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. 2020 May 27;48(12):6906–6918. doi: 10.1093/nar/gkaa411

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© The Author(s) 2020. 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 Non-Commercial License (http://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 2. — MALDI-MS spectra showing methylation in vitro by NEQ053 at U54 in N. equitans tRNA^Thr. (A) Spectrum of oligonucleotides formed by RNase A digestion of unmodified tRNA^Thr. The measured mass/charge (m/z) of each fragment is shown above the peak with the theoretical m/z values (in box). (B) Enlargement of the spectral region containing the GGGUp fragment from nucleotides 51–54 with an m/z of 1360.3 when derived from the unmodified tRNA^Thr, and with m/z of 1374.3 after incubation of the tRNA in vitro with NEQ053 prior to digestion. (C) Schematic of the N. equitans tRNA^Thr secondary structure. The target site of NEQ053 indicates that the enzyme could be renamed as TrmU54.