Evidence map›Paper›PMID 26438534›Full record

ArticleNucleic acids research2015

Insights into molecular plasticity in protein complexes from Trm9-Trm112 tRNA modifying enzyme crystal structure.

Juliette Létoquart, Nhan van Tran, Vonny Caroline, Alexey Aleksandrov, Noureddine Lazar, Herman van Tilbeurgh, Dominique Liger, Marc Graille

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Mechanisms and rationales of SAM homeostasis.Trends in biochemical sciences · 2025
    Review
  2. tRNA modification enzyme-dependent redox homeostasis regulates synapse formation and memory.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Structures and mechanisms of the RNA mActa biochimica et biophysica Sinica · 2024
    Review
  4. Article
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  9. Article
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  11. Review
  12. Review
  13. Urm1: A Non-Canonical UBL.Biomolecules · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
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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

8 authors at 5 institutions in 1 country.

Juliette LétoquartLaboratoire de Biochimie, CNRS, UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France Fonction et Architecture des Assemblages Macromoléculaires, Département B3S, Institut de Biologie Intégrative de la Cellule (I2BC), CNRS, UMR 9198, CEA, Université Paris Sud, F-91405 Orsay Cedex, France.
Nhan van TranLaboratoire de Biochimie, CNRS, UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
Vonny CarolineLaboratoire de Biochimie, CNRS, UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
Alexey AleksandrovLaboratoire de Biochimie, CNRS, UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
Noureddine LazarFonction et Architecture des Assemblages Macromoléculaires, Département B3S, Institut de Biologie Intégrative de la Cellule (I2BC), CNRS, UMR 9198, CEA, Université Paris Sud, F-91405 Orsay Cedex, France.
Herman van TilbeurghFonction et Architecture des Assemblages Macromoléculaires, Département B3S, Institut de Biologie Intégrative de la Cellule (I2BC), CNRS, UMR 9198, CEA, Université Paris Sud, F-91405 Orsay Cedex, France.
Dominique LigerFonction et Architecture des Assemblages Macromoléculaires, Département B3S, Institut de Biologie Intégrative de la Cellule (I2BC), CNRS, UMR 9198, CEA, Université Paris Sud, F-91405 Orsay Cedex, France dominique.liger@i2bc.paris-saclay.fr.
Marc GrailleLaboratoire de Biochimie, CNRS, UMR 7654, Ecole Polytechnique, F-91128 Palaiseau Cedex, France Fonction et Architecture des Assemblages Macromoléculaires, Département B3S, Institut de Biologie Intégrative de la Cellule (I2BC), CNRS, UMR 9198, CEA, Université Paris Sud, F-91405 Orsay Cedex, France marc.graille@polytechnique.edu.
Centre National de la Recherche Scientifique · FRÉcole Polytechnique · FRInstitut de Biologie Intégrative de la Cellule · FRArchitecture et Fonction des Macromolécules Biologiques · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most of the factors involved in translation (tRNA, rRNA and proteins) are subject to post-transcriptional and post-translational modifications, which participate in the fine-tuning and tight control of ribosome and protein synthesis processes. In eukaryotes, Trm112 acts as an obligate activating platform for at least four methyltransferases (MTase) involved in the modification of 18S rRNA (Bud23), tRNA (Trm9 and Trm11) and translation termination factor eRF1 (Mtq2). Trm112 is then at a nexus between ribosome synthesis and function. Here, we present a structure-function analysis of the Trm9-Trm112 complex, which is involved in the 5-methoxycarbonylmethyluridine (mcm(5)U) modification of the tRNA anticodon wobble position and hence promotes translational fidelity. We also compare the known crystal structures of various Trm112-MTase complexes, highlighting the structural plasticity allowing Trm112 to interact through a very similar mode with its MTase partners, although those share less than 20% sequence identity.

Indexed as

BiocatalysisCatalytic DomainCrystallography, X-RayModels, MolecularSaccharomyces cerevisiae ProteinstRNA MethyltransferasesYarrowiaSaccharomyces cerevisiae ProteinsTrm112 protein, S cerevisiaeTRM9 protein, S cerevisiaetRNA Methyltransferases

Identifiers

PMID26438534
PMCPMC4678810
OpenAlexW2204243973

What OpenQuestion holds

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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.