Evidence map›Paper›PMID 23836657›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

tRNA tKUUU, tQUUG, and tEUUC wobble position modifications fine-tune protein translation by promoting ribosome A-site binding.

Vanessa Anissa Nathalie Rezgui, Kshitiz Tyagi, Namit Ranjan, Andrey L Konevega, Joerg Mittelstaet, Marina V Rodnina, Matthias Peter, Patrick G A Pedrioli

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
7.3field-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

111 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. Review
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  4. Unconventional monooxygenation by the ONature chemical biology · 2026
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  5. tRNA modifications in viral replication.The Journal of biological chemistry · 2026
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  14. Article
  15. Article
  16. tRNA epitranscriptome determines pathogenicity of the opportunistic pathogenProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Review
  18. Article
  19. Article
  20. Article

51 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

8 authors at 3 institutions in 3 countries.

Vanessa Anissa Nathalie RezguiDepartment of Biology, Institute of Biochemistry, Eidgenössiche Technische Hochschule Zürich, 8093 Zürich, Switzerland.
Kshitiz Tyagi
Namit Ranjan
Andrey L Konevega
Joerg Mittelstaet
Marina V Rodnina
Matthias Peter
Patrick G A Pedrioli
Max Planck Institute for Biophysical Chemistry · DEUniversity of Dundee · GBPetersburg Nuclear Physics Institute · RU

Funding

Medical Research Council G1100713
6 · The paper itself

Abstract

tRNA modifications are crucial to ensure translation efficiency and fidelity. In eukaryotes, the URM1 and ELP pathways increase cellular resistance to various stress conditions, such as nutrient starvation and oxidative agents, by promoting thiolation and methoxycarbonylmethylation, respectively, of the wobble uridine of cytoplasmic (tK(UUU)), (tQ(UUG)), and (tE(UUC)). Although in vitro experiments have implicated these tRNA modifications in modulating wobbling capacity and translation efficiency, their exact in vivo biological roles remain largely unexplored. Using a combination of quantitative proteomics and codon-specific translation reporters, we find that translation of a specific gene subset enriched for AAA, CAA, and GAA codons is impaired in the absence of URM1- and ELP-dependent tRNA modifications. Moreover, in vitro experiments using native tRNAs demonstrate that both modifications enhance binding of tK(UUU) to the ribosomal A-site. Taken together, our data suggest that tRNA thiolation and methoxycarbonylmethylation regulate translation of genes with specific codon content.

Indexed as

Protein BiosynthesisBinding SitesCodonProteinsRibosomesRNA, MessengerRNA, TransferCodonProteinsRNA, MessengerRNA, TransferSILACsystems biologytranslation regulation

Identifiers

PMID23836657
PMCPMC3725067
OpenAlexW2006734870

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.