Evidence map›Paper›PMID 19332551›Full record

ArticleThe Journal of biological chemistry2009

Widespread distribution of cell defense against D-aminoacyl-tRNAs.

Sandra Wydau, Guillaume van der Rest, Caroline Aubard, Pierre Plateau, Sylvain Blanquet

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Mammalian Tolerance to Amino Acid Heterochirality.Chembiochem : a European journal of chemical biology · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    Review
  10. Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019
    Review
  11. Expanding the Scope of Protein Synthesis Using Modified Ribosomes.Journal of the American Chemical Society · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Emergence and evolution.Topics in current chemistry · 2014
    Review
  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

5 authors.

Sandra WydauLaboratoire de Biochimie and Laboratoire des Mécanismes Réactionnels, Ecole Polytechnique, CNRS, 91128 Palaiseau Cedex, France.
Guillaume van der Rest
Caroline Aubard
Pierre Plateau
Sylvain Blanquet

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several l-aminoacyl-tRNA synthetases can transfer a d-amino acid onto their cognate tRNA(s). This harmful reaction is counteracted by the enzyme d-aminoacyl-tRNA deacylase. Two distinct deacylases were already identified in bacteria (DTD1) and in archaea (DTD2), respectively. Evidence was given that DTD1 homologs also exist in nearly all eukaryotes, whereas DTD2 homologs occur in plants. On the other hand, several bacteria, including most cyanobacteria, lack genes encoding a DTD1 homolog. Here we show that Synechocystis sp. PCC6803 produces a third type of deacylase (DTD3). Inactivation of the corresponding gene (dtd3) renders the growth of Synechocystis sp. hypersensitive to the presence of d-tyrosine. Based on the available genomes, DTD3-like proteins are predicted to occur in all cyanobacteria. Moreover, one or several dtd3-like genes can be recognized in all cellular types, arguing in favor of the nearubiquity of an enzymatic function involved in the defense of translational systems against invasion by d-amino acids.

Indexed as

AminoacyltransferasesBiocatalysisChromosomes, BacterialComplex MixturesEscherichia coliGenes, BacterialGene SilencingIonsMetalsPhylogenyRNA, Transfer, Amino AcylSequence Homology, Amino AcidSubstrate SpecificitySynechocystisTyrosineAminoacyltransferasesComplex MixturesD-tyrosine tRNA(Tyr) deacylaseIonsMetalsRNA, Transfer, Amino AcylTyrosine

Identifiers

PMID19332551
PMCPMC2682858

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.