Figure 7. The influence of RuvA_Mpn and RuvA_Mge on the ATPase activities of RuvB_FH and RuvB_Mge, respectively.

ATP hydrolysis by RuvB_FH and RuvB_Mge was measured at a protein concentration of 0.5 µM, either in the absence of presence of the corresponding RuvA protein (at 1 µM). The ATPase activity was determined using an NADH-coupled assay. In this assay, the activity is calculated from the stationary velocities of ATP hydrolysis, as determined by monitoring the absorption of NADH at 340 nm [15], [46]. The ‘no protein’ reaction (×) indicates a control reaction performed in the absence of any protein. (+), RuvA_Mge alone; (○), RuvA_Mpn alone; (□), RuvB_Mge alone; (▪), RuvB_Mge plus RuvA_Mge; (▵), RuvB_FH alone; (▴), RuvB_FH plus RuvA_Mpn. The graph shows a representative experiment.