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  • Title: One-dimensional diffusion of microtubules bound to flagellar dynein.
    Author: Vale RD, Soll DR, Gibbons IR.
    Journal: Cell; 1989 Dec 01; 59(5):915-25. PubMed ID: 2531633.
    Abstract:
    Dynein is a multisubunit ATPase that powers microtubule-based motility. We find that a dissociated dynein particle containing the beta heavy chain subunit translocates microtubules unidirectionally over a glass surface in the presence of ATP. However, after nucleotide hydrolysis is inhibited by vanadate, unidirectional translocation ceases, and microtubules instead undergo irregular back-and-forth motion along their longitudinal axes. Quantitative analysis reveals that this motion is due to thermal-driven diffusion, but, unlike a particle undergoing Brownian motion, the diffusion is restricted to one dimension. The properties of the diffusional movement indicate that dynein can interact with microtubules in a way that permits the latter to diffuse only along their longitudinal axes. This weak binding interaction may constitute an important intermediate state in dynein's force-generating cycle.
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