Evidence map›Paper›PMID 30010922›Full record

ArticleNucleic acids research2018

Evolutionary insights into Trm112-methyltransferase holoenzymes involved in translation between archaea and eukaryotes.

Nhan van Tran, Leslie Muller, Robert L Ross, Roxane Lestini, Juliette Létoquart, Nathalie Ulryck, Patrick A Limbach, Valérie de Crécy-Lagard, Sarah Cianférani, Marc Graille

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-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

33 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. The Landscape of tRNA Modifications in Archaea.bioRxiv : the preprint server for biology · 2025
    Article
  4. Journal of bacteriology · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. METTLing in Stem Cell and Cancer Biology.Stem cell reviews and reports · 2023
    Review
  11. Article
  12. Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

10 authors at 6 institutions in 2 countries.

Nhan van TranLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, F-91128 Palaiseau cedex, France.
Leslie MullerLaboratoire de Spectrométrie de Masse BioOrganique (LSMBO), Université de Strasbourg, CNRS, IPHC UMR 7178, F-67000 Strasbourg, France.
Robert L RossRieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati, P.O. Box 210172, Cincinnati, OH 45221-0172, USA.
Roxane LestiniLaboratoire d'Optique et Biosciences, Ecole Polytechnique, CNRS UMR7645-INSERM U1182 91128, Palaiseau Cedex, France.
Juliette LétoquartLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, F-91128 Palaiseau cedex, France.
Nathalie UlryckLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, F-91128 Palaiseau cedex, France.
Patrick A LimbachRieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati, P.O. Box 210172, Cincinnati, OH 45221-0172, USA.
Valérie de Crécy-LagardDepartment of Microbiology and Cell Science, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, FL 32611, USA.
Sarah CianféraniLaboratoire de Spectrométrie de Masse BioOrganique (LSMBO), Université de Strasbourg, CNRS, IPHC UMR 7178, F-67000 Strasbourg, France.
Marc GrailleLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, F-91128 Palaiseau cedex, France.
Centre National de la Recherche Scientifique · FRUniversité Paris-Saclay · FRUniversity of Cincinnati · USInserm · FRUniversité de Strasbourg · FRUniversity of Florida · US

Funding

Synthesis and function of Queuosine in BacteriaR01GM070641 · NIGMS · UNIVERSITY OF FLORIDA · PI DE CRECY-LAGARD, VALERIE A · 2006 to 2023
$5.3M
UPLC for Enhanced Mass Spectrometry of Modified RNAsR01GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 1999 to 2025
$5.1M
NIGMS NIH HHS R01 GM058843NIGMS NIH HHS R01 GM070641
6 · The paper itself

Abstract

Protein synthesis is a complex and highly coordinated process requiring many different protein factors as well as various types of nucleic acids. All translation machinery components require multiple maturation events to be functional. These include post-transcriptional and post-translational modification steps and methylations are the most frequent among these events. In eukaryotes, Trm112, a small protein (COG2835) conserved in all three domains of life, interacts and activates four methyltransferases (Bud23, Trm9, Trm11 and Mtq2) that target different components of the translation machinery (rRNA, tRNAs, release factors). To clarify the function of Trm112 in archaea, we have characterized functionally and structurally its interaction network using Haloferax volcanii as model system. This led us to unravel that methyltransferases are also privileged Trm112 partners in archaea and that this Trm112 network is much more complex than anticipated from eukaryotic studies. Interestingly, among the identified enzymes, some are functionally orthologous to eukaryotic Trm112 partners, emphasizing again the similarity between eukaryotic and archaeal translation machineries. Other partners display some similarities with bacterial methyltransferases, suggesting that Trm112 is a general partner for methyltransferases in all living organisms.

Indexed as

RNA Processing, Post-TranscriptionalArchaeal ProteinsBacterial ProteinsCrystallography, X-RayDatasets as TopicEnzyme ActivationEukaryotic CellsEvolution, MolecularHaloferax volcaniiHoloenzymesImmunoprecipitationMass SpectrometryMethylationModels, MolecularProtein BindingProtein ConformationArchaeal ProteinsBacterial ProteinsHoloenzymesRecombinant ProteinstRNA Methyltransferases

Identifiers

PMID30010922
PMCPMC6144793
OpenAlexW2884309310

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.