Chemomechanical coupling of the forward and backward steps of single kinesin molecules

Nat Cell Biol. 2002 Oct;4(10):790-7. doi: 10.1038/ncb857.

Abstract

The molecular motor kinesin travels processively along a microtubule in a stepwise manner. Here we have studied the chemomechanical coupling of the hydrolysis of ATP to the mechanical work of kinesin by analysing the individual stepwise movements according to the directionality of the movements. Kinesin molecules move primarily in the forward direction and only occasionally in the backward direction. The hydrolysis of a single ATP molecule is coupled to either the forward or the backward movement. This bidirectional movement is well described by a model of Brownian motion assuming an asymmetric potential of activation energy. Thus, the stepwise movement along the microtubule is most probably due to Brownian motion that is biased towards the forward direction by chemical energy stored in ATP molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Adenosine Triphosphate / pharmacology
  • Animals
  • Biological Transport / drug effects
  • Biological Transport / physiology*
  • Cattle
  • Dose-Response Relationship, Drug
  • Energy Metabolism / drug effects
  • Energy Metabolism / physiology
  • Eukaryotic Cells / metabolism*
  • Kinesins / drug effects
  • Kinesins / metabolism*
  • Kinetics
  • Microtubules / metabolism*
  • Models, Biological
  • Molecular Motor Proteins / drug effects
  • Molecular Motor Proteins / metabolism*
  • Time Factors

Substances

  • Molecular Motor Proteins
  • Adenosine Triphosphate
  • Kinesins