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. 1999 Jun 8;96(12):6672–6677. doi: 10.1073/pnas.96.12.6672

Figure 3.

Figure 3

Effect of 3′ terminal CCA in pGln on pre-steady-state cleavage kinetics by RNase P RNA or holoenzyme from E. coli and Synechocystis 6803. Ten picomolar 32P-labeled pGln (○) or pGlnCCA (●) was incubated with 20 nM E. coli M1 RNA (A), 40 nM Synechocystis RNase P RNA (B), holoenzyme reconstituted with 0.5 nM E. coli M1 RNA and 5 nM C5 protein (C), or holoenzyme reconstituted with 2 nM Synechocystis RNase P RNA and 20 nM Synechocystis RNase P protein (D) and aliquots withdrawn at different times. Buffer conditions are as described in Materials and Methods. An average of three independent experiments is shown.