Plasmodium falciparum UvrD Helicase Translocates in 3′ to 5′ Direction, Colocalizes with MLH and Modulates Its Activity through Physical Interaction
Figure 8
Direction of unwinding by PfUDN.
A, The structures of the linear substrate for the 5′ to 3′ direction (substrate 3A, Tale S1). An asterisk (*) denotes the 32P-labeled end. B, Helicase activity using the substrate 3A (Tale S1) shown in A. Lane C is the reaction without enzyme and lane B is the heat-denatured substrate. Lanes 1–6 are reactions with increasing concentration of PfUDN. C, The structure of the linear substrate for the 3′ to 5′ direction (substrate 3B, Tale S1). An asterisk (*) denotes the 32P-labeled end. D, The helicase activity using the substrate 3B (Tale S1) shown in C. Lane C is the reaction without enzyme and lane B is the heat-denatured substrate. Lanes 1–6 are reactions with increasing concentration of PfUDN. E, The quantitative enzyme activity data from the autoradiogram in D are shown and the concentration of PfUDN used is also written.