Kinesin heads fused to hinge-free myosin tails drive efficient motility.
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.
Eickel
Verena
V
Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK. r.cross@mcri.ac.uk
Drummond
Douglas
D
Carter
Nick
N
Lockhart
Andrew
A
Jones
John Kendrick
JK
Cross
Robert
R
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
D011994:Recombinant Proteins; D024462:Myosin Type II; D009218:Myosins; D016547:Kinesins