Evidence map›Paper›PMID 42098403›Full record

ArticleNature structural & molecular biology2026

Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed.

Thomas Schöndorf, Valentyn Petrychenko, Ilgin Kotan, Drishan Dahal, Natalia Napieraj, Luis Daniel Cruz-Zaragoza, Cong Wang, Oliver Urbach, Tanja Gall, Sven Dennerlein and 3 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. When membrane insertion sets the pace of mitochondrial translation.Nature structural & molecular biology · 2026
    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

13 authors.

Thomas Schöndorf *Department of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.
Valentyn Petrychenko *Project Group Molecular Machines in Motion, Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Goettingen, Germany.ORCID http://orcid.org/0000-0001-9867-9493
Ilgin KotanCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-9028-979X
Drishan DahalDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.ORCID http://orcid.org/0009-0009-7280-2102
Natalia NapierajDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.ORCID http://orcid.org/0000-0003-3750-5179
Luis Daniel Cruz-ZaragozaDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.ORCID http://orcid.org/0000-0001-9568-0245
Cong WangDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.
Oliver UrbachDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.
Tanja GallDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.
Sven DennerleinDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany.
Günter KramerCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-7552-8393
Niels FischerProject Group Molecular Machines in Motion, Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Goettingen, Germany. niels.fischer@mpinat.mpg.de.ORCID http://orcid.org/0000-0002-4609-4052
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Goettingen, Goettingen, Germany. peter.rehling@medizin.uni-goettingen.de.ORCID http://orcid.org/0000-0001-5661-5272

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human mitochondrial genome encodes 13 subunits of the oxidative phosphorylation system essential for energy metabolism to drive cellular activities. Translation of 11 mRNAs by membrane-bound ribosomes is coupled to insertion of the nascent polypeptides into the inner membrane aided by the OXA1L insertase. To this end, the mechanism of membrane insertion of nascent polypeptides and the functional link to the translation process are not sufficiently understood. Here, we applied ribosome profiling to assess translation dynamics in combination with cryo-electron microscopy analysis of a COX1 ribosome-nascent chain complex to visualize cotranslational folding of the nascent chain. We find that the membrane topology of the translation product impacts translation speed and that positioning of amphipathic helices in the ribosome vestibule induces structural changes, correlating with translation pausing events. Thus, our findings reveal a link between translation process and folding and membrane insertion of nascent polypeptides at the inner mitochondrial membrane.

Indexed as

Mitochondrial MembranesMitochondrial ProteinsProtein BiosynthesisRibosomesCryoelectron MicroscopyElectron Transport Complex IVHumansModels, MolecularProtein FoldingRibosome ProfilingElectron Transport Complex IVMitochondrial Proteins

Identifiers

PMID42098403
PMCPMC13186706

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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.