Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

Article Abstract:

The inhibition of kinesin's binding of microtubules and the slow hydrolysis of ATP, in solution, appears due to the attachment of tail domains to the motor domains of kinesin in a folded configuration. Immobilized kinesin with one dimeric molecule tightly binds with and drives the sliding of a microtubule. DKH392, an experimental construct possessing two head and no tails, exhibits both high ATPase rates and diffusion with microtubules, validating highly processive kinesin activity with the motor remaining bound to microtubules through several cycles of ATP hydrolysis.

Protein binding

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Molecular motors join forces

Article Abstract:

Animal cells use various transport systems to deliver membrane-bound components to the periphery of the cell. Molecular motors (trains) undertake long-range movements, with microtubules as the tracks. Different sorts of motors (vans) can undertake the last stage of the journey. Huang and colleagues have reported that cells incorporate the two methods of transport into one bifunctional vehicle, with the microtubule motor, myosin Va, and conventional kinesin directly interacting.

Observations, Cell research, Cytological research

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Polar explorations

Article Abstract:

Three experiments, on structurally similar kinesin and ncd proteins bound to tubulin subunits of a microtubule, show that orientation is primarily the same for different nucleotide states of kinesin and for ncd. Both motors have the same orientations and changes in bound nucleotide do not change the direction. It is important to mention polarity of the structures to achieve directed movement.

Analysis, Protein research

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