Evidence map›Paper›PMID 31287866›Full record

ArticleNucleic acids research2019

Mammalian NSUN2 introduces 5-methylcytidines into mitochondrial tRNAs.

Saori Shinoda, Sho Kitagawa, Shinichi Nakagawa, Fan-Yan Wei, Kazuhito Tomizawa, Kimi Araki, Masatake Araki, Takeo Suzuki, Tsutomu Suzuki

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

77 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  7. Article
  8. NSUN7 is a catalytically inactive RNA mNature communications · 2025
    Article
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  10. Article
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  15. Article
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  18. NSUN2/ALYREF axis-driven mCancer immunology, immunotherapy : CII · 2025
    Article
  19. Review
  20. Article

17 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 1 country.

Saori ShinodaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Sho KitagawaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Shinichi NakagawaFaculty of Pharmaceutical Sciences, Hokkaido University, Hokkaido 060-0812, Japan.
Fan-Yan WeiDepartment of Molecular Physiology, Faculty of Life Sciences, Kumamoto University, Kumamoto 860-8556, Japan.
Kazuhito TomizawaDepartment of Molecular Physiology, Faculty of Life Sciences, Kumamoto University, Kumamoto 860-8556, Japan.
Kimi ArakiInstitute of Resource Development and Analysis, Kumamoto University, Kumamoto 860-0811, Japan.
Masatake ArakiInstitute of Resource Development and Analysis, Kumamoto University, Kumamoto 860-0811, Japan.
Takeo SuzukiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Tsutomu SuzukiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, the University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
The University of Tokyo · JPKumamoto University · JPHokkaido University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-transcriptional modifications in mitochondrial tRNAs (mt-tRNAs) play critical roles in mitochondrial protein synthesis, which produces respiratory chain complexes. In this study, we took advantage of mass spectrometric analysis to map 5-methylcytidine (m5C) at positions 48-50 in eight mouse and six human mt-tRNAs. We also confirmed the absence of m5C in mt-tRNAs isolated from Nsun2 knockout (KO) mice, as well as from NSUN2 KO human culture cells. In addition, we successfully reconstituted m5C at positions 48-50 of mt-tRNA in vitro with NSUN2 protein in the presence of S-adenosylmethionine. Although NSUN2 is predominantly localized to the nucleus and introduces m5C into cytoplasmic tRNAs and mRNAs, structured illumination microscopy clearly revealed NSUN2 foci inside mitochondria. These observations provide novel insights into the role of NSUN2 in the physiology and pathology of mitochondrial functions.

Indexed as

RNA Processing, Post-Transcriptional5-MethylcytosineAnimalsCRISPR-Cas SystemsFibroblastsGene EditingGene Knockout TechniquesHEK293 CellsHeLa CellsHumansMethylationMethyltransferasesMiceMice, KnockoutMitochondriaNucleic Acid Conformation5-MethylcytosineMethyltransferasesNSUN2 protein, humanNSUN3 protein, humanRNA, MessengerRNA, MitochondrialRNA, TransferS-Adenosylmethionine

Identifiers

PMID31287866
PMCPMC6895283
OpenAlexW2962401373

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.