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Force production by single kinesin motors

Nature Cell Biology volume 2, pages 718–723 (2000)Cite this article

Abstract

Motor proteins such as kinesin, myosin and polymerase convert chemical energy into work through a cycle that involves nucleotide hydrolysis. Kinetic rates in the cycle that depend upon load identify transitions at which structural changes, such as power strokes or diffusive motions, are likely to occur. Here we show, by modelling data obtained with a molecular force clamp, that kinesin mechanochemistry can be characterized by a mechanism in which a load-dependent isomerization follows ATP binding. This model quantitatively accounts for velocity data over a wide range of loads and ATP levels, and indicates that movement may be accomplished through two sequential 4-nm substeps. Similar considerations account for kinesin processivity, which is found to obey a load-dependent Michaelis–Menten relationship.

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Figure 1: Load-dependent isomerization.
Figure 2: Global fits of velocity to equations (1) and (4).
Figure 3: Global fits of mean run length to equation (5).
Figure 4: Proposed mechanochemical cycle of kinesin.

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Acknowledgements

We thank T. Perkins and L. Satterwhite for helpful discussions, J. de Georgis for squid dissection, and D. Peoples for expert machining. Experiments were carried out at Princeton University and were supported by grants from the NIGMS, NSF and W.M. Keck Foundation (to S.M.B.), predoctoral fellowships from the American Heart Association, the Charlotte Elizabeth Proctor Fund and the Program in Mathematics and Molecular Biology Burroughs Wellcome Fund (to M.J.S.), and a postdoctoral fellowship from the Burroughs Wellcome Fund of the Life Sciences Research Foundation (to K.V.). Data analysis and modelling were also supported by Lucent Technologies.

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  1. Mark J. Schnitzer and Koen Visscher: These authors contributed equally to this work.

Authors and Affiliations

  1. Biological Computation Research Department, Bell Laboratories, Lucent Technologies, Murray Hill, 07974, New Jersey, USA

    Mark J. Schnitzer

  2. Departments of Physics and Molecular and Cellular Biology, University of Arizona, Tucson, 85721, Arizona, USA

    Koen Visscher

  3. Departments of Applied Physics and Biological Sciences, Stanford University, Stanford, 94305, California, USA

    Steven M. Block

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  1. Mark J. Schnitzer
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Correspondence to Koen Visscher.

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Schnitzer, M., Visscher, K. & Block, S. Force production by single kinesin motors. Nat Cell Biol 2, 718–723 (2000). https://doi.org/10.1038/35036345

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