Figure 3
From: Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips
ADP binding to Acto·Myo19-3IQ as measured by kinetic competition with ATP. (A) Normalized time courses of light scattering decrease after mixing 0.2 µM Acto·Myo19-3IQ with 125 µM ATP in the absence or presence of different [ADP] ranging from 0.125 to 25 µM. Data are averaged transients (n = 3-5). Smooth lines through the data represent best fits to double or single exponential functions. (B) [ADP]-dependence of the slow observed rate constants for Acto·Myo19-3IQ as measured by kinetic competition with 125 µM ATP. (C) Normalized amplitudes of the slow phase obtained by fitting transients to double or single exponential functions as a function of [ADP]. The solid lines are fits of the data to Eq. 2. (D) [ATP]-dependence of the observed rate constants of Acto·Myo19-3IQ·D dissociation as measured by light scattering at saturated [ADP] of 25 µM. (E) The temperature dependence of the observed lag preceding ATP (500 µM)-induced Acto·Myo19-3IQ·D (0.2 µM) dissociation as measured by light scattering at saturated [ADP] of 25 µM. The solid line represents the best fit to the sum of exponential representing lag and the observed process as described previously64, error bars of the fitting are within data points. (F) The kinetic reaction mechanism for ADP release from Acto·Myo19-3IQ.
