Evidence map›Paper›PMID 25219964›Full record

ArticleChemistry & biology2014

A divalent metal ion-dependent N(1)-methyl transfer to G37-tRNA.

Reiko Sakaguchi, Georges Lahoud, Thomas Christian, Howard Gamper, Ya-Ming Hou

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2014. 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
1.4field-weighted citation impact, top 20% 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, 31 citations in OpenAlex.

  1. Nicotinamide-Based Covalent Inhibitors of tRNA (mACS medicinal chemistry letters · 2026
    Article
  2. Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. tRNA mbioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Review
  9. Structural and functional characterization of TrmM in mProtein science : a publication of the Protein Society · 2022
    Article
  10. Loss ofeLife · 2021
    Article
  11. MgACS catalysis · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Codon-Specific Translation by mFrontiers in genetics · 2018
    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

5 authors at 1 institution in 1 country.

Reiko SakaguchiDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10(th) Street, BLSB 220, Philadelphia, PA 19107, USA.
Georges LahoudDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10(th) Street, BLSB 220, Philadelphia, PA 19107, USA.
Thomas ChristianDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10(th) Street, BLSB 220, Philadelphia, PA 19107, USA.
Howard GamperDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10(th) Street, BLSB 220, Philadelphia, PA 19107, USA.
Ya-Ming HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10(th) Street, BLSB 220, Philadelphia, PA 19107, USA. Electronic address: ya-ming.hou@jefferson.edu.
Thomas Jefferson University · US

Funding

FUNCTIONS OF tRNA MODIFICATIONSR01GM081601 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2008 to 2011
$1.3M
Probes for a tRNA modification enzymeU01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2016
$603k
Probes for a tRNA modification enzymeR01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2014 to 2014
$295k
NIGMS NIH HHS GM081601NIGMS NIH HHS R01 GM081601NIGMS NIH HHS R01 GM108972NIGMS NIH HHS U01 GM108972
6 · The paper itself

Abstract

The catalytic mechanism of the majority of S-adenosyl methionine (AdoMet)-dependent methyl transferases requires no divalent metal ions. Here we report that methyl transfer from AdoMet to N(1) of G37-tRNA, catalyzed by the bacterial TrmD enzyme, is strongly dependent on divalent metal ions and that Mg(2+) is the most physiologically relevant. Kinetic isotope analysis, metal rescue, and spectroscopic measurements indicate that Mg(2+) is not involved in substrate binding, but in promoting methyl transfer. On the basis of the pH-activity profile indicating one proton transfer during the TrmD reaction, we propose a catalytic mechanism in which the role of Mg(2+) is to help to increase the nucleophilicity of N(1) of G37 and stabilize the negative developing charge on O(6) during attack on the methyl sulfonium of AdoMet. This work demonstrates how Mg(2+) contributes to the catalysis of AdoMet-dependent methyl transfer in one of the most crucial posttranscriptional modifications to tRNA.

Indexed as

BiocatalysisEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationIonsKineticsMagnesiumMetalsRNA, TransferS-AdenosylmethioninetRNA MethyltransferasesEscherichia coli ProteinsIonsMagnesiumMetalsRNA, TransferS-AdenosylmethionineTrmD protein, E colitRNA Methyltransferases

Identifiers

PMID25219964
PMCPMC4224600
OpenAlexW1963614491

What OpenQuestion holds

Textmetadata
LicenceTDM
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.