Two substrates are better than one: dual specificities for Dnmt2 methyltransferases

Trends Biochem Sci. 2006 Jun;31(6):306-8. doi: 10.1016/j.tibs.2006.04.005. Epub 2006 May 6.


Dnmt2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases; however, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought. This finding has important implications for understanding the evolutionary relationships among these enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • DNA (Cytosine-5-)-Methyltransferases / genetics
  • DNA (Cytosine-5-)-Methyltransferases / metabolism*
  • DNA Methylation
  • Evolution, Molecular*
  • Humans
  • RNA Processing, Post-Transcriptional / physiology*
  • RNA, Transfer / metabolism*
  • Substrate Specificity / genetics


  • RNA, Transfer
  • DNA (Cytosine-5-)-Methyltransferases
  • TRDMT1 protein, human