Journal article
Two substrates are better than one: dual specificities for Dnmt2 methyltransferases
Publication Details
Authors: | Nellen, W. |
Publication year: | 2006 |
Journal: | Trends in Biochemical Sciences |
Pages range : | 306-308 |
Volume number: | 31 |
Start page: | 306 |
End page: | 308 |
ISSN: | 0968-0004 |
eISSN: | 1362-4326 |
DOI-Link der Erstveröffentlichung: |
Abstract
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.
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.
