FEBS Letters | |
Effect of temperature on kinesin‐driven microtubule gliding and kinesin ATPase activity | |
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
【 预 览 】
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