Positional isomers of a non-nucleoside substrate differentially affect myosin function release_5q3gdrpldfgardnmqviiw7jssa

by Edward Debold, Mike Woodward, Eric Ostrander, Seung Jeong, Xiarong Liu, Brent Scott, Matt Unger, Jianhan Chen, Dhandapani Venkataraman

Released as a post by Cold Spring Harbor Laboratory.



Molecular motors have evolved to transduce chemical energy from adenosine triphosphate 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 in myosin's mechano-chemical cycle. Our studies demonstrate that subtle variations in the structure of an abiotic energy source can be used to control the force and motility of myosin without altering myosin's structure.
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Date   2019-12-17
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