Evidence map›Paper›PMID 15096594›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp.

Daniel Y Dubois, Mickaël Blaise, Hubert D Becker, Valérie Campanacci, Gérard Keith, Richard Giegé, Christian Cambillau, Jacques Lapointe, Daniel Kern

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. An MD View of Ligand Binding.Molecules (Basel, Switzerland) · 2025
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  2. Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  4. Article
  5. Synthesis and Structure Elucidation of Glutamyl-Queuosine.Journal of the American Chemical Society · 2023
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Daniel Y DuboisDépartement de Biochimie et Microbiologie, Faculté de Sciences et de Génie, Centre de Recherche sur la Fonction, la Structure et l'Ingénierie des Protéines, Université Laval, Quebec, QC, Canada G1K 7P4.
Mickaël Blaise
Hubert D Becker
Valérie Campanacci
Gérard Keith
Richard Giegé
Christian Cambillau
Jacques Lapointe
Daniel Kern
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and the stem-contact fold. This GluRS-like protein, which lacks the anticodon-binding domain, does not use tRNA(Glu) as substrate in vitro nor in vivo, but aminoacylates tRNA(Asp) with glutamate. The yadB gene is expressed in wild-type E. coli as an operon with the dksA gene, which encodes a protein involved in the general stress response by means of its action at the translational level. The fate of the glutamylated tRNA(Asp) is not known, but its incapacity to bind elongation factor Tu suggests that it is not involved in ribosomal protein synthesis. Genes homologous to yadB are present only in bacteria, mostly in Proteobacteria. Sequence alignments and phylogenetic analyses show that the YadB proteins form a distinct monophyletic group related to the bacterial and organellar GluRSs (alpha-type GlxRSs superfamily) with ubiquitous function as suggested by the similar functional properties of the YadB homologue from Neisseria meningitidis.

Indexed as

Amino Acyl-tRNA SynthetasesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGlutamic AcidPeptide Elongation Factor 2PhylogenyProtein Structure, TertiaryRNA, MessengerRNA, Transfer, AspAmino Acyl-tRNA SynthetasesEscherichia coli ProteinsGlutamic AcidPeptide Elongation Factor 2RNA, MessengerRNA, Transfer, AspYadB protein, E coli

Identifiers

PMID15096594
PMCPMC419640
OpenAlexW1485553339

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.