Modomics - A Database of RNA Modifications
ALKBH8 from Homo sapiens - protein summary.
Alkylated DNA repair protein alkB homolog 8
Position of modification - modification:
t:34 - mchm5U
t:34 - mcm5s2U
t:34 - mcm5U
t:34 - mcm5Um
Exhibits two enzymatic activities: MTase domain provides the mcm5U precursor (ortholog of the yeast Trm9) while AlkB domain is a mchm5U synthesizing oxygenase (hydroxylase activity). AdoMet is the methyl group donor. Interaction with TRM112 is required for MTase activity only. Prior ALKBH8-mediated methylation is a prerequisite for sbsequent thiolation and 2'-O-ribose methylation that form 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) and 5-methoxycarbonylmethyl-2'-O-methyluridine (mcm5Um), respectively. ABH8 depleted cells exhibit highly elevated levels of cm5U and lowered levels of mcm5U and shows an increase cellular sensitivity to DNA-damaging agents, attesting for possible regulatory role of ALKBH8 in the DNA damage response pathway. Complementary information in the case of fungi can be obtained under Trm9, Trm112 and Elongation complex Elf 1-6.
Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification.
Pastore C, Topalidou I, Forouhar F, Yan AC, Levy M, Hunt JF
J Biol Chem
Human AlkB homolog ABH8 Is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival.
Fu D, Brophy JA, Chan CT, Atmore KA, Begley U, Paules RS, Dedon PC, Begley TJ, Samson LD
Mol Cell Biol
ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA.
van den Born E, Vagbo CB, Songe-Moller L, Leihne V, Lien GF, Leszczynska G, Malkiewicz A, Krokan HE, Kirpekar F, Klungland A, Falnes PO
The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA.
Fu Y, Dai Q, Zhang W, Ren J, Pan T, He C
Angew Chem Int Ed Engl
Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding.
Songe-Moller L, van den Born E, Leihne V, Vagbo CB, Kristoffersen T, Krokan HE, Kirpekar F, Falnes PO, Klungland A
Mol Cell Biol
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