Evidence map›Paper›PMID 25217588›Full record

ArticleNucleic acids research2014

Dynamics of RNA modification by a multi-site-specific tRNA methyltransferase.

Djemel Hamdane, Amandine Guelorget, Vincent Guérineau, Béatrice Golinelli-Pimpaneau

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 52 citations in OpenAlex.

  1. tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Distinct Modified Nucleosides in tRNAJournal of bacteriology · 2019
    Article
  10. Article
  11. Review
  12. RNA modification enzyme TruB is a tRNA chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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 4 institutions in 1 country.

Djemel HamdaneLaboratoire d'Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, CNRS, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France Laboratoire de Chimie des Processus Biologiques, Collège de France, CNRS, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France djemel.hamdane@college-de-france.fr.
Amandine GuelorgetLaboratoire d'Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, CNRS, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Vincent GuérineauInstitut de Chimie des Substances Naturelles, Centre de Recherche de Gif, CNRS, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Béatrice Golinelli-PimpaneauLaboratoire d'Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, CNRS, 1 avenue de la Terrasse, 91198 Gif-sur-Yvette, France Laboratoire de Chimie des Processus Biologiques, Collège de France, CNRS, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France beatrice.golinelli@college-de-france.fr.
Centre National de la Recherche Scientifique · FRCollège de France · FRLaboratoire de chimie des processus biologiques · FRLaboratoire d'Enzymologie et Biochimie Structurales · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In most organisms, the widely conserved 1-methyl-adenosine58 (m1A58) tRNA modification is catalyzed by an S-adenosyl-L-methionine (SAM)-dependent, site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation. To study this multi-site specificity, we used three oligoribonucleotide substrates of Pyrococcus abyssi TrmI (PabTrmI) containing a fluorescent 2-aminopurine (2-AP) at the two target positions and followed the RNA binding kinetics and methylation reactions by stopped-flow and mass spectrometry. PabTrmI did not modify 2-AP but methylated the adjacent target adenine. 2-AP seriously impaired the methylation of A57 but not A58, confirming that PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. PabTrmI binding provoked a rapid increase of fluorescence, attributed to base unstacking in the environment of 2-AP. Then, a slow decrease was observed only with 2-AP at position 57 and SAM, suggesting that m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of SAM and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the SAM pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by SAM without prior release of monomethylated tRNA.

Indexed as

2-AminopurineAdenineArchaeal ProteinsBase SequenceModels, MolecularPyrococcus abyssiRNA, Transfer, AspS-AdenosylmethionineSubstrate SpecificitytRNA Methyltransferases2-AminopurineAdenineArchaeal ProteinsRNA, Transfer, AspS-AdenosylmethioninetRNA Methyltransferases

Identifiers

PMID25217588
PMCPMC4191401
OpenAlexW2152300723

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.