Evidence map›Paper›PMID 30968120›Full record

ArticleNucleic acids research2019

The mitoribosome-specific protein mS38 is preferentially required for synthesis of cytochrome c oxidase subunits.

Jeffri-Noelle Mays, Yolanda Camacho-Villasana, Rodolfo Garcia-Villegas, Xochitl Perez-Martinez, Antoni Barrientos, Flavia Fontanesi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
    Article
  2. Article
  3. Stroke and vascular neurology · 2025
    Article
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  6. Review
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  12. Molecular biology of the cell · 2021
    Article
  13. Molecular and cellular biology · 2021
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  14. Review
  15. Article
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  17. Review
  18. 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

6 authors at 2 institutions in 2 countries.

Jeffri-Noelle MaysDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Yolanda Camacho-VillasanaDepartamento de Genetica Molecular, Instituto de Fisiologiía Celular, Universidad Nacional Autonoma de Mexico, Mexico City 04510, Mexico.
Rodolfo Garcia-VillegasDepartamento de Genetica Molecular, Instituto de Fisiologiía Celular, Universidad Nacional Autonoma de Mexico, Mexico City 04510, Mexico.
Xochitl Perez-MartinezDepartamento de Genetica Molecular, Instituto de Fisiologiía Celular, Universidad Nacional Autonoma de Mexico, Mexico City 04510, Mexico.
Antoni BarrientosDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Flavia FontanesiDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Universidad Nacional Autónoma de México · MXUniversity of Miami · US

Funding

Mitochondrial Biogenesis in Health and DiseaseR35GM118141 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2016 to 2025
$8.9M
NIGMS NIH HHS R35 GM118141
6 · The paper itself

Abstract

Message-specific translational regulation mechanisms shape the biogenesis of multimeric oxidative phosphorylation (OXPHOS) enzyme in mitochondria from the yeast Saccharomyces cerevisiae. These mechanisms, driven mainly by the action of mRNA-specific translational activators, help to coordinate synthesis of OXPHOS catalytic subunits by the mitoribosomes with both the import of their nucleus-encoded partners and their assembly to form the holocomplexes. However, little is known regarding the role that the mitoribosome itself may play in mRNA-specific translational regulation. Here, we show that the mitoribosome small subunit protein Cox24/mS38, known to be necessary for mitoribosome-specific intersubunit bridge formation and 15S rRNA H44 stabilization, is required for efficient mitoribogenesis. Consequently, mS38 is necessary to sustain the overall mitochondrial protein synthesis rate, despite an adaptive ∼2-fold increase in mitoribosome abundance in mS38-deleted cells. Additionally, the absence of mS38 preferentially disturbs translation initiation of COX1, COX2, and COX3 mRNAs, without affecting the levels of mRNA-specific translational activators. We propose that mS38 confers the mitochondrial ribosome an intrinsic capacity of translational regulation, probably acquired during evolution from bacterial ribosomes to facilitate the translation of mitochondrial mRNAs, which lack typical anti-Shine-Dalgarno sequences.

Indexed as

Gene Expression RegulationGene Expression Regulation, FungalProtein BiosynthesisArabidopsisDNA, MitochondrialElectron Transport Complex IVHumansKluyveromycesMitochondrial ProteinsMitochondrial RibosomesOryzaOxidative PhosphorylationPolyribosomesRNA, MessengerRNA, MitochondrialSaccharomyces cerevisiaeDNA, MitochondrialElectron Transport Complex IVmitochondrial messenger RNAMitochondrial ProteinsRNA, MessengerRNA, MitochondrialSaccharomyces cerevisiae Proteins

Identifiers

PMID30968120
PMCPMC6582356
OpenAlexW2939222427

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.