ArticleRNA (New York, N.Y.)2011
Differentiating analogous tRNA methyltransferases by fragments of the methyl donor.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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.
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.
Who cites it
29 citing papers in PubMed.
- Connecting tRNA Charging and Decoding through the Axis of Nucleotide Modifications at Position 37.Journal of molecular biology · 2025Review
- A kinetic model for compound heterozygous pathogenic variants in Tyrosyl-tRNA synthetase gene YARS2-Associated neonatal phenotype.The Journal of biological chemistry · 2025Article
- Investigations of Single-Subunit tRNA Methyltransferases from Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- Chemical biology and medicinal chemistry of RNA methyltransferases.Nucleic acids research · 2022Article
- Novel heterozygous compound TRMT5 mutations associated with combined oxidative phosphorylation deficiency 26 in a Chinese family: a case report.BMC pediatrics · 2022Article
- Loss ofeLife · 2021Article
- Article
- MgACS catalysis · 2020Article
- Crystal structure and catalytic mechanism of the essential mRNA (New York, N.Y.) · 2019Article
- tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance.Cell systems · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Selective terminal methylation of a tRNA wobble base.Nucleic acids research · 2018Article
- Codon-Specific Translation by mFrontiers in genetics · 2018Article
- Structural insight into the methyltransfer mechanism of the bifunctional Trm5.Science advances · 2017Article
- Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m¹G37.Biomolecules · 2017Review
- Evolutionary Adaptation of the Essential tRNA Methyltransferase TrmD to the Signaling Molecule 3',5'-cAMP in Bacteria.The Journal of biological chemistry · 2017Article
- Methyl transfer by substrate signaling from a knotted protein fold.Nature structural & molecular biology · 2016Article
- Crystal structures of the bifunctional tRNA methyltransferase Trm5a.Scientific reports · 2016Article
- A novel HSD17B10 mutation impairing the activities of the mitochondrial RNase P complex causes X-linked intractable epilepsy and neurodevelopmental regression.RNA biology · 2016Article
- Single-Turnover Kinetics of Methyl Transfer to tRNA by Methyltransferases.Methods in molecular biology (Clifton, N.J.) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N(1) of G37, using catalytic motifs that share no sequence or structural homology. Here we show that natural and synthetic analogs of AdoMet are unable to distinguish TrmD from Trm5. Instead, fragments of AdoMet, adenosine and methionine, are selectively inhibitory of TrmD rather than Trm5. Detailed structural information of the two enzymes in complex with adenosine reveals how Trm5 escapes targeting by adopting an altered structure, whereas TrmD is trapped by targeting due to its rigid structure that stably accommodates the fragment. Free energy analysis exposes energetic disparities between the two enzymes in how they approach the binding of AdoMet versus fragments and provides insights into the design of inhibitors selective for TrmD.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.