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. 2019 Dec 21;48(3):1435–1450. doi: 10.1093/nar/gkz1191

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© The Author(s) 2019. 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 License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — In vitro activity of the E. coli YfiP protein. (A) Representative ITC thermograms for titrations of purified YfiP protein with either SAM (left), 5-MTA (center) or SAH (right). The resulting dissociation constants are indicated. The cofactor SAM is bound with the highest affinity. (B) Abundance of acp³U after in vitro modification of total tRNA isolated from a ΔyfiP strain with overexpressed and purified YfiP. Equal amounts of total tRNA from mock-incubated (black) and YfiP incubated samples (red) were analyzed by nucleoside LC-MS/MS. On the left the abundance of acp³U (mass transition 346 → 214) is shown and on the right uridine (mass transition 245 → 113) is shown. (C) Detection of acp³U-47 in tRNA^Arg-ICG by a primer extension stop at position C48 after in vitro incubation of total tRNA from a ΔyfiP strain with purified YfiP and SAM. The reverse transcriptase arrest at C48 is missing if the protein or the cofactor SAM are excluded from the reaction.