Evidence map›Paper›PMID 30093495›Full record

ArticleThe EMBO journal2018

Queuosine-modified tRNAs confer nutritional control of protein translation.

Francesca Tuorto, Carine Legrand, Cansu Cirzi, Giuseppina Federico, Reinhard Liebers, Martin Müller, Ann E Ehrenhofer-Murray, Gunnar Dittmar, Hermann-Josef Gröne, Frank Lyko

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

123 citing papers in PubMed, 198 citations in OpenAlex.

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63 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

10 authors at 3 institutions in 2 countries.

Francesca TuortoDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany f.tuorto@dkfz.de.ORCID 0000-0003-1625-1181
Carine LegrandDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Cansu CirziDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Giuseppina FedericoDepartment of Cellular and Molecular Pathology, German Cancer Research Center, Heidelberg, Germany.
Reinhard LiebersDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.
Martin MüllerInstitut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany.
Ann E Ehrenhofer-MurrayInstitut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0001-8709-1942
Gunnar DittmarProteome and Genome Research Unit, Department of Oncology, Luxembourg Institute of Health, Luxembourg, Luxembourg.ORCID 0000-0003-3647-8623
Hermann-Josef GröneDepartment of Cellular and Molecular Pathology, German Cancer Research Center, Heidelberg, Germany.
Frank LykoDivision of Epigenetics, DKFZ-ZMBH Alliance, German Cancer Research Center, Heidelberg, Germany.ORCID 0000-0002-4873-5431
German Cancer Research Center · DEHumboldt-Universität zu Berlin · DELuxembourg Institute of Health · LU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Global protein translation as well as translation at the codon level can be regulated by tRNA modifications. In eukaryotes, levels of tRNA queuosinylation reflect the bioavailability of the precursor queuine, which is salvaged from the diet and gut microbiota. We show here that nutritionally determined Q-tRNA levels promote Dnmt2-mediated methylation of tRNA Asp and control translational speed of Q-decoded codons as well as at near-cognate codons. Deregulation of translation upon queuine depletion results in unfolded proteins that trigger endoplasmic reticulum stress and activation of the unfolded protein response, both in cultured human cell lines and in germ-free mice fed with a queuosine-deficient diet. Taken together, our findings comprehensively resolve the role of this anticodon tRNA modification in the context of native protein translation and describe a novel mechanism that links nutritionally determined modification levels to effective polypeptide synthesis and cellular homeostasis.

Indexed as

Endoplasmic Reticulum StressFood, FormulatedRNA Processing, Post-TranscriptionalUnfolded Protein ResponseAnimalsDNA (Cytosine-5-)-MethyltransferasesHCT116 CellsHeLa CellsHumansMiceNucleoside QRNA, Transfer, AspDNA (Cytosine-5-)-MethyltransferasesDnmt2 protein, mouseNucleoside QRNA, Transfer, AspTRDMT1 protein, humancytosine‐5 methylationprotein translationqueuosinetRNA modificationsunfolded protein response

Identifiers

PMID30093495
PMCPMC6138434
OpenAlexW2886330525

What OpenQuestion holds

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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.