FIGURE 3.
The C terminus of PAPD5 is involved in RNA binding. (A) Schematic representation of the truncation variants of PAPD5 tested for RNA binding. (B) Electrophoretic mobility shift assay of PAPD5 variants. Increasing amounts of PAPD5 full-length protein or fragments comprising the N terminus, central part, or C terminus of the protein were incubated with radioactively labeled in vitro–synthesized human tRNAiMet, and the reactions were resolved on a native polyacrylamide gel. Protein concentrations between 0.5 and 5 nM were tested for the full-length protein and the protein PAPD5 C2, 1–20 nM for the other variants. Lane 1 shows the tRNA after incubation in the absence of protein.