IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v400y1999i6740d10.1038_22146.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/22146
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/22146?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    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. 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.
    3. 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.
    4. 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.
    5. 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.
    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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:400:y:1999:i:6740:d:10.1038_22146. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.