. We used RNA coimmunoprecipitation assays to show that Pet309 interacts with the COX1 mRNA in vivo and that this association is present before processing of the COX1 mRNA from the ATP8/6 polycistronic mRNA. This association was not affected by deletion of 8 of the PPR motifs but was undetectable after deletion of the entire 12-PPR region. However, interaction of the Pet309 protein lacking 12 PPR motifs with the COX1 mRNA was detected after overexpression of the mutated form of the protein, suggesting that deletion of this region decreased the binding affinity for the COX1 mRNA without abolishing it entirely. Moreover, binding of Pet309 to the COX1 mRNA was affected by deletion of Mss51. This work demonstrates an in vivo physical interaction between a yeast mitochondrial translational activator and its target mRNA and shows the cooperativity of the PPR domains of Pet309 in interaction with the COX1 mRNA.

Indexed as

Binding SitesElectron Transport Complex IVGene Expression Regulation, FungalMembrane ProteinsMitochondrial ProteinsMutationPeptide Initiation FactorsRibosomesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsCox1 protein, S cerevisiaeElectron Transport Complex IVMembrane ProteinsMitochondrial ProteinsMss51 protein, S cerevisiaePeptide Initiation FactorsPET309 protein, S cerevisiaeRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsTranscription FactorsCOX1mRNAcytochrome coxidasemitochondriapentatricopeptide repeattranslationyeast

Identifiers

PMID25181249
PMCPMC4179968
OpenAlexW1984512155

What Socratic 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 Socratic graph.