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. 1996 Mar 5;93(5):1913–1917. doi: 10.1073/pnas.93.5.1913

Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy.

C M Coppin 1, J T Finer 1, J A Spudich 1, R D Vale 1
PMCID: PMC39882  PMID: 8700858

Abstract

Kinesin is a molecular motor that transports organelles along microtubules. This enzyme has two identical 7-nm-long motor domains, which it uses to move between consecutive tubulin binding sites spaced 8 nm apart along a microtubular protofilament. The molecular mechanism of this movement, which remains to be elucidated, may be common to all families of motor proteins. In this study, a high-resolution optical-trap microscope was used to measure directly the magnitude of abrupt displacements produced by a single kinesin molecule transporting a microscopic bead. The distribution of magnitudes reveals that kinesin not only undergoes discrete 8-nm movements, in agreement with previous work [Svoboda, K., Schmidt, C. F., Schnapp, B. J. & Block, S.M. (1993) Nature (London) 365, 721-727], but also frequently exhibits smaller movements of about 5 nm. A possible explanation for these unexpected smaller movements is that kinesin's movement from one dimer to the next along a protofilament involves at least two distinct events in the mechanical cycle.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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