Evidence map›Paper›PMID 32522994›Full record

ArticleNature communications2020

Distinct pre-initiation steps in human mitochondrial translation.

Anas Khawaja, Yuzuru Itoh, Cristina Remes, Henrik Spåhr, Olessya Yukhnovets, Henning Höfig, Alexey Amunts, Joanna Rorbach

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 78 citations in OpenAlex.

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  16. Biallelic variants inmedRxiv : the preprint server for health sciences · 2024
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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

8 authors at 4 institutions in 2 countries.

Anas Khawaja *Department of Medical Biochemistry and Biophysics, Division of Molecular Metabolism, Karolinska Institutet, Biomedicum, 171 65, Solna, Sweden.
Yuzuru Itoh *Department of Medical Biochemistry and Biophysics, Division of Molecular Metabolism, Karolinska Institutet, Biomedicum, 171 65, Solna, Sweden.ORCID http://orcid.org/0000-0001-7802-5572
Cristina RemesDepartment of Mitochondrial Biology, Max-Planck-Institute for Biology of Ageing, Joseph-Stelzmann-Str. 9b, 50931, Cologne, Germany.
Henrik SpåhrDepartment of Medical Biochemistry and Biophysics, Division of Molecular Metabolism, Karolinska Institutet, Biomedicum, 171 65, Solna, Sweden.
Olessya YukhnovetsRWTH Aachen, I. Physikalisches Institut (IA), Aachen, Germany.
Henning HöfigRWTH Aachen, I. Physikalisches Institut (IA), Aachen, Germany.ORCID http://orcid.org/0000-0003-0506-783X
Alexey AmuntsDepartment of Medical Biochemistry and Biophysics, Division of Molecular Metabolism, Karolinska Institutet, Biomedicum, 171 65, Solna, Sweden. amunts@scilifelab.se.ORCID http://orcid.org/0000-0002-5302-1740
Joanna RorbachDepartment of Medical Biochemistry and Biophysics, Division of Molecular Metabolism, Karolinska Institutet, Biomedicum, 171 65, Solna, Sweden. joanna.rorbach@ki.se.ORCID http://orcid.org/0000-0002-2891-2840
Karolinska Institutet · SEForschungszentrum Jülich · DEStockholm University · SEMax Planck Institute for Biology of Ageing · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two distinct mitochondrial pre-initiation assembly steps involving those factors. Single-particle cryo-EM revealed that in the first step, interactions between mitochondria-specific protein mS37 and mtIF3 keep the small mitoribosomal subunit in a conformation favorable for a subsequent accommodation of mtIF2 in the second step. Combination with fluorescence cross-correlation spectroscopy analyses suggests that mtIF3 promotes complex assembly without mRNA or initiator tRNA binding, where exclusion is achieved by the N-terminal and C-terminal domains of mtIF3. Finally, the association of large mitoribosomal subunit is required for initiator tRNA and leaderless mRNA recruitment to form a stable initiation complex. These data reveal fundamental aspects of mammalian protein synthesis that are specific to mitochondria.

Indexed as

Cryoelectron MicroscopyHumansMitochondriaRibosomesRNA, MessengerRNA, Messenger

Identifiers

PMID32522994
PMCPMC7287080
OpenAlexW3033896273

What OpenQuestion holds

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LicenceCC BY
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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.