RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage

Genes Dev. 2010 Aug 1;24(15):1590-5. doi: 10.1101/gad.586710.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • DNA (Cytosine-5-)-Methyltransferases / genetics
  • DNA (Cytosine-5-)-Methyltransferases / metabolism*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / enzymology*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / physiology
  • Female
  • Male
  • Methylation
  • Mice
  • RNA / metabolism*
  • RNA, Transfer / metabolism*
  • Ribonuclease, Pancreatic / metabolism
  • Sequence Deletion / genetics
  • Stress, Physiological*
  • Survival Analysis

Substances

  • Drosophila Proteins
  • RNA
  • RNA, Transfer
  • Mt2 protein, Drosophila
  • DNA (Cytosine-5-)-Methyltransferases
  • angiogenin
  • Ribonuclease, Pancreatic