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A Unified Walking Model for Dimeric Motor Proteins.
Sasaki, Kazuo; Kaya, Motoshi; Higuchi, Hideo.
Afiliação
  • Sasaki K; Department of Applied Physics, Graduate School of Engineering, Tohoku University, Sendai, Japan. Electronic address: sasaki@camp.apph.tohoku.ac.jp.
  • Kaya M; Department of Physics, University of Tokyo, Hongo Bunkyo-ku, Tokyo, Japan.
  • Higuchi H; Department of Physics, University of Tokyo, Hongo Bunkyo-ku, Tokyo, Japan; Universal Biology Institute, Graduate School of Science, University of Tokyo, Hongo Bunkyo-ku, Tokyo, Japan. Electronic address: higuchi@phys.s.u-tokyo.ac.jp.
Biophys J ; 115(10): 1981-1992, 2018 11 20.
Article em En | MEDLINE | ID: mdl-30396511
ABSTRACT
Dimeric motor proteins, kinesin-1, cytoplasmic dynein-1, and myosin-V, move stepwise along microtubules and actin filaments with a regular step size. The motors take backward as well as forward steps. The step ratio r and dwell time τ, which are the ratio of the number of backward steps to the number of forward steps and the time between consecutive steps, respectively, were observed to change with the load. To understand the movement of motor proteins, we constructed a unified and simple mathematical model to explain the load dependencies of r and of τ measured for the above three types of motors quantitatively. Our model consists of three states, and the forward and backward steps are represented by the cycles of transitions visiting different pairs of states among the three, implying that a backward step is not the reversal of a forward step. Each of r and τ is given by a simple expression containing two exponential functions. The experimental data for r and τ for dynein available in the literature are not sufficient for a quantitative analysis, which is in contrast to those for kinesin and myosin-V. We reanalyze the data to obtain r and τ of native dynein to make up the insufficient data to fit them to the model. Our model successfully describes the behavior of r and τ for all of the motors in a wide range of loads from large assisting loads to superstall loads.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Modelos Moleculares / Cinesinas / Fenômenos Mecânicos / Multimerização Proteica Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Modelos Moleculares / Cinesinas / Fenômenos Mecânicos / Multimerização Proteica Idioma: En Ano de publicação: 2018 Tipo de documento: Article