Evidence map›Paper›PMID 32602580›Full record

ArticleThe EMBO journal2020

Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1.

Eva Kummer, Nenad Ban

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  11. Translation in Mitochondrial Ribosomes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Evolution: Mitochondrial Ribosomes Across Species.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  15. Article
  16. Review
  17. Review
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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

2 authors at 1 institution in 1 country.

Eva KummerDepartment of Biology, Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zurich, Zurich, Switzerland.
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zurich, Zurich, Switzerland.ORCID 0000-0002-9527-210X
École Polytechnique Fédérale de Lausanne · CH

Funding

EMBO Postdoctoral Long Term Fellowship 1196-2014Ernst Jung PrizeOtto Naegeli PrizeSNSF National Center for Excellence (NCCR) in RNA and Disease 138262Swiss National Science Foundation 310030B_163478
6 · The paper itself

Abstract

Mitochondria are eukaryotic organelles of bacterial origin where respiration takes place to produce cellular chemical energy. These reactions are catalyzed by the respiratory chain complexes located in the inner mitochondrial membrane. Notably, key components of the respiratory chain complexes are encoded on the mitochondrial chromosome and their expression relies on a dedicated mitochondrial translation machinery. Defects in the mitochondrial gene expression machinery lead to a variety of diseases in humans mostly affecting tissues with high energy demand such as the nervous system, the heart, or the muscles. The mitochondrial translation system has substantially diverged from its bacterial ancestor, including alterations in the mitoribosomal architecture, multiple changes to the set of translation factors and striking reductions in otherwise conserved tRNA elements. Although a number of structures of mitochondrial ribosomes from different species have been determined, our mechanistic understanding of the mitochondrial translation cycle remains largely unexplored. Here, we present two cryo-EM reconstructions of human mitochondrial elongation factor G1 bound to the mammalian mitochondrial ribosome at two different steps of the tRNA translocation reaction during translation elongation. Our structures explain the mechanism of tRNA and mRNA translocation on the mitoribosome, the regulation of mtEFG1 activity by the ribosomal GTPase-associated center, and the basis of decreased susceptibility of mtEFG1 to the commonly used antibiotic fusidic acid.

Indexed as

Protein BiosynthesisAnimalsCryoelectron MicroscopyHumansMitochondrial MembranesMitochondrial ProteinsMitochondrial RibosomesPeptide Elongation Factor GRNA, MitochondrialRNA, TransferSwineGFM1 protein, humanMitochondrial ProteinsPeptide Elongation Factor GRNA, MitochondrialRNA, Transfercryo-EMelongationmitoribosomemtEFG1translation

Identifiers

PMID32602580
PMCPMC7396830
OpenAlexW3039606902

What OpenQuestion holds

Textmetadata
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.