Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin

by: Kenji Kawaguchi, Shin'ichi Ishiwata

Science, Vol. 291, No. 5504. (26 January 2001), pp. 667-669.

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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.

@article{Kawaguchi2001, 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.}, author = {Kawaguchi, Kenji and Ishiwata, Shin'ichi }, citeulike-article-id = {1356311}, doi = {10.1126/science.291.5504.667}, journal = {Science}, keywords = {kinesin, motor}, month = {January}, number = {5504}, pages = {667--669}, posted-at = {2007-06-01 21:43:21}, priority = {3}, title = {Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin}, url = {http://dx.doi.org/10.1126/science.291.5504.667}, volume = {291}, year = {2001} }

RIS record

TY - JOUR ID - Kawaguchi2001 L3 - citeulike-article-id:1356311 TI - Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin JF - Science VL - 291 IS - 5504 SP - 667 EP - 669 N2 - 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. KW - kinesin KW - motor AU - Kawaguchi, Kenji AU - Ishiwata, Shin'ichi PY - 2001/01/26/ UR - http://dx.doi.org/10.1126/science.291.5504.667 ER -

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