RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage.
By M. Schaefer, Tim Pollex, Katharina Hanna, Francesca Tuorto, Madeleine Meusburger, M. Helm, F. Lyko. Genes & Development, 2010
698 citations recorded by the source corpus.
Dnmt2 proteins are the most conserved members of the DNA methyltransferase enzyme family, but their substrate specificity and biological functions have been a subject of controversy. We show here that, in addition to tRNA(Asp-GTC), tRNA(Val-AAC) and tRNA(Gly-GCC) are also methylated by Dnmt2. Drosophila Dnmt2 mutants showed reduced viability under stress conditions, and Dnmt2 relocalized to stress granules following heat shock. Strikingly, stress-induced cleavage of tRNAs was Dnmt2-dependent, and Dnmt2-mediated methylation protected tRNAs against ribonuclease cleavage. These results uncover a novel biological function of Dnmt2-mediated tRNA methylation, and suggest a role for Dnmt2 enzymes during the biogenesis of tRNA-derived small RNAs.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/896d028b57305e36c7223f7bd2d33d3debe2cb27
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
Citations in the corpus
- tRNA biology charges to the front. (2010, background): “Drosophila Dnmt2 mutants are significantly less viable in response to oxidative or heat stress, and substrate tRNAs in these mutants are more sensitive to stressinduced cleavage and cleavage by angiogenin (Schaefer et al. 2010).”
- MODOMICS: a database of RNA modification pathways—2013 update (2012, background): “Examples include the immune response to rRNA and tRNA methylation (17,18), the linkage between tRNA modification and host resistance to viral infection (19) and stress-induced cleavage of small RNAs (20).”
- Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA (2012, methodology): “Secondly, TRDMT1 (tRNA aspartic acid MTase 1, also known as DNMT2), has been shown to methylate position 38 on tRNAAsp(GUC) in eukaryotes (12,31,32), and tRNAVal(AAC) and tRNAGly(GCC) in Drosophila (12).”