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. 2018 Aug;24(8):1080–1092. doi: 10.1261/rna.064345.117

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© 2018 Singh et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 2. — Domain swapping experiment of _TkTrm10 and _SaTrm10. MTase activity measurements of _TkTrm10 and _SaTrm10 chimeric proteins using total E. coli tRNA as substrate. E. coli tRNA was incubated in the presence of 30 µg of purified enzyme and [methyl-¹⁴C]-SAM (see Materials and Methods). tRNA was recovered and digested by nuclease P1. The resulting 5′-phosphate mononucleosides were analyzed by 2D-TLC followed by autoradiography. Circles in dotted lines show the migration of the four canonical nucleotides used as UV markers. The domain organization of the chimeric proteins is shown schematically with the Thermococcus part of the protein in green and the Sulfolobus part in red. The SPOUT domains are indicated. The numbers represent the N and C terminus or junction regions of _TkTrm10 and _SaTrm10.