ArticleNucleic acids research2019
Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 26 citations in OpenAlex.
- Molecular basis of tRNA substrate recognition and modification by the atypical SPOUT methyltransferase Trm10.Nucleic acids research · 2026Article
- Review
- Optimized tRNA structure-seq reveals robust tRNA secondary structures inbioRxiv : the preprint server for biology · 2026Article
- Structural insights into tRNA recognition of the human FTSJ1-THADA complex.Communications biology · 2025Article
- Exquisite Complex Reaction Cascade in the Natural 1,2,4-Triazine Assembly.Journal of the American Chemical Society · 2025Article
- Identification of Amino Acids in Trm734 Required for 2'-ACS omega · 2024Article
- Transcriptional Reprogramming ofJournal of fungi (Basel, Switzerland) · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Review
- Identification of a Trm732 Motif Required for 2'-ACS omega · 2022Article
- Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022Article
- Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications.The FEBS journal · 2021Review
- Modifications of the human tRNA anticodon loop and their associations with genetic diseases.Cellular and molecular life sciences : CMLS · 2021Review
- The occurrence order and cross-talk of different tRNA modifications.Science China. Life sciences · 2021Review
- Intellectual disability-associated gene ftsj1 is responsible for 2'-O-methylation of specific tRNAs.EMBO reports · 2020Article
- Methods, development and applications of small-angle X-ray scattering to characterize biological macromolecules in solution.Current research in structural biology · 2020Review
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8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complex between Trm7 and Trm734 (Trm7-Trm734) from Saccharomyces cerevisiae catalyzes 2'-O-methylation at position 34 in tRNA. We report biochemical and structural studies of the Trm7-Trm734 complex. Purified recombinant Trm7-Trm734 preferentially methylates tRNAPhe transcript variants possessing two of three factors (Cm32, m1G37 and pyrimidine34). Therefore, tRNAPhe, tRNATrp and tRNALeu are specifically methylated by Trm7-Trm734. We have solved the crystal structures of the apo and S-adenosyl-L-methionine bound forms of Trm7-Trm734. Small angle X-ray scattering reveals that Trm7-Trm734 exists as a hetero-dimer in solution. Trm7 possesses a Rossmann-fold catalytic domain, while Trm734 consists of three WD40 β-propeller domains (termed BPA, BPB and BPC). BPA and BPC form a unique V-shaped cleft, which docks to Trm7. The C-terminal region of Trm7 is required for binding to Trm734. The D-arm of substrate tRNA is required for methylation by Trm7-Trm734. If the D-arm in tRNAPhe is docked onto the positively charged area of BPB in Trm734, the anticodon-loop is located near the catalytic pocket of Trm7. This model suggests that Trm734 is required for correct positioning of tRNA for methylation. Additionally, a point-mutation in Trm7, which is observed in FTSJ1 (human Trm7 ortholog) of nosyndromic X-linked intellectual disability patients, decreases the methylation activity.
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