ArticleNucleic acids research2013
Target recognition, RNA methylation activity and transcriptional regulation of the Dictyostelium discoideum Dnmt2-homologue (DnmA).
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 30 papers.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- The RNA-binding protein RNP1A is essential and interacts with contractility kit proteins to facilitate cell mechanics.Journal of cell science · 2026Article
- DNA-encoded library screening uncovers potent DNMT2 inhibitors targeting a cryptic allosteric binding site.iScience · 2025Article
- Dissecting the function of the DNMT2-homolog (DNMA) in Dictyostelium discoideum.G3 (Bethesda, Md.) · 2025Article
- A microscale thermophoresis-based enzymatic RNA methyltransferase assay enables the discovery of DNMT2 inhibitors.Communications chemistry · 2025Article
- Discovery of the major 15-30 nt mammalian small RNAs, their biogenesis and function.Nature communications · 2023Article
- TheNAR genomics and bioinformatics · 2023Article
- Characterization of the dual role of Plasmodium falciparum DNA methyltransferase in regulating transcription and translation.Nucleic acids research · 2023Article
- An Optimized Microscale Thermophoresis Method for High-Throughput Screening of DNA Methyltransferase 2 Ligands.ACS pharmacology & translational science · 2022Article
- Position 34 of tRNA is a discriminative element for m5C38 modification by human DNMT2.Nucleic acids research · 2021Article
- New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1.RNA biology · 2021Article
- RNA 5-methylcytosine modification and its emerging role as an epitranscriptomic mark.RNA biology · 2021Review
- Changes of the tRNA Modification Pattern during the Development ofNon-coding RNA · 2021Article
- Ubiquitination-mediated degradation of TRDMT1 regulates homologous recombination and therapeutic response.NAR cancer · 2021Article
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
- Transcriptome Analysis ofFrontiers in plant science · 2020Article
- Direct RNA Sequencing for the Study of Synthesis, Processing, and Degradation of Modified Transcripts.Frontiers in genetics · 2020Article
- Review
- RNA Methylation in ncRNA: Classes, Detection, and Molecular Associations.Frontiers in genetics · 2018Article
- The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA.RNA biology · 2017Article
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation.RNA biology · 2017Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although the DNA methyltransferase 2 family is highly conserved during evolution and recent reports suggested a dual specificity with stronger activity on transfer RNA (tRNA) than DNA substrates, the biological function is still obscure. We show that the Dictyostelium discoideum Dnmt2-homologue DnmA is an active tRNA methyltransferase that modifies C38 in tRNA(Asp(GUC)) in vitro and in vivo. By an ultraviolet-crosslinking and immunoprecipitation approach, we identified further DnmA targets. This revealed specific tRNA fragments bound by the enzyme and identified tRNA(Glu(CUC/UUC)) and tRNA(Gly(GCC)) as new but weaker substrates for both human Dnmt2 and DnmA in vitro but apparently not in vivo. Dnmt2 enzymes form transient covalent complexes with their substrates. The dynamics of complex formation and complex resolution reflect methylation efficiency in vitro. Quantitative PCR analyses revealed alterations in dnmA expression during development, cell cycle and in response to temperature stress. However, dnmA expression only partially correlated with tRNA methylation in vivo. Strikingly, dnmA expression in the laboratory strain AX2 was significantly lower than in the NC4 parent strain. As expression levels and binding of DnmA to a target in vivo are apparently not necessarily accompanied by methylation, we propose an additional biological function of DnmA apart from methylation.
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