Insights into the mechanisms of myosin and kinesin molecular motors from the single-molecule unbinding force measurements

Sergey V. Mikhailenko, Yusuke Oguchi, Shin'ichi Ishiwata

研究成果: Review article査読

7 被引用数 (Scopus)

抄録

In cells, ATP (adenosine triphosphate)-driven motor proteins, both cytoskeletal and nucleic acid-based, operate on their corresponding 'tracks', that is, actin, microtubules or nucleic acids, by converting the chemical energy of ATP hydrolysis into mechanical work. During each mechanochemical cycle, a motor proceeds via several nucleotide states, characterized by different affinities for the 'track' filament and different nucleotide (ATP or ADP) binding kinetics, which is crucial for a motor to efficiently perform its cellular functions. The measurements of the rupture force between the motor and the track by applying external loads to the individual motor-substrate bonds in various nucleotide states have proved to be an important tool to obtain valuable insights into the mechanism of the motors' performance.We review the application of this technique to various linear molecular motors, both processive and nonprocessive, giving special attention to the importance of the experimental geometry.

本文言語English
ページ(範囲)S295-S306
ジャーナルJournal of the Royal Society Interface
7
SUPPL. 3
DOI
出版ステータスPublished - 2010 6 6

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Bioengineering
  • Biomaterials
  • Biochemistry
  • Biomedical Engineering

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