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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Main Authors: Schaefer, Matthias R. (Author) , Pollex, Tim (Author) , Hanna, Katharina (Author) , Tuorto, Francesca (Author) , Meusburger, Madeleine (Author) , Helm, Mark (Author) , Lyko, Frank (Author)
Format: Article (Journal)
Language:English
Published: 2010
In: Genes & development
Year: 2010, Volume: 24, Issue: 15, Pages: 1590-1595
ISSN:1549-5477
DOI:10.1101/gad.586710
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1101/gad.586710
Verlag, lizenzpflichtig, Volltext: http://genesdev.cshlp.org/content/24/15/1590
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Author Notes:Matthias Schaefer, Tim Pollex, Katharina Hanna, Francesca Tuorto, Madeleine Meusburger, Mark Helm and Frank Lyko
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Summary: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.
Item Description:Gesehen am 10.08.2023
Physical Description:Online Resource
ISSN:1549-5477
DOI:10.1101/gad.586710