ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA

Erwin van den Born, Cathrine B. Vågbø, Lene Songe-Møller, Vibeke Leihne, Guro F. Lien, Grazyna Leszczynska, Andrzej Malkiewicz, Hans E. Krokan, Finn Kirpekar, Arne Klungland () and Pål Ø. Falnes ()
Additional contact information
Erwin van den Born: University of Oslo, PO Box 1041 Blindern, Oslo 0316, Norway.
Cathrine B. Vågbø: Norwegian University of Science and Technology
Lene Songe-Møller: Centre for Molecular Biology and Neuroscience, Institute of Medical Microbiology, Oslo University Hospital
Vibeke Leihne: University of Oslo, PO Box 1041 Blindern, Oslo 0316, Norway.
Guro F. Lien: Centre for Molecular Biology and Neuroscience, Institute of Medical Microbiology, Oslo University Hospital
Grazyna Leszczynska: Institute of Organic Chemistry, Technical University
Andrzej Malkiewicz: Institute of Organic Chemistry, Technical University
Hans E. Krokan: Norwegian University of Science and Technology
Finn Kirpekar: University of Southern Denmark
Arne Klungland: Centre for Molecular Biology and Neuroscience, Institute of Medical Microbiology, Oslo University Hospital
Pål Ø. Falnes: University of Oslo, PO Box 1041 Blindern, Oslo 0316, Norway.

Nature Communications, 2011, vol. 2, issue 1, 1-7

Abstract: Abstract Mammals have nine different homologues (ALKBH1–9) of the Escherichia coli DNA repair demethylase AlkB. ALKBH2 is a genuine DNA repair enzyme, but the in vivo function of the other ALKBH proteins has remained elusive. It was recently shown that ALKBH8 contains an additional transfer RNA (tRNA) methyltransferase domain, which generates the wobble nucleoside 5-methoxycarbonylmethyluridine (mcm5U) from its precursor 5-carboxymethyluridine (cm5U). In this study, we report that (R)- and (S)-5-methoxycarbonylhydroxymethyluridine (mchm5U), hydroxylated forms of mcm5U, are present in mammalian , and , respectively, representing the first example of a diastereomeric pair of modified RNA nucleosides. Through in vitro and in vivo studies, we show that both diastereomers of mchm5U are generated from mcm5U, and that the AlkB domain of ALKBH8 specifically hydroxylates mcm5U into (S)-mchm5U in . These findings expand the function of the ALKBH oxygenases beyond nucleic acid repair and increase the current knowledge on mammalian wobble uridine modifications and their biogenesis.

Date: 2011
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DOI: 10.1038/ncomms1173

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