ArticleNucleic acids research2000
The human tRNA(m(2)(2)G(26))dimethyltransferase: functional expression and characterization of a cloned hTRM1 gene.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 70 citations in OpenAlex.
- tRNA modifications in cancer: from molecular mechanisms to clinical translation.Biomarker research · 2026Review
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- Neurogenetic Disorders with Hearing Loss: Mechanisms, Classifications, and Emerging Insights.Current neurology and neuroscience reports · 2025Review
- Mammalian Queuosine tRNA Modification Impacts Translation to Enhance Cell Proliferation and MHC-II Expression.Journal of molecular biology · 2025Article
- Bi-allelic pathogenic variants in TRMT1 disrupt tRNA modification and induce a neurodevelopmental disorder.American journal of human genetics · 2025Article
- Human TRMT1 and TRMT1L paralogs ensure the proper modification state, stability, and function of tRNAs.Cell reports · 2025Article
- TRMT1L-catalyzed mCell reports · 2025Article
- TRMT1L-catalyzed mbioRxiv : the preprint server for biology · 2024Article
- A tRNA-modifying enzyme facilitates RNase P activity in Arabidopsis nuclei.Nature plants · 2023Article
- Investigations of Single-Subunit tRNA Methyltransferases from Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- Human TRMT1 catalyzes mScience China. Life sciences · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Conditional Covalent Lethality Driven by Oncometabolite Accumulation.ACS chemical biology · 2022Article
- Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases.Nature communications · 2022Article
- SARS-CoV-2 Infection, Sex-Related Differences, and a Possible Personalized Treatment Approach with Valproic Acid: A Review.Biomedicines · 2022Review
- Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications.The FEBS journal · 2021Review
- Subcellular relocalization and nuclear redistribution of the RNA methyltransferases TRMT1 and TRMT1L upon neuronal activation.RNA biology · 2021Article
- Integrated genomic analysis reveals regulatory pathways and dynamic landscapes of the tRNA transcriptome.Scientific reports · 2021Article
- Combined exposure to polychlorinated biphenyls and high-fat diet modifies the global epitranscriptomic landscape in mouse liver.Environmental epigenetics · 2021Article
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B.Nucleic acids research · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This paper presents the first example of a complete gene sequence coding for and expressing a biologically functional human tRNA methyltransferase: the hTRM1 gene product tRNA(m(2)(2)G)dimethyltransferase. We isolated a human cDNA (1980 bp) made from placental mRNA coding for the full-length (659 amino acids) human TRM1 polypeptide. The sequence was fairly similar to Saccharomyces cerevisiae Trm1p, to Caenorhabditis elegans TRM1p and to open reading frames (ORFs) found in mouse and a plant (Arabidopsis thaliana) DNA. The human TRM1 gene was expressed at low temperature in Escherichia coli as a functional recombinant protein, able to catalyze the formation of dimethylguanosine in E.coli tRNA in vivo. It targeted solely position G(26) in T7 transcribed spliced and unspliced human tRNA(Tyr) in vitro and in yeast trm1 mutant tRNA. Thus, the human TRM1 protein is a tRNA(m(2)(2)G(26))dimethyltransferase. Compared with yeast Trm1p, hTRM1p has a C-terminal protrusion of approximately 90 amino acids which shows similarities to a mouse protein related to RNA splicing. A deletion of these 90 C-terminal amino acids left the modification activity in vitro intact. Among point mutations in the hTRM1 gene, only those located in conserved regions of hTRM1p completely eliminated modification activity.
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