Direct observation of single kinesin molecules moving along microtubules

Article Abstract:

Low-background total internal reflection fluorescence microscopy is used to observe the movement of fluorescent labeled kinesin molecules at the physiological ionic strength, along a microtubule. The kinesin molecule moves even in the absence of linkage between the motor and cargo, while the kinesin molecule moves through an average distance of 600 nanometer after it is linked to the microtubule. Processive movement is observed only for kinesin molecules with two motor domain, and not for molecules with one motor domain.

Usage, Observations, Fluorescence microscopy, Microtubules

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Chemomechanical cycle of kinesin differs from that of myosin

Article Abstract:

Analysis of microtubule movement shows that kinesin's chemomechanical cycle is unlike the cycle followed by two other motor proteins, myosin and dynein. All three proteins use a chemomechanical pathway to allow the muscles to obtain the energy needed for work from adenosine triphosphate (ATP). However, while dynein and myosin quickly break away from their filaments after attaching to ATP, kinesin remains linked to its microtubules in the initial stages of the hydrolysis cycle.

Physiological aspects, Muscle proteins, Dynein, Myosin

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A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd

Article Abstract:

The mechanical event in the minus-end-directed Ncd (rotation of the coiled-coil neck) is coupled to the same step of the ATPase cycle (ATP binding) as the mechanical event in the plus-end-directed kinesins. Ncd convergently evolves a large-scale rotation of an elongated lever and the primary use of only one of the two heads in the motor dimer.

Science & research, Adenosine triphosphate, ATP, Chemical properties, Dimer acids

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