Evidence map›Paper›PMID 38811035›Full record

ArticleNucleic acids research2024

A role for the S4-domain containing protein YlmH in ribosome-associated quality control in Bacillus subtilis.

Hiraku Takada, Helge Paternoga, Keigo Fujiwara, Jose A Nakamoto, Esther N Park, Lyudmila Dimitrova-Paternoga, Bertrand Beckert, Merilin Saarma, Tanel Tenson, Allen R Buskirk and 4 more

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  2. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  3. Article
  4. Article
  5. 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

14 authors.

Hiraku TakadaFaculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.ORCID 0000-0003-2034-5666
Helge PaternogaInstitute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.ORCID 0000-0001-8335-3239
Keigo FujiwaraFaculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.
Jose A NakamotoDepartment of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.
Esther N ParkDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Lyudmila Dimitrova-PaternogaInstitute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
Bertrand BeckertDubochet Center for Imaging (DCI) at EPFL, EPFL SB IPHYS DCI, Lausanne, Switzerland.
Merilin SaarmaUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.
Tanel TensonUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.
Allen R BuskirkDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0003-2720-6896
Gemma C AtkinsonDepartment of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.
Shinobu ChibaFaculty of Life Sciences, Kyoto Sangyo University and Institute for Protein Dynamics, Kamigamo, Motoyama, Kita-ku, Kyoto 603-8555, Japan.ORCID 0000-0003-3485-3477
Daniel N WilsonInstitute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.ORCID 0000-0003-3816-3828
Vasili HauryliukDepartment of Experimental Medical Science, Lund University, 221 00 Lund, Sweden.

Funding

The role of collisions in rescuing stalled ribosomes in bacteriaR01GM136960 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Allen Rowdon Buskirk · 2021 to 2026
$1.9M
Cancerfonden 20 0872 PjCentre for Structural Systems Biology, HamburgCrafoord foundation 20220562Deutsche Forschungsgemeinschaft WI3285/11-1DFG INST 152/772-1Estonian Research Council PRG335Institute for Fermentation, Osaka G-2021-2-063JSPS Grants-in-Aid for Scientific Research 20H05926JST, ACT X, Japan JP1159335Knut and Alice Wallenberg Foundation 2020-0037NIGMS NIH HHS R01 GM136960NIH HHS GM136960Swedish Research Council 2019-01085Umeå Centre for Microbial ResearchUniversität Hamburg
6 · The paper itself

Abstract

Ribosomes trapped on mRNAs during protein synthesis need to be rescued for the cell to survive. The most ubiquitous bacterial ribosome rescue pathway is trans-translation mediated by tmRNA and SmpB. Genetic inactivation of trans-translation can be lethal, unless ribosomes are rescued by ArfA or ArfB alternative rescue factors or the ribosome-associated quality control (RQC) system, which in Bacillus subtilis involves MutS2, RqcH, RqcP and Pth. Using transposon sequencing in a trans-translation-incompetent B. subtilis strain we identify a poorly characterized S4-domain-containing protein YlmH as a novel potential RQC factor. Cryo-EM structures reveal that YlmH binds peptidyl-tRNA-50S complexes in a position analogous to that of S4-domain-containing protein RqcP, and that, similarly to RqcP, YlmH can co-habit with RqcH. Consistently, we show that YlmH can assume the role of RqcP in RQC by facilitating the addition of poly-alanine tails to truncated nascent polypeptides. While in B. subtilis the function of YlmH is redundant with RqcP, our taxonomic analysis reveals that in multiple bacterial phyla RqcP is absent, while YlmH and RqcH are present, suggesting that in these species YlmH plays a central role in the RQC.

Indexed as

Bacillus subtilisBacterial ProteinsProtein BiosynthesisRibosomesCryoelectron MicroscopyModels, MolecularProtein BindingProtein DomainsRNA-Binding ProteinsRNA, Transfer, Amino AcylBacterial ProteinsRNA-Binding ProteinsRNA, Transfer, Amino AcyltRNA, peptidyl-

Identifiers

PMID38811035
PMCPMC11317155

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.