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Figure 4 | Journal of Experimental & Clinical Cancer Research

Figure 4

From: Mutations of human DNA topoisomerase I at poly(ADP-ribose) binding sites: modulation of camptothecin activity by ADP-ribose polymers

Figure 4

Influence of PARs on the kinetics of religation. A. Time course (1–8 min) of the religation experiment between the complementary R11 DNA strand and the enzyme covalent complexes described at the top of the figure, in the absence (lanes 2–5) or presence of 100 μMCPT (lanes 6–9) or 50 pmol PARs (lanes 10–13) and PARs plus CPT (lanes 14–17). Lane 1: no R11 added; lane 18: no protein added. Cl represents the DNA fragment cleaved at the preferred site. B. Plots of the percentage of disappearance of the cleavage complex relative to time 0, for the wild-type (square symbol) and 8bmut (circle symbols), in the absence (yellow lines) or presence of CPT (blue lines), PARs (green lines) and PARs plus CPT (red lines). Data shown are means ± SD from 3 independent experiments.

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