Evidence map›Paper›PMID 24911101›Full record

ArticleACS chemical biology2014

Plant, animal, and fungal micronutrient queuosine is salvaged by members of the DUF2419 protein family.

Rémi Zallot, Céline Brochier-Armanet, Kirk W Gaston, Farhad Forouhar, Patrick A Limbach, John F Hunt, Valérie de Crécy-Lagard

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Macroevolutionary changes in natural selection on codon usage reflect evolution of the tRNA pool across a budding yeast subphylum.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. 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
  6. Dinucleotide preferences underlie apparent codon preference reversals in theProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Queuosine salvage inMicrobiology (Reading, England) · 2024
    Article
  11. Alternate routes to mnmJournal of bacteriology · 2024
    Article
  12. Queuosine Salvage inbioRxiv : the preprint server for biology · 2024
    Article
  13. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors at 5 institutions in 2 countries.

Rémi ZallotDepartment of Microbiology and Cell Science, University of Florida , Gainesville, Florida 32611, United States.
Céline Brochier-Armanet
Kirk W Gaston
Farhad Forouhar
Patrick A Limbach
John F Hunt
Valérie de Crécy-Lagard
University of Cincinnati · USUniversity of Florida · USColumbia University · USNew York Structural Biology Center · USUniversité Claude Bernard Lyon 1 · FR

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
NIGMS NIH HHS 2U54GM75026NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

Queuosine (Q) is a modification found at the wobble position of tRNAs with GUN anticodons. Although Q is present in most eukaryotes and bacteria, only bacteria can synthesize Q de novo. Eukaryotes acquire queuine (q), the free base of Q, from diet and/or microflora, making q an important but under-recognized micronutrient for plants, animals, and fungi. Eukaryotic type tRNA-guanine transglycosylases (eTGTs) are composed of a catalytic subunit (QTRT1) and a homologous accessory subunit (QTRTD1) forming a complex that catalyzes q insertion into target tRNAs. Phylogenetic analysis of eTGT subunits revealed a patchy distribution pattern in which gene losses occurred independently in different clades. Searches for genes co-distributing with eTGT family members identified DUF2419 as a potential Q salvage protein family. This prediction was experimentally validated in Schizosaccharomyces pombe by confirming that Q was present by analyzing tRNA(Asp) with anticodon GUC purified from wild-type cells and by showing that Q was absent from strains carrying deletions in the QTRT1 or DUF2419 encoding genes. DUF2419 proteins occur in most Eukarya with a few possible cases of horizontal gene transfer to bacteria. The universality of the DUF2419 function was confirmed by complementing the S. pombe mutant with the Zea mays (maize), human, and Sphaerobacter thermophilus homologues. The enzymatic function of this family is yet to be determined, but structural similarity with DNA glycosidases suggests a ribonucleoside hydrolase activity.

Indexed as

AnimalsFungiModels, MolecularNucleoside QPhylogenyPlantsProteinsNucleoside QProteins

Identifiers

PMID24911101
PMCPMC4136680
OpenAlexW2331155190

What OpenQuestion holds

Textmetadata
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.