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The AlkB Domain of Mammalian ABH8 Catalyzes Hydroxylation of 5-Methoxycarbonylmethyluridine at the Wobble Position of tRNA

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  • This work was supported by the U.S. National Institute of Health (GM071440 to C.H.) and by an NIH EUREKA award (GM088599 to C.H. and T.P.). Q.D. was supported by the Chicago Biomedical Consortium (CBC). W.Z. was partially supported by the American Recovery and Reinvestment Act NIGMS Administrative Supplementary grant (3R01M071440-05S1). We thank Dr. Leslie M. Hicks for performing mass spectrometry analysis and Dr. Stephen B. H. Kent for the use of the LC mass spectrometer.

Abstract

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Family ties: The AlkB family of nonheme iron, α-ketoglutarate (αKG)-dependent dioxygenases is involved in biological processes such as DNA/RNA repair and obesity. The AlkB domain of ABH8 is shown to catalyze the hydroxylation of a modified uridine (mcm5U) into (S)-mchm5U at the wobble position of the anticodon stem–loop in tRNA (see scheme), thereby suggesting that this protein is a tRNA hypermodification enzyme.

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