Pathway of processive ATP hydrolysis by kinesin
- 1 February 1995
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 373 (6516), 671-676
- https://doi.org/10.1038/373671a0
Abstract
Direct measurement of the kinetics of kinesin dissociation from microtubules, the release of phosphate and ADP from kinesin, and rebinding of kinesin to the microtubule have defined the mechanism for the kinesin ATPase cycle. The processivity of ATP hydrolysis is ten molecules per site at low salt concentration but is reduced to one ATP per site at higher salt concentration. Kinesin dissociates from the microtubule after ATP hydrolysis. This step is rate-limiting. The subsequent rebinding of kinesin - ADP to the microtubule is fast, so kinesin spends only a small fraction of its duty cycle in the dissociated state. These results provide an explanation for the motility differences between skeletal myosin and kinesin.Keywords
This publication has 27 references indexed in Scilit:
- Direct, Real-Time Measurement of Rapid Inorganic Phosphate Release Using a Novel Fluorescent Probe and Its Application to Actomyosin Subfragment 1 ATPaseBiochemistry, 1994
- Pre-Steady-State Kinetics of the Microtubule.cntdot.Kinesin ATPaseBiochemistry, 1994
- Expression, purification, and characterization of the Drosophila kinesin motor domain produced in Escherichia coliBiochemistry, 1993
- Decoration of the microtubule surface by one kinesin head per tubulin heterodimerNature, 1993
- Chemomechanical cycle of kinesin differs from that of myosinNature, 1993
- Bead movement by single kinesin molecules studied with optical tweezersNature, 1990
- Microtubules accelerate ADP release by dyneinBiochemistry, 1989
- Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindleNature, 1985
- Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMP-PNPNature, 1985
- New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as subtrates for various enzymesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983