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. 2012 Oct 5;40(22):11583–11593. doi: 10.1093/nar/gks910

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© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — All three human TRM10 homologues have methyltransferase activity, but differ in their substrate specificity. Recombinant yeast Trm10p, the human TRMT10C–SDR5C1 complex and human TRMT10A and TRMT10B were assayed with different human tRNA substrates labelled at position 9, and the tRNA hydrolysates were resolved by TLC. (A) (Cyt)tRNA^Arg; (B) (mt)tRNA^Ile; (C) (mt)tRNA^Leu(UUR); (D) (mt)tRNA^Tyr; (E) (cyt)tRNA^Arg-I9 (G9 replaced by inosine); (F) (mt)tRNA^His; (G) (mt)tRNA^Lys; (H) (cyt)tRNA^Arg-A9 (G9 replaced by adenosine).