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https://www.readbyqxmd.com/read/22443471/changes-in-protein-dynamics-of-the-dna-repair-dioxygenase-alkb-upon-binding-of-fe-2-and-2-oxoglutarate
#1
Boris Bleijlevens, Tara Shivarattan, Kim S van den Boom, Annett de Haan, Gert van der Zwan, Pete J Simpson, Steve J Matthews
The Escherichia coli DNA repair enzyme AlkB is a 2-oxoglutarate (2OG)-dependent Fe(2+) binding dioxygenase that removes methyl lesions from DNA and RNA. To date, nine human AlkB homologues are known: ABH1 to ABH8 and the obesity-related FTO. Similar to AlkB, these homologues exert their activity on nucleic acids, although for some homologues the biological substrate remains to be identified. 2OG dioxygenases require binding of the cofactors Fe(2+) and 2OG in the active site to form a catalytically competent complex...
April 24, 2012: Biochemistry
https://www.readbyqxmd.com/read/22065580/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
#2
Chiara Pastore, Irini Topalidou, Farhad Forouhar, Amy C Yan, Matthew Levy, John F Hunt
Humans express nine paralogs of the bacterial DNA repair enzyme AlkB, an iron/2-oxoglutarate-dependent dioxygenase that reverses alkylation damage to nucleobases. The biochemical and physiological roles of these paralogs remain largely uncharacterized, hampering insight into the evolutionary expansion of the AlkB family. However, AlkB homolog 8 (ABH8), which contains RNA recognition motif (RRM) and methyltransferase domains flanking its AlkB domain, recently was demonstrated to hypermodify the anticodon loops in some tRNAs...
January 13, 2012: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/20583019/the-alkb-domain-of-mammalian-abh8-catalyzes-hydroxylation-of-5-methoxycarbonylmethyluridine-at-the-wobble-position-of-trna
#3
Ye Fu, Qing Dai, Wen Zhang, Jin Ren, Tao Pan, Chuan He
No abstract text is available yet for this article.
November 15, 2010: Angewandte Chemie
https://www.readbyqxmd.com/read/20308323/human-alkb-homolog-abh8-is-a-trna-methyltransferase-required-for-wobble-uridine-modification-and-dna-damage-survival
#4
Dragony Fu, Jennifer A N Brophy, Clement T Y Chan, Kyle A Atmore, Ulrike Begley, Richard S Paules, Peter C Dedon, Thomas J Begley, Leona D Samson
tRNA nucleosides are extensively modified to ensure their proper function in translation. However, many of the enzymes responsible for tRNA modifications in mammals await identification. Here, we show that human AlkB homolog 8 (ABH8) catalyzes tRNA methylation to generate 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position of certain tRNAs, a critical anticodon loop modification linked to DNA damage survival. We find that ABH8 interacts specifically with tRNAs containing mcm(5)U and that purified ABH8 complexes methylate RNA in vitro...
May 2010: Molecular and Cellular Biology
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