title: Directionality and processivity of molecular motors.
abstract: Analysis of a mutant with altered directionality has led to new insights into motor directionality. The prediction from current models for processivity of a two-heads-bound state has been confirmed by electron microscopy for myosin V and by unbinding experiments for kinesin. Evidence is emerging that non-processive motors bind their filament with one head, hydrolyze ATP and then release, requiring binding by a second motor to complete a step.
authors.affiliation: Center for Interdisciplinary Research and Department of Metallurgy, Graduate School of Engineering, Tohoku University, 980-8579, Sendai, Japan. higuchi@material.tohoku.ac.jp
authors.forename: Hideo
authors.initials: H
authors.lastname: Higuchi
authors.forename: Sharyn A
authors.initials: SA
authors.lastname: Endow
mesh_terms: D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009218:Myosins / Q000737:chemistry / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D009218:Myosins; D016547:Kinesins