Evidence map›Paper›PMID 31721420›Full record

ArticleEMBO reports2020

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome-nascent chain complex.

Cong Wang, Ricarda Richter-Dennerlein, David Pacheu-Grau, Fan Liu, Ying Zhu, Sven Dennerlein, Peter Rehling

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 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
2.5field-weighted citation impact, top 10% 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, 53 citations in OpenAlex.

  1. Review
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  10. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
    Article
  11. Article
  12. Review
  13. Mechanisms of mitochondrial respiratory adaptation.Nature reviews. Molecular cell biology · 2022
    Review
  14. Article
  15. Article
  16. Review
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  18. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  19. TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. 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

7 authors at 2 institutions in 1 country.

Cong WangDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Ricarda Richter-DennerleinDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0001-8904-1543
David Pacheu-GrauDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Fan LiuLeibniz-Forschungsinstitut for Molecular Pharmacology (FMP), Berlin, Germany.
Ying ZhuLeibniz-Forschungsinstitut for Molecular Pharmacology (FMP), Berlin, Germany.
Sven DennerleinDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0001-5661-5272
Universitätsmedizin Göttingen · DELeibniz Association · DE

Funding

Deutsche Forschungsgemeinschaft (DFG) EXC 2067/1-390729940European Research Council ERC ERCAdG No. 339580Leibniz AssociationMax Planck SocietyNiedersächsisches Ministerium für Wissenschaft und Kultur (MWK) FoP 88b
6 · The paper itself

Abstract

The mitochondrial genome encodes for thirteen core subunits of the oxidative phosphorylation system. These proteins assemble with imported proteins in a modular manner into stoichiometric enzyme complexes. Assembly factors assist in these biogenesis processes by providing co-factors or stabilizing transient assembly stages. However, how expression of the mitochondrial-encoded subunits is regulated to match the availability of nuclear-encoded subunits is still unresolved. Here, we address the function of MITRAC15/COA1, a protein that participates in complex I biogenesis and complex IV biogenesis. Our analyses of a MITRAC15 knockout mutant reveal that MITRAC15 is required for translation of the mitochondrial-encoded complex I subunit ND2. We find that MITRAC15 is a constituent of a ribosome-nascent chain complex during ND2 translation. Chemical crosslinking analyses demonstrate that binding of the ND2-specific assembly factor ACAD9 to the ND2 polypeptide occurs at the C-terminus and thus downstream of MITRAC15. Our analyses demonstrate that expression of the founder subunit ND2 of complex I undergoes regulation. Moreover, a ribosome-nascent chain complex with MITRAC15 is at the heart of this process.

Indexed as

Protein BiosynthesisRibosomesCell NucleusHEK293 CellsHumansMitochondriaMitochondrial ProteinsOxidative PhosphorylationMitochondrial Proteinscomplex Imitochondrianascent chaintranslation

Identifiers

PMID31721420
PMCPMC6945058
OpenAlexW2987809071

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.