A mutation in switch I alters the load-dependent kinetics of myosin Va.

ABSTRACT: Myosin Va is the molecular motor that drives intracellular vesicular transport, powered by the transduction of chemical energy from ATP into mechanical work. The coupling of the powerstroke and phosphate (P_i) release is key to understanding the transduction process, and crucial details of this process remain unclear. Therefore, we determined the effect of elevated P_i on the force-generating capacity of a mini-ensemble of myosin Va S1 (WT) in a laser trap assay. By increasing the stiffness of the laser trap we determined the effect of increasing resistive loads on the rate of P_i-induced detachment from actin, and quantified this effect using the Bell approximation. We observed that WT myosin generated higher forces and larger displacements at the higher lase

SUBMITTER: Marang C 

PROVIDER: S-EPMC10229639 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature