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Single kinesin molecules studied with a molecular force clamp

Author

Listed:
  • Koen Visscher

    (Department of Molecular Biology
    Princeton Materials Institute)

  • Mark J. Schnitzer

    (Department of Molecular Biology
    Princeton University)

  • Steven M. Block

    (Department of Molecular Biology
    Princeton Materials Institute
    Princeton University)

Abstract

Kinesin is a two-headed, ATP-driven motor protein that moves processively along microtubules in discrete steps of 8 nm, probably by advancing each of its heads alternately in sequence1,2,3,4. Molecular details of how the chemical energy stored in ATP is coupled to mechanical displacement remain obscure. To shed light on this question, a force clamp was constructed, based on a feedback-driven optical trap capable of maintaining constant loads on single kinesin motors5. The instrument provides unprecedented resolution of molecular motion and permits mechanochemical studies under controlled external loads. Analysis of records of kinesin motion under variable ATP concentrations and loads revealed several new features. First, kinesin stepping appears to be tightly coupled to ATP hydrolysis over a wide range of forces, with a single hydrolysis per 8-nm mechanical advance. Second, the kinesin stall force depends on the ATP concentration. Third, increased loads reduce the maximum velocity as expected, but also raise the apparent Michaelis–Menten constant. The kinesin cycle therefore contains at least one load-dependent transition affecting the rate at which ATP molecules bind and subsequently commit to hydrolysis. It is likely that at least one other load-dependent rate exists, affecting turnover number. Together, these findings will necessitate revisions to our understanding of how kinesin motors function.

Suggested Citation

  • Koen Visscher & Mark J. Schnitzer & Steven M. Block, 1999. "Single kinesin molecules studied with a molecular force clamp," Nature, Nature, vol. 400(6740), pages 184-189, July.
  • Handle: RePEc:nat:nature:v:400:y:1999:i:6740:d:10.1038_22146
    DOI: 10.1038/22146
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    Cited by:

    1. Chou, Y.C. & Hsiao, Yi-Feng & To, Kiwing, 2015. "Dynamic model of the force driving kinesin to move along microtubule—Simulation with a model system," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 433(C), pages 66-73.
    2. Bibi Najma & Minu Varghese & Lev Tsidilkovski & Linnea Lemma & Aparna Baskaran & Guillaume Duclos, 2022. "Competing instabilities reveal how to rationally design and control active crosslinked gels," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. Peter Keller & Sylvie Rœlly & Angelo Valleriani, 2015. "A Quasi Random Walk to Model a Biological Transport Process," Methodology and Computing in Applied Probability, Springer, vol. 17(1), pages 125-137, March.
    4. Lipowsky, Reinhard & Klumpp, Stefan, 2005. "‘Life is motion’: multiscale motility of molecular motors," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 352(1), pages 53-112.
    5. Lv, Wangyong & Wang, Huiqi & Lin, Lifeng & Wang, Fei & Zhong, Suchuan, 2015. "Transport properties of elastically coupled fractional Brownian motors," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 437(C), pages 149-161.
    6. Woochul Nam & Bogdan I Epureanu, 2016. "Effects of Obstacles on the Dynamics of Kinesins, Including Velocity and Run Length, Predicted by a Model of Two Dimensional Motion," PLOS ONE, Public Library of Science, vol. 11(1), pages 1-18, January.

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