Fig. 5
Hs AlaRS has pre-transfer editing activity against Aze, Hs ProRS has no editing activity against Aze. a ATP hydrolysis in the presence of 20 mM Ala, 100 mM Ser, or 100 mM Aze with 1 µM Hs AlaRS. b Relative level of charged tRNAAla after aminoacylation for 5 min by full-length Hs AlaRS (FL) or aminoacylation domain of AlaRS (AD) with either 2.5 mM Ala, Ser, or Aze. c Deacylation assay with Hs ProXp-ala using either Ala-tRNAPro or Aze-tRNAPro. d Aminoacylation of tRNAPro by Hs ProRS with Pro in the presence of different concentrations of Aze at 20 min. e Relative level of charged tRNAPro after 20 min aminoacylation by Hs ProRS with either 2.5 mM Pro, Aze, Ala, or His. (All graphs represent mean ± s.d., average of three experiments.)
