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. Author manuscript; available in PMC: 2007 Oct 15.
Published in final edited form as: Mol Cell. 2007 Feb 23;25(4):531–542. doi: 10.1016/j.molcel.2007.01.015

Figure 3.

Figure 3

Representative multiple turnover progress curves for wild type HisRS and mutant tRNAHis comparing the production of [α-32P]-AMP (filled red circles) and [14C]-His~tRNAHis (filled blue triangles) at pH 7.5 and 37°C.

(A) Representative enzyme-tRNA combinations in which ktrans was greater than kcat, and progress curves for the two products were linear. The plots for wt tRNAHis/wt HisRS, and G34U tRNAHis/wt HisRS are depicted here. The remaining plots for other mutants are presented in Supplementary Figure 2.

(B) Representative enzyme-tRNA combinations in which there was a burst of AMP formation in the first turnover. The plots for wt tRNAHis/Q118E HisRS, and C73U tRNAHis/wt HisRS are depicted here. The remaining plots for other mutants are presented in Supplementary Figure 2.

(C) Enzyme-tRNA combinations where slow burst kinetics was observed, owing to effects on both adenylation and aminoacyl transfer. The wt tRNAHis/ R121H HisRS and 5’-ppp tRNAHis/wt HisRS were the only combinations that exhibited this behavior.