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 temper ature from 25 to 30 degrees C caused a conformational transition. To gain i nsight into functional consequences of such a transition, we studied the te mperature dependence of a full-length kinesin by measuring both the velocit y of microtubule gliding across kinesin-coated surfaces and microtubule-pro moted kinesin ATPase activity in solution. The corresponding Arrhenius plot s revealed distinct breaks at 27 degrees C, corroborating the temperature-d ependent conformational transition for a motility-competent full-length kin esin, Microtubules were found to glide up to 45 degrees C; at higher temper atures, kinesin was irreversibly damaged. (C) 2000 Federation of European B iochemical Societies.