### 抄録

We studied the fluctuation in the translational sliding movement of microtubules driven by kinesin in a motility assay in vitro. By calculating the mean-square displacement deviation from the average as a function of time, we obtained motional diffusion coefficients for microtubules and analyzed the dependence of the coefficients on microtubule length. Our analyses suggest that 1) the motional diffusion coefficient consists of the sum of two terms, one that is proportional to the inverse of the microtubule length (as the longitudinal diffusion coefficient of a filament in Brownian movement is) and another that is independent of the length, and 2) the length-dependent term decreases with increasing kinesin concentration. This latter term almost vanishes within the length range we studied at high kinesin concentrations. From the length-dependence relationship, we evaluated the friction coefficient for sliding microtubules. This value is much larger than the solvent friction and thus consistent with protein friction. The length independence of the motional diffusion coefficient observed at sufficiently high kinesin concentrations indicates the presence of correlation in the sliding movement fluctuation. This places significant constraint on the possible mechanisms of the sliding movement generation by kinesin motors in vitro.

元の言語 | 英語 |
---|---|

ページ（範囲） | 878-886 |

ページ数 | 9 |

ジャーナル | Biophysical Journal |

巻 | 70 |

発行部数 | 2 I |

DOI | |

出版物ステータス | 出版済み - 1 1 1996 |

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### All Science Journal Classification (ASJC) codes

- Biophysics

### これを引用

*Biophysical Journal*,

*70*(2 I), 878-886. https://doi.org/10.1016/S0006-3495(96)79631-5

**Fluctuation in the microtubule sliding movement driven by kinesin in vitro.** / Imafuku, Yasuhiro; Toyoshima, Yoko Y.; Tawada, Katsuhisa.

研究成果: ジャーナルへの寄稿 › 記事

*Biophysical Journal*, 巻. 70, 番号 2 I, pp. 878-886. https://doi.org/10.1016/S0006-3495(96)79631-5

}

TY - JOUR

T1 - Fluctuation in the microtubule sliding movement driven by kinesin in vitro

AU - Imafuku, Yasuhiro

AU - Toyoshima, Yoko Y.

AU - Tawada, Katsuhisa

PY - 1996/1/1

Y1 - 1996/1/1

N2 - We studied the fluctuation in the translational sliding movement of microtubules driven by kinesin in a motility assay in vitro. By calculating the mean-square displacement deviation from the average as a function of time, we obtained motional diffusion coefficients for microtubules and analyzed the dependence of the coefficients on microtubule length. Our analyses suggest that 1) the motional diffusion coefficient consists of the sum of two terms, one that is proportional to the inverse of the microtubule length (as the longitudinal diffusion coefficient of a filament in Brownian movement is) and another that is independent of the length, and 2) the length-dependent term decreases with increasing kinesin concentration. This latter term almost vanishes within the length range we studied at high kinesin concentrations. From the length-dependence relationship, we evaluated the friction coefficient for sliding microtubules. This value is much larger than the solvent friction and thus consistent with protein friction. The length independence of the motional diffusion coefficient observed at sufficiently high kinesin concentrations indicates the presence of correlation in the sliding movement fluctuation. This places significant constraint on the possible mechanisms of the sliding movement generation by kinesin motors in vitro.

AB - We studied the fluctuation in the translational sliding movement of microtubules driven by kinesin in a motility assay in vitro. By calculating the mean-square displacement deviation from the average as a function of time, we obtained motional diffusion coefficients for microtubules and analyzed the dependence of the coefficients on microtubule length. Our analyses suggest that 1) the motional diffusion coefficient consists of the sum of two terms, one that is proportional to the inverse of the microtubule length (as the longitudinal diffusion coefficient of a filament in Brownian movement is) and another that is independent of the length, and 2) the length-dependent term decreases with increasing kinesin concentration. This latter term almost vanishes within the length range we studied at high kinesin concentrations. From the length-dependence relationship, we evaluated the friction coefficient for sliding microtubules. This value is much larger than the solvent friction and thus consistent with protein friction. The length independence of the motional diffusion coefficient observed at sufficiently high kinesin concentrations indicates the presence of correlation in the sliding movement fluctuation. This places significant constraint on the possible mechanisms of the sliding movement generation by kinesin motors in vitro.

UR - http://www.scopus.com/inward/record.url?scp=0030071058&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030071058&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(96)79631-5

DO - 10.1016/S0006-3495(96)79631-5

M3 - Article

C2 - 8789105

AN - SCOPUS:0030071058

VL - 70

SP - 878

EP - 886

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 2 I

ER -