Article

Thermal activation of single kinesin molecules with temperature pulse microscopy

  1. Kenji Kawaguchi1,
  2. Shin'ichi Ishiwata1,2,3,4,*

Article first published online: 12 APR 2001

DOI: 10.1002/cm.1019

Issue

Cell Motility and the Cytoskeleton

Cell Motility and the Cytoskeleton

Volume 49, Issue 1, pages 41–47, May 2001

Additional Information

How to Cite

Kawaguchi, K. and Ishiwata, S. (2001), Thermal activation of single kinesin molecules with temperature pulse microscopy. Cell Motility and the Cytoskeleton, 49: 41–47. doi: 10.1002/cm.1019

Author Information

  1. 1

    Department of Physics, School of Science and Engineering, Waseda University, Tokyo, Japan

  2. 2

    Advanced Research Institute for Science and Engineering, Waseda University, Tokyo, Japan

  3. 3

    Materials Research Laboratory for Bioscience and Photonics, Waseda University, Tokyo, Japan

  4. 4

    Core Research for Evolutional Science and Technology, “Genetic Programming” Team 13, Kawasaki, Japan

*Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan

Publication History

  1. Issue published online: 12 APR 2001
  2. Article first published online: 12 APR 2001
  3. Manuscript Accepted: 7 FEB 2001
  4. Manuscript Received: 30 OCT 2000

Funded by

  • Grants-in-Aid for Scientific Research
  • Ministry of Education, Science, Sports, and Culture of Japan
  • Grants-in-Aid from Japan Science and Technology Corporation (CREST)

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Keywords:

  • Arrhenius plot;
  • motor protein;
  • microtubule;
  • temperature effect on kinesin;
  • single molecule assay

Abstract

Conventional kinesin is a processive motor protein that keeps “walking” along a microtubule using chemical energy released by ATP hydrolysis. We previously studied the effects of temperature between 15° and 35°C on the moving velocity, force, and processivity of single kinesin molecules using a bead assay [Kawaguchi and Ishiwata, 2000b: Biochem Biophys Res Commun 272:895–899]. However, we could not examine the effects of temperature higher than 35°C because of the thermal damage to proteins. Here, using temperature pulse microscopy (TPM) [Kato et al., 1999: Proc Natl Acad Sci USA 96:9602–9606], we could examine the temperature dependence of the gliding velocity of single kinesin molecules interacting with a microtubule above 35°C up to 50°C (instantaneously, ∼60°C), where the velocity reached 3.68 μm/s, the highest ever reported. The Arrhenius plot showed no breaks between 15° and 50°C with a unique activation energy of about 50 kJ/mol, suggesting that the molecular mechanism of kinesin motility is common over a broad temperature range including physiological temperature. Cell Motil. Cytoskeleton 49:41–47, 2001. © 2001 Wiley-Liss, Inc.

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