Site-specific RNA methylation by a methyltransferase ribozyme

Carolin P. M. Scheitl, Mohammad Ghaem Maghami, Ann-Kathrin Lenz and Claudia Höbartner ()
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Carolin P. M. Scheitl: Julius-Maximilians-Universität Würzburg
Mohammad Ghaem Maghami: Julius-Maximilians-Universität Würzburg
Ann-Kathrin Lenz: Julius-Maximilians-Universität Würzburg
Claudia Höbartner: Julius-Maximilians-Universität Würzburg

Nature, 2020, vol. 587, issue 7835, 663-667

Abstract: Abstract Nearly all classes of coding and non-coding RNA undergo post-transcriptional modification, including RNA methylation. Methylated nucleotides are among the evolutionarily most-conserved features of transfer (t)RNA and ribosomal (r)RNA1,2. Many contemporary methyltransferases use the universal cofactor S-adenosylmethionine (SAM) as a methyl-group donor. SAM and other nucleotide-derived cofactors are considered to be evolutionary leftovers from an RNA world, in which ribozymes may have catalysed essential metabolic reactions beyond self-replication3. Chemically diverse ribozymes seem to have been lost in nature, but may be reconstructed in the laboratory by in vitro selection. Here we report a methyltransferase ribozyme that catalyses the site-specific installation of 1-methyladenosine in a substrate RNA, using O6-methylguanine as a small-molecule cofactor. The ribozyme shows a broad RNA-sequence scope, as exemplified by site-specific adenosine methylation in various RNAs. This finding provides fundamental insights into the catalytic abilities of RNA, serves a synthetic tool to install 1-methyladenosine in RNA and may pave the way to in vitro evolution of other methyltransferase and demethylase ribozymes.

Date: 2020
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DOI: 10.1038/s41586-020-2854-z

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