Extensibility of the extended tail domain of processive and nonprocessive myosin V molecules.
Myosin V is a single-molecule motor that moves organelles along actin. When myosin V pulls loads inside the cell in a highly viscous environment, the force on the motor is unlikely to be constant. We propose that the tether between the single-molecule motor and the cargo (i.e., the extended tail domain of the molecule) must be able to absorb the sudden mechanical motions of the motor and allow smooth relaxation of the motion of the cargo to a new position. To test this hypothesis, we compared the elastic properties of the extended tail domains of processive (mouse myosin Va) and nonprocessive (Drosophila myosin V) molecular motors. The extended tail domain of these myosins consists of mechanically strong coiled-coil regions interspersed with flexible loops. In this work we explored the mechanical properties of coiled-coil regions using atomic force microscopy. We found that the processive and nonprocessive coiled-coil fragments display different unfolding patterns. The unfolding of coiled-coil structures occurs much later during the atomic force microscopy stretch cycle for processive myosin Va than for nonprocessive Drosophila myosin V, suggesting that this elastic tether between the cargo and motor may play an important role in sustaining the processive motions of this single-molecule motor.
Nagy
Attila
A
Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA.
Piszczek
Grzegorz
G
Sellers
James R
JR
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004331:Drosophila melanogaster; D004548:Elasticity; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism; D051379:Mice; D018625:Microscopy, Atomic Force; D008854:Microscopy, Electron; D009068:Movement; D024701:Myosin Type V / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D019476:Insect Proteins; D024701:Myosin Type V