Evidence map›Paper›PMID 24081582›Full record

ArticleNucleic acids research2014

Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate.

Zhenhua Shao, Wei Yan, Junhui Peng, Xiaobing Zuo, Yang Zou, Fudong Li, Deshun Gong, Rongsheng Ma, Jihui Wu, Yunyu Shi and 4 more

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 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mitochondrial RNA in Inflammation.International journal of biological sciences · 2025
    Review
  6. Article
  7. Article
  8. tRNA mbioRxiv : the preprint server for biology · 2023
    Article
  9. Review
  10. Natural product reports · 2023
    Review
  11. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  12. Review
  13. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  14. TheRNA (New York, N.Y.) · 2022
    Article
  15. Article
  16. Structural basis of RNA processing by human mitochondrial RNase P.Nature structural & molecular biology · 2021
    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

14 authors at 1 institution in 1 country.

Zhenhua ShaoHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China and X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60349, USA.
Wei Yan
Junhui Peng
Xiaobing Zuo
Yang Zou
Fudong Li
Deshun Gong
Rongsheng Ma
Jihui Wu
Yunyu Shi
Zhiyong Zhang
Maikun Teng
Xu Li
Qingguo Gong
University of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transfer RNA (tRNA) methylation is necessary for the proper biological function of tRNA. The N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which is widely identified in eukaryotes and archaea, was found to be catalyzed by the Trm10 family of methyltransferases (MTases). Here, we report the first crystal structures of the tRNA MTase spTrm10 from Schizosaccharomyces pombe in the presence and absence of its methyl donor product S-adenosyl-homocysteine (SAH) and its ortholog scTrm10 from Saccharomyces cerevisiae in complex with SAH. Our crystal structures indicated that the MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Furthermore, small angle X-ray scattering analysis reveals that Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. We also performed tRNA MTase assays and isothermal titration calorimetry experiments to investigate the catalytic mechanism of Trm10 in vitro. In combination with mutational analysis and electrophoretic mobility shift assays, our results provide insights into the substrate tRNA recognition mechanism of Trm10 family MTases.

Indexed as

Amino Acid SequenceBiocatalysisCatalytic DomainCrystallography, X-RayGuanineMethyltransferasesModels, MolecularMolecular Sequence DataRNA, TransferSaccharomyces cerevisiae ProteinsS-AdenosylhomocysteineS-AdenosylmethionineSchizosaccharomyces pombe ProteinstRNA MethyltransferasesGuanineMethyltransferasesRNA, TransferSaccharomyces cerevisiae ProteinsS-AdenosylhomocysteineS-AdenosylmethionineSchizosaccharomyces pombe ProteinsTRM10 protein, S cerevisiaeTrm10 protein, S pombetRNA Methyltransferases

Identifiers

PMID24081582
PMCPMC3874184
OpenAlexW2027173928

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Registered trials

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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.