@unpublished{MaghamiScheitlHoebartner2019,
  author    = {Maghami, Mohammad Ghaem and Scheitl, Carolin P. M. and H{\"o}bartner, Claudia},
  title     = {Direct in vitro selection of trans-acting ribozymes for posttranscriptional, site-specific, and covalent fluorescent labeling of RNA},
  series = {Journal of the American Chemical Society},
  journal   = {Journal of the American Chemical Society},
  doi       = {10.1021/jacs.9b10531},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-192333},
  year      = {2019},
  abstract  = {General and efficient tools for site-specific fluorescent or bioorthogonal labeling of RNA are in high demand. Here, we report direct in vitro selection, characterization, and application of versatile trans-acting 2'-5' adenylyl transferase ribozymes for covalent and site-specific RNA labeling. The design of our partially structured RNA pool allowed for in vitro evolution of ribozymes that modify a predetermined nucleotide in cis (i.e. intramolecular reaction), and were then easily engineered for applications in trans (i.e. in an intermolecular setup). The resulting ribozymes are readily designed for specific target sites in small and large RNAs and accept a wide variety of N6-modified ATP analogues as small molecule substrates. The most efficient new ribozyme (FH14) shows excellent specificity towards its target sequence also in the context of total cellular RNA.},
  language  = {en}
}
@unpublished{ScheitlMieczkowskiSchindelinetal.2022,
  author    = {Scheitl, Carolin P. M. and Mieczkowski, Mateusz and Schindelin, Hermann and H{\"o}bartner, Claudia},
  title     = {Structure and mechanism of the methyltransferase ribozyme MTR1},
  series = {Nature Chemical Biology},
  journal   = {Nature Chemical Biology},
  edition   = {submitted version},
  doi       = {10.1038/s41589-022-00976-x},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-272170},
  year      = {2022},
  abstract  = {RNA-catalysed RNA methylation was recently shown to be part of the catalytic repertoire of ribozymes. The methyltransferase ribozyme MTR1 catalyses the site-specific synthesis of 1-methyladenosine (m\(^1\)A) in RNA, using O\(^6\)-methylguanine (m\(^6\)G) as methyl group donor. Here we report the crystal structure of MTR1 at a resolution of 2.8 {\AA}, which reveals a guanine binding site reminiscent of natural guanine riboswitches. The structure represents the postcatalytic state of a split ribozyme in complex with the m1A-containing RNA product and the demethylated cofactor guanine. The structural data suggest the mechanistic involvement of a protonated cytidine in the methyl transfer reaction. A synergistic effect of two 2'-O-methylated ribose residues in the active site results in accelerated methyl group transfer. Supported by these results, it seems plausible that modified nucleotides may have enhanced early RNA catalysis and that metabolite-binding riboswitches may resemble inactivated ribozymes that have lost their catalytic activity during evolution.},
  language  = {en}
}