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. 2018 Sep;24(9):1144–1157. doi: 10.1261/rna.067165.118

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© 2018 Munir 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 1. — RslTpt1 genetic organization and tRNA 2′-phosphotransferase activity in yeast. (A) (Top panel) The ORF encoding Runella slithyformis Tpt1 is followed by three co-oriented ORFs encoding putative enzymes with likely roles in nucleic acid repair. (Bottom panel) The amino acid sequence of R. slithyformis (Rsl) Tpt1 (NCBI accession AEI48611) is aligned to that of Saccharomyces cerevisiae (Sce) Tpt1 (NCBI accession ABE08504). Positions of side chain identity/similarity are denoted by dots. Gaps in the alignments are denoted by dashes. Four conserved amino acids identified by alanine scanning as essential for SceTpt1 function in vivo are shown in white font on black background. The RslTpt1 residues Arg16, His17, Arg64, and Arg119 that were mutated to alanine in the present study are denoted by [ | ]. (B) Genetic complementation of S. cerevisiae tpt1Δ by expression of RslTpt1. Serial dilutions of tpt1Δ p[CEN SceTPT1], tpt1Δ p[CEN RslTPT1], and tpt1Δ p[2µ RslTPT1] cells recovered after plasmid shuffle were spotted to YPD agar plates, which were incubated at 20°C, 30°C, and 37°C.