title: A force-dependent state controls the coordination of processive myosin V.
abstract: Myosin V is an efficient processive molecular motor. Recent experiments have shown how the structure and kinetics of myosin V are specialized to produce a highly processive motor capable of taking multiple 36-nm steps on an actin filament track. Here, we examine how two identical heads coordinate their activity to produce efficient hand-over-hand stepping. We have used a modified laser-trap microscope to apply a approximately 2-pN forward or backward force on a single-headed myosin V molecule, hypothesized to simulate forces experienced by the rear or lead head, respectively. We found that pulling forward produces only a small change in the kinetics, whereas pulling backward induces a large reduction in the cycling of the head. These results support a model in which the coordination of myosin V stepping is mediated by strain-generated inhibition of the lead head.
authors.affiliation: Department of Biochemistry, Stanford University Medical Center, Stanford, CA 94305, USA.
authors.forename: Thomas J
authors.initials: TJ
authors.lastname: Purcell
authors.forename: H Lee
authors.initials: HL
authors.lastname: Sweeney
authors.forename: James A
authors.initials: JA
authors.lastname: Spudich
mesh_terms: D000818:Animals; D018613:Microscopy, Confocal; D020409:Molecular Motor Proteins / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*; D024701:Myosin Type V / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*
chemical_list: D020409:Molecular Motor Proteins; D024701:Myosin Type V