Evidence map›Paper›PMID 33576519›Full record

ArticleThe EMBO journal2021

Interconnected assembly factors regulate the biogenesis of mitoribosomal large subunit.

Victor Tobiasson, Ondřej Gahura, Shintaro Aibara, Rozbeh Baradaran, Alena Zíková, Alexey Amunts

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  4. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. The late stages of yeast mitoribosome large subunit biogenesis.Biochimica et biophysica acta. Molecular cell research · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Mitoribosome Biogenesis.Methods in molecular biology (Clifton, N.J.) · 2023
    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

6 authors at 3 institutions in 2 countries.

Victor TobiassonScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden.ORCID 0000-0001-8920-017X
Ondřej GahuraInstitute of Parasitology, Biology Centre, Czech Academy of Sciences, Ceske Budejovice, Czech Republic.ORCID 0000-0002-2925-4763
Shintaro AibaraScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden.ORCID 0000-0003-2221-482X
Rozbeh BaradaranScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden.ORCID 0000-0002-6096-9169
Alena ZíkováInstitute of Parasitology, Biology Centre, Czech Academy of Sciences, Ceske Budejovice, Czech Republic.ORCID 0000-0002-8686-0225
Alexey AmuntsScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden.ORCID 0000-0002-5302-1740
Stockholm University · SEInstitute of Parasitology · CZUniversity of South Bohemia in České Budějovice · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitoribosomes consist of ribosomal RNA and protein components, coordinated assembly of which is critical for function. We used mitoribosomes from Trypanosoma brucei with reduced RNA and increased protein mass to provide insights into the biogenesis of the mitoribosomal large subunit. Structural characterization of a stable assembly intermediate revealed 22 assembly factors, some of which have orthologues/counterparts/homologues in mammalian genomes. These assembly factors form a protein network that spans a distance of 180 Å, shielding the ribosomal RNA surface. The central protuberance and L7/L12 stalk are not assembled entirely and require removal of assembly factors and remodeling of the mitoribosomal proteins to become functional. The conserved proteins GTPBP7 and mt-EngA are bound together at the subunit interface in proximity to the peptidyl transferase center. A mitochondrial acyl-carrier protein plays a role in docking the L1 stalk, which needs to be repositioned during maturation. Additional enzymatically deactivated factors scaffold the assembly while the exit tunnel is blocked. Together, this extensive network of accessory factors stabilizes the immature sites and connects the functionally important regions of the mitoribosomal large subunit.

Indexed as

Cryoelectron MicroscopyGTP-Binding ProteinsMitochondrial RibosomesProtein BindingProtein BiosynthesisProtein ConformationRibosome Subunits, LargeRNA, RibosomalTrypanosoma brucei bruceiGTP-Binding ProteinsRNA, Ribosomalassemblymitochondriamitoribosometranslationtrypanosoma

Identifiers

PMID33576519
PMCPMC7957421
OpenAlexW3126255965

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.