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. 2020 Nov 16;48(21):12282–12296. doi: 10.1093/nar/gkaa911

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Influence of DNA and ATP binding on ctXPB’s ATPase activity. (A) Influence of dsDNA and ctp52/ctp8 on the ATPase activity of ctXPB. Increasing amounts of dsDNA were titrated onto fixed concentrations of ctXPB (open circles) and ctXPB with ctp52/ctp8 (open squares). Increasing amounts of ctp52/ctp8 were titrated onto fixed concentrations of ctXPB plus dsDNA (open triangles). The x-axis shows the logarithmic concentration of the respective activator complex that was titrated. The y-axis shows the NADH-consumption-derived ATP turnover rate in μmol ATP per liter per minute. N ≥ 4. (B) Fluorescence polarization measurements to investigate the influence of ctp52/ctp8 on ctXPB’s dsDNA binding ability. Increasing amounts of ctXPB (open squares) and ctXPB with ctp52/ctp8 (open circles) were titrated onto fixed amounts of fluorescently labeled dsDNA. The calculated k_D values are listed in Table 2. N = 3. (C) ATPase activity profile with Michaelis Menten kinetics. Increasing amounts of substrate (ATP) were titrated onto different complexes of ctXPB with its activators dsDNA (circles), ctp52/ctp8 (squares) and dsDNA plus ctp52/ctp8 (rhombs). The x-axis shows the concentration of the respective activator complex. The y-axis shows the NADH-consumption-derived ATP turnover rate in μmol ATP per liter per minute. V_max, K_M, k_cat and k_cat/K_M values for the different ctXPB activation complexes are listed in Table 3. N ≥ 3. (D) ATPase activity of ctXPB in the presence of dsDNA with or without different ctp52/ctp8 complexes. N ≥ 8.