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. 2021 Dec 6;49(22):13045–13061. doi: 10.1093/nar/gkab1148

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — I34 is the prerequisite for hDNMT2-mediated m⁵C38 modification in tRNA^Val(AAC). (A) The secondary structures of tRNA^Val(AAC), -(CAC) and -(.AC). (B) UPLC-MS/MS analysis of m⁵C (Q1/Q3 = 258.1/126.1) of tRNA^Val(AAC) after incubation with or without hDNMT2. UPLC-MS/MS analysis of I (Q1/Q3 = 269.1 to 137.1) of tRNA^Val(AAC) after incubation with the ADAT2-ADAT3 complex. The products of tRNA^Val(AAC) incubated with ADAT2-ADAT3 and then reacted with hDNMT2 were also digested and detected by UPLC-MS/MS analysis. (C) The capacity of tRNA^Val(AAC) and tRNA^Val(IAC) to be methylated by hDNMT2. (D) Schematic diagram showing that in tRNA^Val(AAC), hDNMT2-mediated m⁵C38 modification depends on the A-to-I modification at position 34 formed by the ADAT2-ADAT3 complex.