Evidence map›Paper›PMID 30715423›Full record

ArticleNucleic acids research2019

Queuine links translational control in eukaryotes to a micronutrient from bacteria.

Martin Müller, Carine Legrand, Francesca Tuorto, Vincent P Kelly, Yaser Atlasi, Frank Lyko, Ann E Ehrenhofer-Murray

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.4field-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

66 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
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  5. EnterohemorrhagicmSystems · 2026
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  18. The oncogene SLC35F2 is a high-specificity transporter for the micronutrients queuine and queuosine.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Queuosine tRNA Modification: Connecting the Microbiome to the Translatome.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  20. Article

6 more citing papers are in PubMed but not listed here.

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 5 institutions in 3 countries.

Martin MüllerInstitut für Biologie, Molekulare Zellbiologie, Humboldt-Universität zu Berlin, Berlin, Germany.
Carine LegrandDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Francesca TuortoDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Vincent P KellySchool of Biochemistry & Immunology, Trinity Biomedical Sciences Institute, 152-160 Pearse Street, Trinity College Dublin, Dublin, Ireland.
Yaser AtlasiDepartment of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, Nijmegen, Netherlands.
Frank LykoDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Ann E Ehrenhofer-MurrayInstitut für Biologie, Molekulare Zellbiologie, Humboldt-Universität zu Berlin, Berlin, Germany.
DKFZ-ZMBH Alliance · DEHumboldt-Universität zu Berlin · DEHeidelberg University · DERadboud Institute for Molecular Life Sciences · NLTrinity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the wobble position of tRNA with a GUN anticodon is modified to the 7-deaza-guanosine derivative queuosine (Q34), but the original source of Q is bacterial, since Q is synthesized by eubacteria and salvaged by eukaryotes for incorporation into tRNA. Q34 modification stimulates Dnmt2/Pmt1-dependent C38 methylation (m5C38) in the tRNAAsp anticodon loop in Schizosaccharomyces pombe. Here, we show by ribosome profiling in S. pombe that Q modification enhances the translational speed of the C-ending codons for aspartate (GAC) and histidine (CAC) and reduces that of U-ending codons for asparagine (AAU) and tyrosine (UAU), thus equilibrating the genome-wide translation of synonymous Q codons. Furthermore, Q prevents translation errors by suppressing second-position misreading of the glycine codon GGC, but not of wobble misreading. The absence of Q causes reduced translation of mRNAs involved in mitochondrial functions, and accordingly, lack of Q modification causes a mitochondrial defect in S. pombe. We also show that Q-dependent stimulation of Dnmt2 is conserved in mice. Our findings reveal a direct mechanism for the regulation of translational speed and fidelity in eukaryotes by a nutrient originating from bacteria.

Indexed as

AnimalsAnticodonAsparagineDNA (Cytosine-5-)-MethyltransferasesDNA, MitochondrialEukaryotaGuanineMethylationMiceMicronutrientsProtein BiosynthesisRibosomesRNA, TransferSchizosaccharomycesSchizosaccharomyces pombe ProteinsTyrosine7-deazaguanineAnticodonAsparagineDNA (Cytosine-5-)-MethyltransferasesDNA, MitochondrialDnmt2 protein, mouseGuanineMicronutrientsPmt1 protein, S pombequeuineRNA, TransferSchizosaccharomyces pombe ProteinsTyrosine

Identifiers

PMID30715423
PMCPMC6468285
OpenAlexW2912327202

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.