Jurkowski, Tomasz P  ORCID: https://orcid.org/0000-0002-2012-0240, Meusburger, Madeleine, Phalke, Sameer, Helm, Mark, Nellen, Wolfgang, Reuter, Gunter and Jeltsch, Albert
2008.
Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism.
RNA
14
(8)
, 1663—1670.
10.1261/rna.970408
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Abstract
Although their amino acid sequences and structure closely resemble DNA methyltransferases, Dnmt2 proteins were recently shown by Goll and colleagues to function as RNA methyltransferases transferring a methyl group to the C5 position of C38 in tRNAAsp. We observe that human DNMT2 methylates tRNA isolated from Dnmt2 knock-out Drosophila melanogaster and Dictyostelium discoideum. RNA extracted from wild type D. melanogaster was methylated to a lower degree, but in the case of Dictyostelium, there was no difference in the methylation of RNA isolated from wild-type and Dnmt2 knock-out strains. Methylation of in vitro transcribed tRNAAsp confirms it to be a target of DNMT2. Using site directed mutagenesis, we show here that the enzyme has a DNA methyltransferase-like mechanism, because similar residues from motifs IV, VI, and VIII are involved in catalysis as identified in DNA methyltransferases. In addition, exchange of C292, which is located in a CFT motif conserved among Dnmt2 proteins, strongly reduced the catalytic activity of DNMT2. Dnmt2 represents the first example of an RNA methyltransferase using a DNA methyltransferase type of mechanism.
| Item Type: | Article |
|---|---|
| Date Type: | Published Online |
| Status: | Published |
| Schools: | Schools > Biosciences |
| Publisher: | Cold Spring Harbor Laboratory Press: 12 month Embargo |
| ISSN: | 1355-8382 |
| Date of Acceptance: | 17 April 2008 |
| Last Modified: | 25 Oct 2022 13:08 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/118982 |
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