Evidence map›Paper›PMID 22941646›Full record

ArticleNucleic acids research2012

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

Elizabeth Wiltrout, Jeffrey M Goodenbour, Mathieu Fréchin, Tao Pan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Yeast adapts to diverse ecological niches driven by genomics and metabolic reprogramming.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  15. Translational control in aging and neurodegeneration.Wiley interdisciplinary reviews. RNA · 2021
    Review
  16. Article
  17. Review
  18. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    Review
  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

4 authors at 2 institutions in 2 countries.

Elizabeth WiltroutDepartment of Chemistry, University of Chicago, Chicago, Illinois 60637, USA.
Jeffrey M Goodenbour
Mathieu Fréchin
Tao Pan
University of Chicago · USUniversity of Zurich · CH

Funding

Predoctoral Training Program in Chemistry & BiologyT32GM008720 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 1999 to 2020
$4.7M
Mis-translation as a new mechanism of stress response in biologyDP1GM105386 · NIGMS · UNIVERSITY OF CHICAGO · PI PAN, TAO · 2012 to 2015
$3.1M
NCCDPHP CDC HHS DP1GM105386NIGMS NIH HHS DP1 GM105386NIGMS NIH HHS T32-GM008720
6 · The paper itself

Abstract

Accurate transfer RNA (tRNA) aminoacylation by aminoacyl-tRNA synthetases controls translational fidelity. Although tRNA synthetases are generally highly accurate, recent results show that the methionyl-tRNA synthetase (MetRS) is an exception. MetRS readily misacylates non-methionyl tRNAs at frequencies of up to 10% in mammalian cells; such mismethionylation may serve a beneficial role for cells to protect their own proteins against oxidative damage. The Escherichia coli MetRS mismethionylates two E. coli tRNA species in vitro, and these two tRNAs contain identity elements for mismethionylation. Here we investigate tRNA mismethionylation in Saccharomyces cerevisiae. tRNA mismethionylation occurs at a similar extent in vivo as in mammalian cells. Both cognate and mismethionylated tRNAs have similar turnover kinetics upon cycloheximide treatment. We identify specific arginine/lysine to methionine-substituted peptides in proteomic mass spectrometry, indicating that mismethionylated tRNAs are used in translation. The yeast MetRS is part of a complex containing the anchoring protein Arc1p and the glutamyl-tRNA synthetase (GluRS). The recombinant Arc1p-MetRS-GluRS complex binds and mismethionylates many tRNA species in vitro. Our results indicate that the yeast MetRS is responsible for extensive misacylation of non-methionyl tRNAs, and mismethionylation also occurs in this evolutionary branch.

Indexed as

Transfer RNA AminoacylationGlutamate-tRNA LigaseMethionineMethionine-tRNA LigaseProtein BiosynthesisRNA-Binding ProteinsRNA, TransferRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsARC1 protein, S cerevisiaeGlutamate-tRNA LigaseMethionineMethionine-tRNA LigaseRNA-Binding ProteinsRNA, TransferRNA, Transfer, Amino AcylSaccharomyces cerevisiae Proteins

Identifiers

PMID22941646
PMCPMC3488245
OpenAlexW2072334582

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.