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

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Abstract
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.