Evidence map›Paper›PMID 33602856›Full record

ArticleScience (New York, N.Y.)2021

Mechanism of membrane-tethered mitochondrial protein synthesis.

Yuzuru Itoh, Juni Andréll, Austin Choi, Uwe Richter, Priyanka Maiti, Robert B Best, Antoni Barrientos, Brendan J Battersby, Alexey Amunts

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

104 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
  2. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. When membrane insertion sets the pace of mitochondrial translation.Nature structural & molecular biology · 2026
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    Article
  20. Vacuolar-type HNature communications · 2025
    Article

44 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 4 countries.

Yuzuru ItohScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165 Solna, Stockholm, Sweden. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0001-7802-5572
Juni AndréllScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165 Solna, Stockholm, Sweden. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0003-2313-9155
Austin ChoiDepartment of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0002-5476-4183
Uwe RichterInstitute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0002-0724-6957
Priyanka MaitiDepartment of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.ORCID https://orcid.org/0000-0003-4207-0341
Robert B BestLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.ORCID https://orcid.org/0000-0002-7893-3543
Antoni BarrientosDepartment of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0001-9018-3231
Brendan J BattersbyInstitute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0002-8136-2753
Alexey AmuntsScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165 Solna, Stockholm, Sweden. abarrientos@med.miami.edu brendan.battersby@helsinki.fi amunts@scilifelab.se.ORCID https://orcid.org/0000-0002-5302-1740
Science for Life Laboratory · SEUniversity of Miami · USUniversity of Helsinki · FINational Institutes of Health · US

Funding

Understanding protein folding, evolution and function via molecular simulationZIADK075104 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEST, ROBERT · 2013 to 2025
$13.7M
Mitochondrial Biogenesis in Health and DiseaseR35GM118141 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2016 to 2025
$8.9M
European Research Council 805230NIGMS NIH HHS R35 GM118141
6 · The paper itself

Abstract

Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo-electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1-like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery.

Indexed as

Protein BiosynthesisCryoelectron MicroscopyElectron Transport Complex IVHumansMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsMitochondrial RibosomesModels, MolecularNuclear ProteinsProtein BindingProtein ConformationProtein FoldingRibosomesElectron Transport Complex IVMembrane ProteinsMitochondrial ProteinsNuclear ProteinsOXA1 protein

Identifiers

PMID33602856
PMCPMC7610362
OpenAlexW3132414590

What OpenQuestion holds

Textmetadata
LicenceTDM
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.