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. 2009 Dec 6;38(4):1312–1324. doi: 10.1093/nar/gkp1118

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© The Author(s) 2009. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Steady-state rate constant for ATP hydrolysis is dependent on RNA concentration. (a) Titration of the RNA unwinding substrate. NS3 (200 nM) was incubated with [α³²P]-ATP (10 mM) and various concentrations of ds9-C20 at 37°C for 10 min and then quenched by addition of EDTA to 100 mM. Product (ADP) was resolved from substrate (ATP) by TLC and visualized by phosphorimaging. The phosphorimage was quantitated, and the concentration of ADP was determined. Shown is the plot of the rate of ATP hydrolysis as a function of RNA concentration. (b) Steady-state rate constant for ATP hydrolysis is independent of ATP concentration at fixed RNA concentration. NS3 (200 nM) was incubated with ds9-C20 (20 µM) and various concentrations of [α³²P]-ATP at 37°C for 10 min and then quenched by addition of EDTA to 100 mM. Product (ADP) was resolved from substrate (ATP) by TLC and visualized by phosphorimaging. The phosphorimage was quantitated, and the concentration of ADP was determined. Shown is the plot of the rate of ATP hydrolysis as a function of ATP concentration. The average rate of hydrolysis of 3.4 ± 1 s⁻¹ is shown as a dotted line.