Evidence map›Paper›PMID 23258706›Full record

ArticleNucleic acids research2013

In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya.

Ludovic Perrochia, Estelle Crozat, Arnaud Hecker, Wenhua Zhang, Joseph Bareille, Bruno Collinet, Herman van Tilbeurgh, Patrick Forterre, Tamara Basta

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

57 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Epitranscriptome: Review of Top 25 Most-Studied RNA Modifications.International journal of molecular sciences · 2022
    Review
  14. Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022
    Review
  15. Nuclear Functions of KaeA, a Subunit of the KEOPS Complex inInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. 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

9 authors at 3 institutions in 1 country.

Ludovic PerrochiaInstitut de Génétique et Microbiologie, Université Paris-Sud, IFR115, UMR8621-CNRS, 91405 Orsay, France.
Estelle Crozat
Arnaud Hecker
Wenhua Zhang
Joseph Bareille
Bruno Collinet
Herman van Tilbeurgh
Patrick Forterre
Tamara Basta
Université Paris-Sud · FRCentre National de la Recherche Scientifique · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N(6)-threonylcarbamoyladenosine (t(6)A) is a modified nucleotide found in all transfer RNAs (tRNAs) decoding codons starting with adenosine. Its role is to facilitate codon-anticodon pairing and to prevent frameshifting during protein synthesis. Genetic studies demonstrated that two universal proteins, Kae1/YgjD and Sua5/YrdC, are necessary for t(6)A synthesis in Saccharomyces cerevisiae and Escherichia coli. In Archaea and Eukarya, Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS), together with three proteins that have no bacterial homologues. Here, we reconstituted for the first time an in vitro system for t(6)A modification in Archaea and Eukarya, using purified KEOPS and Sua5. We demonstrated binding of tRNAs to archaeal KEOPS and detected two distinct adenosine triphosphate (ATP)-dependent steps occurring in the course of the synthesis. Our data, together with recent reconstitution of an in vitro bacterial system, indicated that t(6)A cannot be catalysed by Sua5/YrdC and Kae1/YgjD alone but requires accessory proteins that are not universal. Remarkably, we observed interdomain complementation when bacterial, archaeal and eukaryotic proteins were combined in vitro, suggesting a conserved catalytic mechanism for the biosynthesis of t(6)A in nature. These findings shed light on the reaction mechanism of t(6)A synthesis and evolution of molecular systems that promote translation fidelity in present-day cells.

Indexed as

AdenosineAdenosine TriphosphateArchaeal ProteinsBacterial ProteinsBiocatalysisDNA-Binding ProteinsEndopeptidasesProtein KinasesPyrococcus abyssiRNA-Binding ProteinsRNA, TransferSaccharomyces cerevisiae ProteinsAdenosineAdenosine TriphosphateArchaeal ProteinsBacterial ProteinsDNA-Binding ProteinsEndopeptidasesKEOPS complex, S cerevisiaeN(6)-(N-threonylcarbonyl)adenosineProtein KinasesRNA-Binding ProteinsRNA, TransferSaccharomyces cerevisiae ProteinsSUA5 protein, S cerevisiae

Identifiers

PMID23258706
PMCPMC3561968
OpenAlexW2001329802

What OpenQuestion holds

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LicenceCC BY-NC
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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.