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Showing 1–4 of 4 results
Advanced filters: Author: Ann-Kathrin Lenz Clear advanced filters

  • Crystal structures of the ribozyme SAMURI reveal the alkyltransferase mechanism and show N3-modified adenosine and dealkylated cofactor in the active site, allowing for a comparison with riboswitches that bind S-adenosylmethionine but do not catalyze methyl transfer.

    • Hsuan-Ai Chen
    • Takumi Okuda
    • Claudia Höbartner
    ResearchOpen Access
    Nature Chemical Biology
    P: 1-10

  • Ribozyme-mediated post-transcriptional RNA modification is a powerful method for site-specific RNA labelling and analysis of RNA functions. Now, an alkyltransferase ribozyme—termed SAMURI—has been shown to catalyse the transfer of a propargyl group from a stabilized synthetic S-adenosylmethionine analogue to a specific adenosine on the target RNA within cells.

    • Takumi Okuda
    • Ann-Kathrin Lenz
    • Claudia Höbartner
    ResearchOpen Access
    Nature Chemistry
    Volume: 15, P: 1523-1531

  • A methyltransferase ribozyme, along with the small-molecule cofactor O6-methylguanine, is shown to catalyse the site-specific installation of 1-methyladenosine in various RNAs, providing insights into the catalytic abilities of RNA.

    • Carolin P. M. Scheitl
    • Mohammad Ghaem Maghami
    • Claudia Höbartner
    Research
    Nature
    Volume: 587, P: 663-667

  • Fluorogenic RNA aptamers such as Chili display strong fluorescence enhancement upon aptamer–ligand complex formation. Here, the authors provide insights into the mechanism of fluorescence activation of Chili by solving the crystal structures of Chili with its bound positively charged ligands DMHBO+ and DMHBI+, and they reveal that Chili uses an excited state proton transfer mechanism based on time-resolved optical spectroscopy measurements.

    • Mateusz Mieczkowski
    • Christian Steinmetzger
    • Claudia Höbartner
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11