Evidence map›Paper›PMID 21693558›Full record

ArticleNucleic acids research2011

Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14.

Sheena Menezes, Kirk W Gaston, Kady L Krivos, Ethel E Apolinario, Norbert O Reich, Kevin R Sowers, Patrick A Limbach, John J Perona

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. The Landscape of tRNA Modifications in Archaea.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Distinct Modified Nucleosides in tRNAJournal of bacteriology · 2019
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

Sheena MenezesDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510, USA.
Kirk W Gaston
Kady L Krivos
Ethel E Apolinario
Norbert O Reich
Kevin R Sowers
Patrick A Limbach
John J Perona
University of Maryland, Baltimore County · USUniversity of California, Santa Barbara · US

Funding

UPLC for Enhanced Mass Spectrometry of Modified RNAsR01GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 1999 to 2025
$5.1M
Selectivity determinants in DNA restriction and modification enzymesR01GM053763 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PERONA, JOHN J. · 1996 to 2009
$1.8M
Mass Spectrometry of Ribosomal RNA:Protein InteractionsR56GM058843 · NIGMS · UNIVERSITY OF CINCINNATI · PI LIMBACH, PATRICK A · 2009 to 2009
$330k
NIGMS NIH HHS GM53763NIGMS NIH HHS GM58843NIGMS NIH HHS R01 GM053763NIGMS NIH HHS R01 GM058843NIGMS NIH HHS R56 GM058843
6 · The paper itself

Abstract

The modified nucleosides N(2)-methylguanosine and N(2)(2)-dimethylguanosine in transfer RNA occur at five positions in the D and anticodon arms, and at positions G6 and G7 in the acceptor stem. Trm1 and Trm11 enzymes are known to be responsible for several of the D/anticodon arm modifications, but methylases catalyzing post-transcriptional m(2)G synthesis in the acceptor stem are uncharacterized. Here, we report that the MJ0438 gene from Methanocaldococcus jannaschii encodes a novel S-adenosylmethionine-dependent methyltransferase, now identified as Trm14, which generates m(2)G at position 6 in tRNA(Cys). The 381 amino acid Trm14 protein possesses a canonical RNA recognition THUMP domain at the amino terminus, followed by a γ-class Rossmann fold amino-methyltransferase catalytic domain featuring the signature NPPY active site motif. Trm14 is associated with cluster of orthologous groups (COG) 0116, and most closely resembles the m(2)G10 tRNA methylase Trm11. Phylogenetic analysis reveals a canonical archaeal/bacterial evolutionary separation with 20-30% sequence identities between the two branches, but it is likely that the detailed functions of COG 0116 enzymes differ between the archaeal and bacterial domains. In the archaeal branch, the protein is found exclusively in thermophiles. More distantly related Trm14 homologs were also identified in eukaryotes known to possess the m(2)G6 tRNA modification.

Indexed as

Amino Acid SequenceArchaeal ProteinsBase SequenceBiocatalysisMethanococcalesMolecular Sequence DataPhylogenyRecombinant ProteinsRNA, TransferRNA, Transfer, CysSequence AlignmenttRNA MethyltransferasesArchaeal ProteinsRecombinant ProteinsRNA, TransferRNA, Transfer, CystRNA (guanine(10)-N(2))-dimethyltransferasetRNA Methyltransferases

Identifiers

PMID21693558
PMCPMC3177210
OpenAlexW1965478956

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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.