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Processivity of kinesin motility is enhanced on increasing temperature.

ABSTRACT: Kinesin is a motor protein that processively moves step by step along a microtubule. To investigate the effects of temperature on run length, i.e., processivity of kinesin motility, we performed a single-molecular bead assay at temperature range of 20-40°C. An increase in the walking velocity of kinesin corresponded to the Arrhenius activation enthalpy of 48 kJ/mol, being consistent with the previous reports. Here, we found that the run length increased, that is, the kinesin processivity enhanced with increasing temperature. Then, we estimated the probability of detachment of kinesin from a microtubule per one 8-nm stepping event, and found that it diminishes from 0.014 to 0.006/step with increasing temperature from 20 to 40°C. And we noticed that prolonged incubation at 30, 35 and 40°C significantly slowed down the walking velocity, but further increased the run length and duration. Those results are interpreted according to the effect of temperature on the rate constants of some key kinetic steps in the ATPase cycle.

SUBMITTER: Nara I

PROVIDER: S-EPMC5036643 | biostudies-literature | 2006

REPOSITORIES: biostudies-literature

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Processivity of kinesin motility is enhanced on increasing temperature.

Nara Ikuko I Ishiwata Shin'ichi S

Biophysics (Nagoya-shi, Japan) 20060222

Kinesin is a motor protein that processively moves step by step along a microtubule. To investigate the effects of temperature on run length, i.e., processivity of kinesin motility, we performed a single-molecular bead assay at temperature range of 20-40°C. An increase in the walking velocity of kinesin corresponded to the Arrhenius activation enthalpy of 48 kJ/mol, being consistent with the previous reports. Here, we found that the run length increased, that is, the kinesin processivity enhance ...[more]

PMID: 27857556

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