Interaction Between Motor Domains Can Explain the Complex Dynamics of Heterodimeric Kinesins

Abstract

Motor proteins are active enzyme molecules that play a crucial role in many biological processes. They transform the chemical energy into the mechanical work and move unidirectionally along rigid cytoskeleton filaments. Single-molecule experiments suggest that motor proteins, consisting of two motor domains, move in a hand-over-hand mechanism when each subunit changes between trailing and leading positions in alternating steps, and these subunits do not interact with each other. However, recent experiments on heterodimeric kinesins suggest that the motion of motor domains is not independent, but rather strongly coupled and coordinated, although the mechanism of these interactions are not known. We propose a simple discrete stochastic model to describe the dynamics of homodimeric and heterodimeric two-headed motor proteins. It is argued that interactions between motor domains modify free energy landscapes of each motor subunit, and motor proteins still move via the hand-over-hand mechanism but with different transitions rates. Our calculations of biophysical properties agree with experimental observations. Several ways to test the theoretical model are proposed.Comment: To appear in New J. Phy