Abstract
Many types of cellular motility are driven by motor proteins of the myosin family. On the one hand the diversity of functions ranging from muscle contraction to cell locomotion, intracellular transport or even signal transduction in hearing is reflected in differences in structure, mechanics and regulation between different classes of myosins. On the other hand recent structural, kinetic and single molecule mechanical studies revealed basic mechanisms of chemo-mechanical energy transduction that seem to be shared amongst myosin motors, such as a working stroke in two phases coupled to the release of Pi and ADP or strain dependence of ADP release. Many details of the basic mechanism still remain unclear, including the effect of stall forces on the mechanics of a single motor head. Because of their large working stroke and relatively slow kinetics non-muscle myosins including myosin V are well suited to investigate details of the basic mechanism. Using optical tweezers we have resolved load dependent conformational changes of single-headed myosin V constructs near stall and will discuss implications of these findings for the general mechanism of myosin motility and for processive movement of the native, dimeric myosin V motor. Supported by MRC and NIH.
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