Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function.

ABSTRACT: Molecular motors have evolved to transduce chemical energy from ATP into mechanical work to drive essential cellular processes, from muscle contraction to vesicular transport. Dysfunction of these motors is a root cause of many pathologies necessitating the need for intrinsic control over molecular motor function. Herein, we demonstrate that positional isomerism can be used as a simple and powerful tool to control the molecular motor of muscle, myosin. Using three isomers of a synthetic non-nucleoside triphosphate, we demonstrate that myosin's force- and motion-generating capacity can be dramatically altered at both the ensemble and single-molecule levels. By correlating our experimental results with computation, we show that each isomer exerts intrinsic control by affecting distinct steps

SUBMITTER: Woodward M 

PROVIDER: S-EPMC7401181 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature