The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA.

ABSTRACT: The amino acid sequence of Dnmt2 is very similar to the catalytic domains of bacterial and eukaryotic DNA-(cytosine 5)-methyltransferases, but it efficiently catalyzes tRNA methylation, while its DNA methyltransferase activity is the subject of controversial reports with rates varying between zero and very weak. By using composite nucleic acid molecules as substrates, we surprisingly found that DNA fragments, when presented as covalent DNA-RNA hybrids in the structural context of a tRNA, can be more efficiently methylated than the corresponding natural tRNA substrate. Furthermore, by stepwise development of tRNA^Asp, we showed that this natural Dnmt2 substrate could be engineered to employ RNAs that act like guide RNAs in vitro. The 5'-half of tRNA^Asp was able to effic

SUBMITTER: Kaiser S 

PROVIDER: S-EPMC5699543 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature