Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex

Article Abstract:

A study of the microtubule cytoskeleton in eukaryotes using unfertilized Xenopus eggs show that the highly conserved protein, gamma-tubulin, plays an important role in microtubule nucleation. Analysis of the protein using electron microscopy revealed at least seven proteins, with each protein having an open ring structure. Further analysis of the proteins showed that the ring structure contains a microtubule-nucleating unit that produces a new minus end of a microtubule.

Xenopus, Cytoskeleton

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Decoration of the microtubule surface by one kinesin head per tubulin heterodimer

Article Abstract:

Interaction between kinesin motor domain and the microtubule surface is marked by binding saturated at one kinesin head per tubulin heterodimer. Kinesin head is the microtubule and adenosine triphosphate (ATP) binding site-containing part of kinesin, an ATPase. Saturation binding and electron microscopy revealed that kinesin is bound to the microtubule surface lattice in an orderly pattern that magnesium-ATP can break apart.

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Pathway of processive ATP hydrolysis by kinesin

Article Abstract:

Kinetic studies of ATP hydrolysis by kinesin indicate that dissociation of kinesin from the microtubule after ATP hydrolysis is the rate-determining step. Salt concentrations influence the processivity of ATP hydrolysis. Motility differences between skeletal kinesin and myosin are explained by the fraction of the time kinesin exists in the dissociated state.

Adenosine triphosphate, ATP, Hydrolysis

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