RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage
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 tRNAAsp-GTC, tRNAVal-AAC and tRNAGly-GCC are also methylated by Dnmt2. Drosophila D...
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| Hauptverfasser: | , , , , , , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2010
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| In: |
Genes & development
Year: 2010, Jahrgang: 24, Heft: 15, Pages: 1590-1595 |
| ISSN: | 1549-5477 |
| DOI: | 10.1101/gad.586710 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1101/gad.586710 Verlag, lizenzpflichtig, Volltext: http://genesdev.cshlp.org/content/24/15/1590 |
| Verfasserangaben: | Matthias Schaefer, Tim Pollex, Katharina Hanna, Francesca Tuorto, Madeleine Meusburger, Mark Helm and Frank Lyko |
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| 520 | |a 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 tRNAAsp-GTC, tRNAVal-AAC and tRNAGly-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. | ||
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