Figure 5.

Aminoacylation and editing activities of chimera protein in comparison with various wild‐type PheRSs: (A) Charging of E. coli tRNA^Phe transcript (0.8 μM) with Phe by chimera (0.4 µM) or HsmtPheRS (0.4 µM). Reactions were performed at 37°C in the presence of 5 mM ATP and 4 μM [³H]Phe; (B) Editing activities of chimera (1 µM) and EcPheRS (20 nM) toward exogenous Tyr‐tRNA^Phe (1.2 μM); (C) Reaminoacylation of m‐Tyr‐tRNA^Phe with Phe by chimera or HsmtPheRS. The E. coli tRNA^Phe transcript was preaminoacylated with m‐Tyr and purified, then incubated (at 1.2 µM concentration) in the presence of ATP, [³H]Phe, and chimera (0.4 μM) or HsmtPheRS (0.4 µM).