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Protozoan ALKBH8 Oxygenases Display both DNA Repair and tRNA Modification Activities

Zdzalik, Daria; Vågbø, Cathrine Broberg; Kirpekar, F; Davydova, Erna; Puścian, Alicja; Maciejewska, Agnieszka M.; Krokan, Hans Einar; Klungland, Arne; Tudek, Barbara; Van den Born, Erwin; Falnes, Pål
Journal article, Peer reviewed
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URI
http://hdl.handle.net/11250/299788
Date
2014
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  • Institutt for klinisk og molekylær medisin [1998]
  • Publikasjoner fra CRIStin - NTNU [19694]
Original version
PLoS ONE 2014, 9(6)   10.1371/journal.pone.0098729
Abstract
The ALKBH family of Fe(II) and 2-oxoglutarate dependent oxygenases comprises enzymes that display sequence homology

to AlkB from E. coli, a DNA repair enzyme that uses an oxidative mechanism to dealkylate methyl and etheno adducts on the

nucleobases. Humans have nine different ALKBH proteins, ALKBH1–8 and FTO. Mammalian and plant ALKBH8 are tRNA

hydroxylases targeting 5-methoxycarbonylmethyl-modified uridine (mcm5U) at the wobble position of tRNAGly(UCC). In

contrast, the genomes of some bacteria encode a protein with strong sequence homology to ALKBH8, and robust DNA

repair activity was previously demonstrated for one such protein. To further explore this apparent functional duality of the

ALKBH8 proteins, we have here enzymatically characterized a panel of such proteins, originating from bacteria, protozoa

and mimivirus. All the enzymes showed DNA repair activity in vitro, but, interestingly, two protozoan ALKBH8s also

catalyzed wobble uridine modification of tRNA, thus displaying a dual in vitro activity. Also, we found the modification

status of tRNAGly(UCC) to be unaltered in an ALKBH8 deficient mutant of Agrobacterium tumefaciens, indicating that bacterial

ALKBH8s have a function different from that of their eukaryotic counterparts. The present study provides new insights on

the function and evolution of the ALKBH8 family of proteins.
Publisher
Public Library of Science
Journal
PLoS ONE

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