Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity.


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 degrees 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 degrees C, corroborating the temperature-dependent conformational transition for a motility-competent full-length kinesin. Microtubules were found to glide up to 45 degrees C; at higher temperatures, kinesin was irreversibly damaged.


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@article{Bhm2000EffectOT, title={Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity.}, author={K . J . B{\"{o}hm and Roland Stracke and Molly Baum and Max Zieren and Eberhard Unger}, journal={FEBS letters}, year={2000}, volume={466 1}, pages={59-62} }