MKLP2 is a divergent molecular motor that has structurally evolved to bind its microtubule track and use the energy of ATP in distinct ways, tuned according to its function in cell division.
Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.
Individual nonmuscle myosin 2 filaments in cells may differ their mechanical and kinetic properties depending on the myosin paralog composition giving the cells a mechanism for fine tuning the output of a given nonmuscle myosin filament.
The protofilaments that curl outward from a disassembling microtubule tip carry a large amount of strain energy and they can drive movement with an efficiency similar to conventional motor proteins.
The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.
Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.
In vitro reconstitution of mRNA motility reveals the basis of directionally biased motion by groups of motors, their response to potential obstacles, and the consequences of reaching microtubule ends.
Quantitative experiments and theory show that the tension-dependent regulation of NDC80 binding to kinetochore microtubules arises from a combination of the changing Aurora B concentration at NDC80 and the nonlinearity of Aurora B autoactivation.
