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. 2003 Jul 31;424(6948):574-7.
doi: 10.1038/nature01804.

Processivity of the single-headed kinesin KIF1A through biased binding to tubulin

Yasushi Okada  1 , Hideo Higuchi, Nobutaka Hirokawa
Affiliations

Processivity of the single-headed kinesin KIF1A through biased binding to tubulin

Yasushi Okada et al. Nature. .

Abstract

Conventional isoforms of the motor protein kinesin behave functionally not as 'single molecules' but as 'two molecules' paired. This dimeric structure poses a barrier to solving its mechanism. To overcome this problem, we used an unconventional kinesin KIF1A (refs 5, 6) as a model molecule. KIF1A moves processively as an independent monomer, and can also work synergistically as a functional dimer. Here we show, by measuring its movement with an optical trapping system, that a single ATP hydrolysis triggers a single stepping movement of a single KIF1A monomer. The step size is distributed stochastically around multiples of 8 nm with a gaussian-like envelope and a standard deviation of 15 nm. On average, the step is directional to the microtubule's plus-end against a load force of up to 0.15 pN. As the source for this directional movement, we show that KIF1A moves to the microtubule's plus-end by approximately 3 nm on average on binding to the microtubule, presumably by preferential binding to tubulin on the plus-end side. We propose a simple physical formulation to explain the movement of KIF1A.

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