Evidence map›Paper›PMID 20729861›Full record

ArticleNature structural & molecular biology2010

A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.

Tatsuo Yanagisawa, Tomomi Sumida, Ryohei Ishii, Chie Takemoto, Shigeyuki Yokoyama

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

83 citing papers in PubMed, 154 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
  3. Review
  4. Review
  5. Co-Translational Deposition of NAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
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  8. Article
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  13. Article
  14. Review
  15. Article
  16. Article
  17. Bacterial translation machinery for deliberate mistranslation of the genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020
    Review
  20. Frontiers in immunology · 2020
    Article

23 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

5 authors at 2 institutions in 2 countries.

Tatsuo YanagisawaRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama, Japan.
Tomomi Sumida
Ryohei Ishii
Chie Takemoto
Shigeyuki Yokoyama
Systems Biology Institute · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoacyl-tRNA synthetase (aaRS) paralogs with unknown functions exist in various species. We now report novel 'protein lysylation' by an Escherichia coli lysyl-tRNA synthetase paralog, GenX/PoxA/YjeA. X-ray crystallographic analysis shows that the structure of the GenX protein resembles that of a class II aaRS. Further in vitro studies reveal that it specifically aminoacylates EF-P with lysine. The shape of the protein substrate mimics that of the L-shaped tRNA, and its lysylation site corresponds to the tRNA 3' end. Thus, we show how the aaRS architecture can be adapted to achieve aminoacylation of a specific protein. Moreover, in vivo analyses reveal that the translation elongation factor P (EF-P) lysylation by GenX is enhanced by YjeK (lysine 2,3-aminomutase paralog), which is encoded next to the EF-P gene, and might convert alpha-lysyl-EF-P to beta-lysyl-EF-P. In vivo analyses indicate that the EF-P modification by GenX and YjeK is essential for cell survival.

Indexed as

AminoacylationAnimalsCrystallography, X-RayEscherichia coliHumansLysineLysine-tRNA LigaseModels, MolecularMutationPeptide Elongation FactorsPhylogenyProtein BindingProtein Processing, Post-TranslationalProtein Structure, QuaternaryProtein Structure, Tertiaryfactor EF-PLysineLysine-tRNA LigasePeptide Elongation Factors

Identifiers

PMID20729861
OpenAlexW2010693453

What OpenQuestion holds

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Registered trials

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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.