ArticleScientific reports2016
Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 33 citations in OpenAlex.
- Cell-type-specific m1A dynamics are associated with microglial phenotypic transition and neuronal metabolic adaptation during spinal cord injury.PLoS computational biology · 2026Article
- TRMT6/61A-mediated tRNA m1A methylation promotes codon-dependent TAB2 translation and drives AML progression.Molecular medicine (Cambridge, Mass.) · 2026Article
- The RNA methylation modification as an immunometabolic regulatory hub in pancreatic cancer: from mechanistic insights to clinical translation perspectives.Molecular cancer · 2026Review
- WDR5-H3K4me3 Epigenetic Axis Promotes TRMT6-Dependent tRNA MAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- RNA Methylation in Cancer Metabolism: from Mechanisms to Therapeutic Opportunities.International journal of biological sciences · 2026Review
- RNA modifications in health and disease: from mechanistic insights to therapeutic applications.Precision clinical medicine · 2025Review
- The Secret Life of NJournal of molecular biology · 2025Review
- MoDorado: enhanced detection of tRNA modifications in nanopore sequencing by off-label use of modification callers.Nucleic acids research · 2025Article
- Evolutionary Dynamics of Plant TRM6/TRM61 Complexes.Plants (Basel, Switzerland) · 2025Article
- The highly conserved intron of tyrosine tRNA is critical forProceedings of the National Academy of Sciences of the United States of America · 2025Article
- tRNA m1A modification regulates cholesterol biosynthesis to promote antitumor immunity of CD8+ T cells.The Journal of experimental medicine · 2025Article
- Epigenetic regulation of RNA methylations in gastric cancer.Oncology reviews · 2025Review
- Writers, readers, and erasers RNA modifications and drug resistance in cancer.Molecular cancer · 2024Review
- RNA modifications in cellular metabolism: implications for metabolism-targeted therapy and immunotherapy.Signal transduction and targeted therapy · 2024Review
- The role of RNA modification in urological cancers: mechanisms and clinical potential.Discover oncology · 2023Review
- Different modification pathways for m1A58 incorporation in yeast elongator and initiator tRNAs.Nucleic acids research · 2023Article
- Epitranscriptomic Reprogramming Is Required to Prevent Stress and Damage from Acetaminophen.Genes · 2022Article
- NComputational and structural biotechnology journal · 2022Review
- Review
- The Arabidopsis TRM61/TRM6 complex is a bona fide tRNA N1-methyladenosine methyltransferase.Journal of experimental botany · 2020Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal β-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae.
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