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Processivity of kinesin motility is enhanced on increasing temperature

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 kin...

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Detalles Bibliográficos
Autores principales: Nara, Ikuko, Ishiwata, Shin’ichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036643/
https://www.ncbi.nlm.nih.gov/pubmed/27857556
http://dx.doi.org/10.2142/biophysics.2.13
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author Nara, Ikuko
Ishiwata, Shin’ichi
author_facet Nara, Ikuko
Ishiwata, Shin’ichi
author_sort Nara, Ikuko
collection PubMed
description 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.
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spelling pubmed-50366432016-11-17 Processivity of kinesin motility is enhanced on increasing temperature Nara, Ikuko Ishiwata, Shin’ichi Biophysics (Nagoya-shi) Articles 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. The Biophysical Society of Japan (BSJ) 2006-02-22 /pmc/articles/PMC5036643/ /pubmed/27857556 http://dx.doi.org/10.2142/biophysics.2.13 Text en 2006 © The Biophysical Society of Japan
spellingShingle Articles
Nara, Ikuko
Ishiwata, Shin’ichi
Processivity of kinesin motility is enhanced on increasing temperature
title Processivity of kinesin motility is enhanced on increasing temperature
title_full Processivity of kinesin motility is enhanced on increasing temperature
title_fullStr Processivity of kinesin motility is enhanced on increasing temperature
title_full_unstemmed Processivity of kinesin motility is enhanced on increasing temperature
title_short Processivity of kinesin motility is enhanced on increasing temperature
title_sort processivity of kinesin motility is enhanced on increasing temperature
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036643/
https://www.ncbi.nlm.nih.gov/pubmed/27857556
http://dx.doi.org/10.2142/biophysics.2.13
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