Evidence map›Paper›PMID 28208632›Full record

ReviewBiomolecules2017

Cross-Talk between Dnmt2-Dependent tRNA Methylation and Queuosine Modification.

Ann E Ehrenhofer-Murray

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

46 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Unlocking the role of tRNA-derived fragments in shaping breast cancer signaling.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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
  11. Queuosine tRNA Modification: Connecting the Microbiome to the Translatome.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  18. Review
  19. Article
  20. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
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

1 author at 1 institution in 1 country.

Ann E Ehrenhofer-MurrayInstitut für Biologie, Humboldt-Universität zu Berlin, 10099 Berlin, Germany. ann.ehrenhofer-murray@hu-berlin.de.
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes of the Dnmt2 family of methyltransferases have yielded a number of unexpected discoveries. The first surprise came more than ten years ago when it was realized that, rather than being DNA methyltransferases, Dnmt2 enzymes actually are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. The second unanticipated finding was our recent discovery of a nutritional regulation of Dnmt2 in the fission yeast Schizosaccharomyces pombe. Significantly, the presence of the nucleotide queuosine in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro in S. pombe. Queuine, the respective base, is a hypermodified guanine analog that is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Interestingly, most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it themselves, but rather salvage it from food or from gut microbes. The queuine obtained from these sources comes from the breakdown of tRNAs, where the queuine ultimately was synthesized by bacteria. Queuine thus has been termed a micronutrient. This review summarizes the current knowledge of Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications. Models for the functional cooperation between these modifications and its wider implications are discussed.

Indexed as

AnimalsBacteriaDNA (Cytosine-5-)-MethyltransferasesGene Expression Regulation, FungalHumansMethylationNucleoside QRNA, TransferSchizosaccharomycesDNA (Cytosine-5-)-MethyltransferasesNucleoside QRNA, Transferanticodon modificationDnmt2epitranscriptomicsPmt1queuinequeuosinetranslationtRNA cleavage

Identifiers

PMID28208632
PMCPMC5372726
OpenAlexW2588394155

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.