ArticleNucleic acids research2013
Identification of a novel methyltransferase, Bmt2, responsible for the N-1-methyl-adenosine base modification of 25S rRNA in Saccharomyces cerevisiae.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled it.
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68 citing papers in PubMed, 1 synthesis or guideline pooled it, 100 citations in OpenAlex.
- Emerging Role of Epitranscriptomics in Diabetes Mellitus and Its Complications.Frontiers in endocrinology · 2022Pooled it
- Origins of Reactivity in SAM-Utilizing Ribozyme SAMURI-Catalyzed RNA Alkylation.Journal of the American Chemical Society · 2026Article
- RNA mCancer communications (London, England) · 2025Article
- Evolutionary Dynamics of Plant TRM6/TRM61 Complexes.Plants (Basel, Switzerland) · 2025Article
- Epitranscriptomic signatures in blood: emerging biomarkers for diagnosis of diabetes and its complications.Frontiers in cell and developmental biology · 2025Review
- Pan-cancer analysis of m1A writer gene RRP8: implications for immune infiltration and prognosis in human cancers.Discover oncology · 2024Article
- Review
- Epitranscriptomic Regulations in the Heart.Physiological research · 2024Review
- The Molecular Basis of Human ALKBH3 Mediated RNA NAngewandte Chemie (International ed. in English) · 2024Article
- Research progress of N1-methyladenosine RNA modification in cancer.Cell communication and signaling : CCS · 2024Review
- The role of RNA modification in urological cancers: mechanisms and clinical potential.Discover oncology · 2023Review
- Novel insight into RNA modifications in tumor immunity: Promising targets to prevent tumor immune escape.Innovation (Cambridge (Mass.)) · 2023Review
- The covalent nucleotide modifications within plant mRNAs: What we know, how we find them, and what should be done in the future.The Plant cell · 2023Article
- Catalytic mechanism and pH dependence of a methyltransferase ribozyme (MTR1) from computational enzymology.Nucleic acids research · 2023Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- The roles of N6-methyladenosine and its target regulatory noncoding RNAs in tumors: classification, mechanisms, and potential therapeutic implications.Experimental & molecular medicine · 2023Review
- ALKBH1-mediated mMolecular oncology · 2023Article
- RNA Modifications in Hematologic Malignancies.Cancer treatment and research · 2023Article
- Targeted Quantitative Profiling of Epitranscriptomic Reader, Writer, and Eraser Proteins Using Stable Isotope-Labeled Peptides.Analytical chemistry · 2022Article
- Predicting genes associated with RNA methylation pathways using machine learning.Communications biology · 2022Article
8 more citing papers are in PubMed but not listed here.
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 25S rRNA of yeast contains several base modifications in the functionally important regions. The enzymes responsible for most of these base modifications remained unknown. Recently, we identified Rrp8 as a methyltransferase involved in m(1)A645 modification of 25S rRNA. Here, we discovered a previously uncharacterized gene YBR141C to be responsible for second m(1)A2142 modification of helix 65 of 25S rRNA. The gene was identified by reversed phase-HPLC screening of all deletion mutants of putative RNA methyltransferase and was confirmed by gene complementation and phenotypic characterization. Because of the function of its encoded protein, YBR141C was named BMT2 (base methyltransferase of 25S RNA). Helix 65 belongs to domain IV, which accounts for most of the intersubunit surface of the large subunit. The 3D structure prediction of Bmt2 supported it to be an Ado Met methyltransferase belonging to Rossmann fold superfamily. In addition, we demonstrated that the substitution of G180R in the S-adenosyl-L-methionine-binding motif drastically reduces the catalytic function of the protein in vivo. Furthermore, we analysed the significance of m(1)A2142 modification in ribosome synthesis and translation. Intriguingly, the loss of m(1)A2142 modification confers anisomycin and peroxide sensitivity to the cells. Our results underline the importance of RNA modifications in cellular physiology.
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