Evidence map›Paper›PMID 36480258›Full record

ArticleeLife2022

Structure of the mitoribosomal small subunit with streptomycin reveals Fe-S clusters and physiological molecules.

Yuzuru Itoh, Vivek Singh, Anas Khawaja, Andreas Naschberger, Minh Duc Nguyen, Joanna Rorbach, Alexey Amunts

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025
    Review
  11. Article
  12. Review
  13. Biallelic variants inmedRxiv : the preprint server for health sciences · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
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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

7 authors at 2 institutions in 1 country.

Yuzuru Itoh *Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Vivek Singh *Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID 0000-0003-4656-3362
Anas Khawaja *Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.ORCID 0000-0002-9721-7454
Andreas NaschbergerScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Minh Duc NguyenDepartment of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.ORCID 0000-0003-2945-9707
Joanna RorbachDepartment of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.ORCID 0000-0002-2891-2840
Alexey AmuntsScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-5302-1740
Stockholm University · SEKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitoribosome regulates cellular energy production, and its dysfunction is associated with aging. Inhibition of the mitoribosome can be caused by off-target binding of antimicrobial drugs and was shown to be coupled with a bilateral decreased visual acuity. Previously, we reported mitochondria-specific protein aspects of the mitoribosome, and in this article we present a 2.4-Å resolution structure of the small subunit in a complex with the anti-tuberculosis drug streptomycin that reveals roles of non-protein components. We found iron-sulfur clusters that are coordinated by different mitoribosomal proteins, nicotinamide adenine dinucleotide (NAD) associated with rRNA insertion, and posttranslational modifications. This is the first evidence of inter-protein coordination of iron-sulfur, and the finding of iron-sulfur clusters and NAD as fundamental building blocks of the mitoribosome directly links to mitochondrial disease and aging. We also report details of streptomycin interactions, suggesting that the mitoribosome-bound streptomycin is likely to be in hydrated gem-diol form and can be subjected to other modifications by the cellular milieu. The presented approach of adding antibiotics to cultured cells can be used to define their native structures in a bound form under more physiological conditions, and since streptomycin is a widely used drug for treatment, the newly resolved features can serve as determinants for targeting.

Indexed as

NADStreptomycinSulfurNADStreptomycinSulfuragingantibioticsFe–S clusterhumanmitochondriamitoribosomemolecular biophysicsstructural biologytranslation

Identifiers

PMID36480258
PMCPMC9731571
OpenAlexW4311575807

What OpenQuestion holds

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LicenceCC BY
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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.