title: Kinesin heads fused to hinge-free myosin tails drive efficient motility.
abstract: The rat kinesin motor domain was fused at residues 433, 411, 376 or 367, respectively, to the C-terminal 1185, 1187, 1197 or 1185 residues of the brush border myosin tail. In motility assays, K433myt and K411myt, which preserve the head-proximal kinesin hinge, and K367myt, which deletes it, drove rapid microtubule sliding ( approximately 0.6 microms(-1)) that was optimal when the head-pairs were spaced apart by adding 1:1 headless myosin tails. K376myt, which partially deletes the head-proximal hinge, showed poor motility in sliding assays but wild type processivity, velocity and stall force in single molecule optical trapping. Accordingly, the head-proximal kinesin hinge is functionally dispensable.
authors.affiliation: Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK. r.cross@mcri.ac.uk
authors.forename: Verena
authors.initials: V
authors.lastname: Eickel
authors.forename: Douglas
authors.initials: D
authors.lastname: Drummond
authors.forename: Nick
authors.initials: N
authors.lastname: Carter
authors.forename: Andrew
authors.initials: A
authors.lastname: Lockhart
authors.forename: John Kendrick
authors.initials: JK
authors.lastname: Jones
authors.forename: Robert
authors.initials: R
authors.lastname: Cross
mesh_terms: D000595:Amino Acid Sequence; D016547:Kinesins / Q000737:chemistry* / Q000648:ultrastructure; D008870:Microtubules / Q000502:physiology; D008871:Microvilli / Q000502:physiology*; D008969:Molecular Sequence Data; D024462:Myosin Type II / Q000737:chemistry / Q000648:ultrastructure; D009218:Myosins / Q000737:chemistry* / Q000648:ultrastructure; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry / Q000648:ultrastructure; D015183:Restriction Mapping
chemical_list: D011994:Recombinant Proteins; D024462:Myosin Type II; D009218:Myosins; D016547:Kinesins