Evidence map›Paper›PMID 37283053›Full record

ArticleNucleic acids research2023

N 2-methylguanosine modifications on human tRNAs and snRNA U6 are important for cell proliferation, protein translation and pre-mRNA splicing.

Can Wang, Nathalie Ulryck, Lydia Herzel, Nicolas Pythoud, Nicole Kleiber, Vincent Guérineau, Vincent Jactel, Chloé Moritz, Markus T Bohnsack, Christine Carapito and 3 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Integrative Analysis UncoversCurrent issues in molecular biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. tRNA mMolecular cancer · 2026
    Article
  10. Review
  11. NSUN7 is a catalytically inactive RNA mNature communications · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 2 countries.

Can WangLaboratoire de Biologie Structurale de la Cellule (BIOC), CNRS, École polytechnique, Institut Polytechnique de Paris, 91120 Palaiseau, France.
Nathalie UlryckLaboratoire de Biologie Structurale de la Cellule (BIOC), CNRS, École polytechnique, Institut Polytechnique de Paris, 91120 Palaiseau, France.
Lydia HerzelDepartment of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany.
Nicolas PythoudLaboratoire de Spectrométrie de Masse BioOrganique, CNRS, Université de Strasbourg, IPHC UMR 7178, Infrastructure Nationale de Protéomique ProFI, FR2048 Strasbourg, France.
Nicole KleiberDepartment of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany.
Vincent GuérineauUniversité Paris-Saclay, CNRS, Institut de Chimie des Substances Naturelles, UPR 2301, 91198 Gif-sur-Yvette, France.
Vincent JactelLaboratoire de Synthèse Organique (LSO), CNRS, École polytechnique, ENSTA, Institut Polytechnique de Paris, 91120 Palaiseau, France.
Chloé MoritzLaboratoire de Spectrométrie de Masse BioOrganique, CNRS, Université de Strasbourg, IPHC UMR 7178, Infrastructure Nationale de Protéomique ProFI, FR2048 Strasbourg, France.
Markus T BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany.ORCID 0000-0001-7063-5456
Christine CarapitoLaboratoire de Spectrométrie de Masse BioOrganique, CNRS, Université de Strasbourg, IPHC UMR 7178, Infrastructure Nationale de Protéomique ProFI, FR2048 Strasbourg, France.
David TouboulUniversité Paris-Saclay, CNRS, Institut de Chimie des Substances Naturelles, UPR 2301, 91198 Gif-sur-Yvette, France.
Katherine E BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany.ORCID 0000-0001-6035-4255
Marc GrailleLaboratoire de Biologie Structurale de la Cellule (BIOC), CNRS, École polytechnique, Institut Polytechnique de Paris, 91120 Palaiseau, France.ORCID 0000-0002-7853-5852
Centre National de la Recherche Scientifique · FRUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modified nucleotides in non-coding RNAs, such as tRNAs and snRNAs, represent an important layer of gene expression regulation through their ability to fine-tune mRNA maturation and translation. Dysregulation of such modifications and the enzymes installing them have been linked to various human pathologies including neurodevelopmental disorders and cancers. Several methyltransferases (MTases) are regulated allosterically by human TRMT112 (Trm112 in Saccharomyces cerevisiae), but the interactome of this regulator and targets of its interacting MTases remain incompletely characterized. Here, we have investigated the interaction network of human TRMT112 in intact cells and identify three poorly characterized putative MTases (TRMT11, THUMPD3 and THUMPD2) as direct partners. We demonstrate that these three proteins are active N2-methylguanosine (m2G) MTases and that TRMT11 and THUMPD3 methylate positions 10 and 6 of tRNAs, respectively. For THUMPD2, we discovered that it directly associates with the U6 snRNA, a core component of the catalytic spliceosome, and is required for the formation of m2G, the last 'orphan' modification in U6 snRNA. Furthermore, our data reveal the combined importance of TRMT11 and THUMPD3 for optimal protein synthesis and cell proliferation as well as a role for THUMPD2 in fine-tuning pre-mRNA splicing.

Indexed as

RNA PrecursorsSaccharomyces cerevisiae ProteinsCell ProliferationGuanosineHumansMethyltransferasesProtein BiosynthesisRNA, Small NuclearRNA SplicingSaccharomyces cerevisiaeSpliceosomestRNA Methyltransferases7-methylguanosineGuanosineMethyltransferasesRNA PrecursorsRNA, Small NuclearSaccharomyces cerevisiae ProteinsTrm112 protein, S cerevisiaeTRMT112 protein, humantRNA Methyltransferases

Identifiers

PMID37283053
PMCPMC10415138
OpenAlexW4379598455

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.