Evidence map›Paper›PMID 36762482›Full record

ArticleNucleic acids research2023

Identification of a novel 5-aminomethyl-2-thiouridine methyltransferase in tRNA modification.

Gyuhyeok Cho, Jangmin Lee, Jungwook Kim

Open 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. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. ThebioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Alternate routes to mnmJournal of bacteriology · 2024
    Article
  10. Article
  11. A tRNA modification inbioRxiv : the preprint server for biology · 2023
    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

3 authors at 1 institution in 1 country.

Gyuhyeok ChoDepartment of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Jangmin LeeDepartment of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.
Jungwook KimDepartment of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Korea.ORCID 0000-0001-5213-9299
Gwangju Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The uridine at the 34th position of tRNA, which is able to base pair with the 3'-end codon on mRNA, is usually modified to influence many aspects of decoding properties during translation. Derivatives of 5-methyluridine (xm5U), which include methylaminomethyl (mnm-) or carboxymethylaminomethyl (cmnm-) groups at C5 of uracil base, are widely conserved at the 34th position of many prokaryotic tRNAs. In Gram-negative bacteria such as Escherichia coli, a bifunctional MnmC is involved in the last two reactions of the biosynthesis of mnm5(s2)U, in which the enzyme first converts cmnm5(s2)U to 5-aminomethyl-(2-thio)uridine (nm5(s2)U) and subsequently installs the methyl group to complete the formation of mnm5(s2)U. Although mnm5s2U has been identified in tRNAs of Gram-positive bacteria and plants as well, their genomes do not contain an mnmC ortholog and the gene(s) responsible for this modification is unknown. We discovered that MnmM, previously known as YtqB, is the methyltransferase that converts nm5s2U to mnm5s2U in Bacillus subtilis through comparative genomics, gene complementation experiments, and in vitro assays. Furthermore, we determined X-ray crystal structures of MnmM complexed with anticodon stem loop of tRNAGln. The structures provide the molecular basis underlying the importance of U33-nm5s2U34-U35 as the key determinant for the specificity of MnmM.

Indexed as

Escherichia coli ProteinsMethyltransferasesMultienzyme ComplexesEscherichia coliRNA, TransferThiouridineUridine2-thiouridineEscherichia coli ProteinsMethyltransferasesMnmC protein, E coliMultienzyme ComplexesRNA, TransferThiouridineUridine

Identifiers

PMID36762482
PMCPMC9976899
OpenAlexW4319821960

What OpenQuestion holds

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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 OpenQuestion graph.