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Kinesin hydrolyses one ATP per 8-nm step

Author

Listed:
  • Mark J. Schnitzer

    (Princeton University
    †Molecular Biology, Princeton University)

  • Steven M. Block

    (†Molecular Biology, Princeton University
    ‡Princeton Materials Institute, Princeton University)

Abstract

Kinesin is a two-headed, ATP-dependent motor protein1,2 that moves along microtubules indiscrete steps3 of 8 nm. In vitro, single molecules produceprocessive movement4,5, motors typically take ∼100steps before releasing from a microtubule5,6,7 . A central question relates tomechanochemical coupling in this enzyme: how many molecules ofATP are consumed per step? For the actomyosin system,experimental approaches to this issue have generated considerablecontroversy8,9. Here we take advantage of theprocessivity of kinesin to determine the coupling ratio withoutrecourse to direct measurements of ATPase activity, which aresubject to large experimental uncertainties8,10,11,12. Beads carrying singlemolecules of kinesin moving on microtubules were tracked with highspatial and temporal resolution by interferometry3,13. Statistical analysis of theintervals between steps at limiting ATP, and studies offluctuations in motor speed as a function of ATPconcentration14,15, allow the coupling ratio to bedetermined. At near-zero load, kinesin moleculeshydrolyse a single ATP molecule per 8-nm advance. Thisfinding excludes various one-to-many andmany-to-one coupling schemes, analogous to thoseadvanced for myosin, and places severe constraints on models for movement.

Suggested Citation

  • Mark J. Schnitzer & Steven M. Block, 1997. "Kinesin hydrolyses one ATP per 8-nm step," Nature, Nature, vol. 388(6640), pages 386-390, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41111
    DOI: 10.1038/41111
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    Cited by:

    1. Ashwin I. D’Souza & Rahul Grover & Gina A. Monzon & Ludger Santen & Stefan Diez, 2023. "Vesicles driven by dynein and kinesin exhibit directional reversals without regulators," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Teagan E. Bate & Megan E. Varney & Ezra H. Taylor & Joshua H. Dickie & Chih-Che Chueh & Michael M. Norton & Kun-Ta Wu, 2022. "Self-mixing in microtubule-kinesin active fluid from nonuniform to uniform distribution of activity," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. 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.
    4. Shreyas Bhaban & Donatello Materassi & Mingang Li & Thomas Hays & Murti Salapaka, 2016. "Interrogating Emergent Transport Properties for Molecular Motor Ensembles: A Semi-analytical Approach," PLOS Computational Biology, Public Library of Science, vol. 12(11), pages 1-30, November.
    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. Lipowsky, Reinhard & Chai, Yan & Klumpp, Stefan & Liepelt, Steffen & Müller, Melanie J.I., 2006. "Molecular motor traffic: From biological nanomachines to macroscopic transport," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 372(1), pages 34-51.
    7. 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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