Effect of temperature on kinesin‐driven microtubule gliding and kinesin ATPase activity

FEBS Letters

Zieren, Martin¹  Unger, Eberhard²  Böhm, Konrad J.²  Stracke, Roland²  Baum, Marina² 

[1] Institute for Physical High Technology, Helmholtzweg 4, D-07743 Jena, Germany;Institute of Molecular Biotechnology, Research Group of Molecular Cytology/Electron Microscopy, Beutenbergstrasse 11, D-07745 Jena, Germany

关键词: Microtubule;    Kinesin;    Motility;    ATPase activity;    Temperature;    Thermal stability;   

DOI  :  10.1016/S0014-5793(99)01757-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

DeCuevas et al. [J. Cell Biol. 116 (1992) 957–965] demonstrated by circular dichroism spectroscopy for the kinesin stalk fragment that shifting temperature from 25 to 30°C caused a conformational transition. To gain insight into functional consequences of such a transition, we studied the temperature dependence of a full-length kinesin by measuring both the velocity of microtubule gliding across kinesin-coated surfaces and microtubule-promoted kinesin ATPase activity in solution. The corresponding Arrhenius plots revealed distinct breaks at 27°C, corroborating the temperature-dependent conformational transition for a motility-competent full-length kinesin. Microtubules were found to glide up to 45°C; at higher temperatures, kinesin was irreversibly damaged.

【 授权许可】

Unknown