ArticleNucleic acids research2017
Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 31 citations in OpenAlex.
- Guanosine 10 methylation by TRMT11-TRMT112 optimizes human mitochondrial tRNAs for efficient translation.Nucleic acids research · 2026Article
- tRNA methylation: functional insights and epitranscriptomic regulation.Cell communication and signaling : CCS · 2026Review
- 2'-O-methylation-dependent installation of NNature communications · 2026Article
- The Rare RNA Methylations m²G, Cm, m⁵U and ms²i⁶A: Roles in Disease Pathogenesis and Emerging Therapeutic Implications.International journal of medical sciences · 2026Review
- A transfer RNA methyltransferase with an unusual domain composition catalyzes 2'-O-methylation at position 6 in tRNA.Nucleic acids research · 2025Article
- Dysregulation of tRNA methylation in cancer: Mechanisms and targeting therapeutic strategies.Cell death discovery · 2024Review
- Activity reconstitution of Kre33 and Tan1 reveals a molecular ruler mechanism in eukaryotic tRNA acetylation.Nucleic acids research · 2024Article
- Multifaceted roles of t6A biogenesis in efficiency and fidelity of mitochondrial gene expression.Nucleic acids research · 2024Article
- N 2-methylguanosine modifications on human tRNAs and snRNA U6 are important for cell proliferation, protein translation and pre-mRNA splicing.Nucleic acids research · 2023Article
- Coordination of RNA modifications in the brain and beyond.Molecular psychiatry · 2023Review
- Review
- Overexpression of 18S rRNA methyltransferase CrBUD23 enhances biomass and lutein content inFrontiers in bioengineering and biotechnology · 2023Article
- Human Thg1 displays tRNA-inducible GTPase activity.Nucleic acids research · 2022Article
- Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022Article
- Human TRMT112-Methyltransferase Network Consists of Seven Partners Interacting with a Common Co-Factor.International journal of molecular sciences · 2021Article
- THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.Nucleic acids research · 2021Article
- A comprehensive review of m6A/m6Am RNA methyltransferase structures.Nucleic acids research · 2021Review
- Structural and functional insights into Archaeoglobus fulgidus m2G10 tRNA methyltransferase Trm11 and its Trm112 activator.Nucleic acids research · 2020Article
- Distinct Modified Nucleosides in tRNAJournal of bacteriology · 2019Article
- The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112.Nucleic acids research · 2019Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-transcriptional and post-translational modifications of factors involved in translation are very important for the control and accuracy of protein biosynthesis. Among these factors, tRNAs harbor the largest variety of grafted chemical structures, which participate in tRNA stability or mRNA decoding. Here, we focused on Trm112 protein, which associates with four different eukaryotic methyltransferases modifying tRNAs (Trm9 and Trm11) but also 18S-rRNA (Bud23) and translation termination factor eRF1 (Mtq2). In particular, we have investigated the role of Trm112 in the Trm11-Trm112 complex, which forms 2-methylguanosine at position 10 on several tRNAs and thereby is assumed to stabilize tRNA structure. We show that Trm112 is important for Trm11 enzymatic activity by influencing S-adenosyl-L-methionine binding and by contributing to tRNA binding. Using hydrogen-deuterium eXchange coupled to mass spectrometry, we obtained experimental evidences that the Trm11-Trm112 interaction relies on the same molecular bases as those described for other Trm112-methyltransferases complexes. Hence, all Trm112-dependent methyltransferases compete to interact with this partner.
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