Evidence map›Paper›PMID 38943426›Full record

ArticleNucleic acids research2024

Resolution of ribosomal stalling by EF-P and ABCF ATPases YfmR and YkpA/YbiT.

Hiraku Takada, Keigo Fujiwara, Gemma C Atkinson, Shinobu Chiba, Vasili Hauryliuk

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

5 authors.

Hiraku TakadaFaculty of Life Sciences and Institute for Protein Dynamics, Kyoto Sangyo University, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.ORCID 0000-0003-2034-5666
Keigo FujiwaraFaculty of Life Sciences and Institute for Protein Dynamics, Kyoto Sangyo University, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.
Gemma C AtkinsonDepartment of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.
Shinobu ChibaFaculty of Life Sciences and Institute for Protein Dynamics, Kyoto Sangyo University, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.ORCID 0000-0003-3485-3477
Vasili HauryliukDepartment of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.ORCID 0000-0003-2389-5057

Funding

Cancerfonden 20 0872 PjCrafoord foundation 20220562Estonian Research Council PRG335Institute for Fermentation, Osaka G-2021-2-063JST, ACT X, Japan JP1159335Knut and Alice Wallenberg Foundation 2020-0037MEXT, JSPS Grant-in-Aid for Scientific Research 20H05926Swedish Research Council 2019-01085Umeå Centre for Microbial Research
6 · The paper itself

Abstract

Efficiency of protein synthesis on the ribosome is strongly affected by the amino acid composition of the assembled amino acid chain. Challenging sequences include proline-rich motifs as well as highly positively and negatively charged amino acid stretches. Members of the F subfamily of ABC ATPases (ABCFs) have been long hypothesised to promote translation of such problematic motifs. In this study we have applied genetics and reporter-based assays to characterise the four housekeeping ABCF ATPases of Bacillus subtilis: YdiF, YfmM, YfmR/Uup and YkpA/YbiT. We show that YfmR cooperates with the translation factor EF-P that promotes translation of Pro-rich motifs. Simultaneous loss of both YfmR and EF-P results in a dramatic growth defect. Surprisingly, this growth defect can be largely suppressed though overexpression of an EF-P variant lacking the otherwise crucial 5-amino-pentanolylated residue K32. Using in vivo reporter assays, we show that overexpression of YfmR can alleviate ribosomal stalling on Asp-Pro motifs. Finally, we demonstrate that YkpA/YbiT promotes translation of positively and negatively charged motifs but is inactive in resolving ribosomal stalls on proline-rich stretches. Collectively, our results provide insights into the function of ABCF translation factors in modulating protein synthesis in B. subtilis.

Indexed as

Bacillus subtilisBacterial ProteinsProtein BiosynthesisRibosomesAmino Acid MotifsATP-Binding Cassette TransportersPeptide Elongation FactorsATP-Binding Cassette TransportersBacterial Proteinsfactor EF-PPeptide Elongation Factors

Identifiers

PMID38943426
PMCPMC11381351

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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.