ArticleNucleic acids research2016
Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular basis of tRNA substrate recognition and modification by the atypical SPOUT methyltransferase Trm10.Nucleic acids research · 2026Article
- TRMT10A maintains lipid homeostasis independently of its tRNA mScience China. Life sciences · 2026Article
- Sulfolobales: Acidothermophilic archaea as models for biology and biotechnological applications.Engineering microbiology · 2026Review
- Optimized tRNA structure-seq reveals robust tRNA secondary structures inbioRxiv : the preprint server for biology · 2026Article
- Molecular basis of tRNA aminocarboxypropyl-transferase TapT for substrate recognition.Nucleic acids research · 2025Article
- Structural insight into the novel Thermus thermophilus SPOUT methyltransferase RlmR catalysing Um2552 formation in the 23S rRNA A-loop: a case of convergent evolution.Nucleic acids research · 2025Article
- Diversity in Biological Function and Mechanism of the tRNA Methyltransferase Trm10.Accounts of chemical research · 2023Article
- Investigations of Single-Subunit tRNA Methyltransferases from Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- tRNA mbioRxiv : the preprint server for biology · 2023Article
- Review
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- TheRNA (New York, N.Y.) · 2022Article
- Structure, dynamics, and molecular inhibition of the Staphylococcus aureus mThe Journal of biological chemistry · 2022Article
- Structural basis of RNA processing by human mitochondrial RNase P.Nature structural & molecular biology · 2021Article
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B.Nucleic acids research · 2020Article
- Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B.RNA (New York, N.Y.) · 2019Article
- Structural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK: insights into tRNA recognition.Nucleic acids research · 2019Article
- Matching tRNA modifications in humans to their known and predicted enzymes.Nucleic acids research · 2019Article
- A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.Biochemistry · 2019Article
- Insights into Catalytic and tRNA Recognition Mechanism of the Dual-Specific tRNA Methyltransferase fromGenes · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purine nucleosides on position 9 of eukaryal and archaeal tRNAs are frequently modified in vivo by the post-transcriptional addition of a methyl group on their N1 atom. The methyltransferase Trm10 is responsible for this modification in both these domains of life. While certain Trm10 orthologues specifically methylate either guanosine or adenosine at position 9 of tRNA, others have a dual specificity. Until now structural information about this enzyme family was only available for the catalytic SPOUT domain of Trm10 proteins that show specificity toward guanosine. Here, we present the first crystal structure of a full length Trm10 orthologue specific for adenosine, revealing next to the catalytic SPOUT domain also N- and C-terminal domains. This structure hence provides crucial insights in the tRNA binding mechanism of this unique monomeric family of SPOUT methyltransferases. Moreover, structural comparison of this adenosine-specific Trm10 orthologue with guanosine-specific Trm10 orthologues suggests that the N1 methylation of adenosine relies on additional catalytic residues.
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.