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Effect of temperature on kinesin‐driven microtubule gliding and kinesin ATPase activity
Author(s) -
Böhm Konrad J.,
Stracke Roland,
Baum Marina,
Zieren Martin,
Unger Eberhard
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01757-3
Subject(s) - kinesin , microtubule , chemistry , biophysics , circular dichroism , atpase , tubulin , crystallography , biology , microbiology and biotechnology , biochemistry , enzyme
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.