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.
Böhm
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KJ
Institute of Molecular Biotechnology, Research Group of Molecular Cytology/Electron Microscopy, Beutenbergstrasse 11, D-07745, Jena, Germany. kboehm@imb-jena.de
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D000818:Animals; D001923:Brain Chemistry; D066298:In Vitro Techniques; D016547:Kinesins / Q000737:chemistry* / Q000502:physiology*; D008870:Microtubules / Q000502:physiology*; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009068:Movement; D011487:Protein Conformation; D013552:Swine; D013696:Temperature; D013816:Thermodynamics
D020409:Molecular Motor Proteins; D016547:Kinesins