Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin
- 26 January 2001
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 291 (5504) , 667-669
- https://doi.org/10.1126/science.291.5504.667
Abstract
The motility of kinesin motors is explained by a “hand-over-hand” model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.Keywords
This publication has 26 references indexed in Scilit:
- Temperature Dependence of Force, Velocity, and Processivity of Single Kinesin MoleculesBiochemical and Biophysical Research Communications, 2000
- A new look at the microtubule binding patterns of dimeric kinesinsJournal of Molecular Biology, 2000
- Alternating Site Mechanism of the Kinesin ATPaseBiochemistry, 1998
- Release of Isolated Single Kinesin Molecules from MicrotubulesBiochemistry, 1998
- The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent MotilityCell, 1997
- The Movement of Kinesin Along MicrotubulesAnnual Review of Physiology, 1996
- Unbinding force of a single motor molecule of muscle measured using optical tweezersNature, 1995
- Kinesin and ncd Bind Through a Single Head to Microtubules and Compete for a Shared MT Binding SiteJournal of Molecular Biology, 1995
- Force and velocity measured for single kinesin moleculesCell, 1994
- Bead movement by single kinesin molecules studied with optical tweezersNature, 1990