ArticleNucleic acids research2017
Mechanistic features of the atypical tRNA m1G9 SPOUT methyltransferase, Trm10.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 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
- Characterization of the nucleolar localization signal of TRMT10A and its importance for the m1G9 methylation of tRNAs in mammalian cells.Journal of molecular cell biology · 2025Article
- Targeting tRNA methyltransferases: from molecular mechanisms to drug discovery.Science China. Life sciences · 2025Review
- Diversity in Biological Function and Mechanism of the tRNA Methyltransferase Trm10.Accounts of chemical research · 2023Article
- tRNA mbioRxiv : the preprint server for biology · 2023Article
- Investigations of Single-Subunit tRNA Methyltransferases from Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- The role of post-transcriptional modifications during development.Biologia futura · 2023Review
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- TheRNA (New York, N.Y.) · 2022Article
- RNA methylation in chloroplasts or mitochondria in plants.RNA biology · 2021Review
- Structural basis of RNA processing by human mitochondrial RNase P.Nature structural & molecular biology · 2021Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Coordination of mRNA and tRNA methylations by TRMT10A.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Interplay between substrate recognition, 5' end tRNA processing and methylation activity of human mitochondrial RNase P.RNA (New York, N.Y.) · 2019Article
- Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B.RNA (New York, N.Y.) · 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
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2 authors at 1 institution in 1 country.
Funding
Abstract
The tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout Eukarya and Archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a novel mechanism of catalysis. To investigate the mechanism of m1G9 methylation by Trm10, we performed a biochemical and kinetic analysis of Trm10 and variants with alterations in highly conserved residues, using crystal structures solved in the absence of tRNA as a guide. Here we demonstrate that a previously proposed general base residue (D210 in Saccharomyces cerevisiae Trm10) is not likely to play this suggested role in the chemistry of methylation. Instead, pH-rate analysis suggests that D210 and other conserved carboxylate-containing residues at the active site collaborate to establish an active site environment that promotes a single ionization that is required for catalysis. Moreover, Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD. These results provide evidence for a non-canonical tRNA methyltransferase mechanism that characterizes the Trm10 enzyme family.
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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.