@unpublished{ScheitlGhaemMaghamiLenzetal.2020,
  author    = {Scheitl, Carolin P.M. and Ghaem Maghami, Mohammad and Lenz, Ann-Kathrin and H{\"o}bartner, Claudia},
  title     = {Site-specific RNA methylation by a methyltransferase ribozyme},
  series = {Nature},
  journal   = {Nature},
  doi       = {10.1038/s41586-020-2854-z},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-218687},
  year      = {2020},
  abstract  = {Nearly all classes of coding and non-coding RNA undergo post-transcriptional modification including RNA methylation. Methylated nucleotides belong to the evolutionarily most conserved features of tRNA and rRNA.1,2 Many contemporary methyltransferases use the universal cofactor S-adenosylmethionine (SAM) as methyl group donor. This and other nucleotide-derived cofactors are considered as evolutionary leftovers from an RNA World, in which ribozymes may have catalysed essential metabolic reactions beyond self-replication.3 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 (m1A) in a substrate RNA, utilizing O6-methylguanine (m6G) as a small-molecule cofactor. The ribozyme shows a broad RNA sequence scope, as exemplified by site-specific adenosine methylation in tRNAs. This finding provides fundamental insights into RNA's catalytic abilities, serves a synthetic tool to install m1A in RNA, and may pave the way to in vitro evolution of other methyltransferase and demethylase ribozymes.},
  language  = {en}
}