Chemomechanical coupling of the forward and backward steps of single kinesin molecules View Full Text


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Article Info

DATE

2002-09-23

AUTHORS

Masayoshi Nishiyama, Hideo Higuchi, Toshio Yanagida

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. More... »

PAGES

790-797

References to SciGraph publications

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  • 1995-02. Pathway of processive ATP hydrolysis by kinesin in NATURE
  • 2001-06. ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2001-05-24. Switch-based mechanism of kinesin motors in NATURE
  • 1996-04. Direct observation of single kinesin molecules moving along microtubules in NATURE
  • 1995-10. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains in NATURE
  • 1999-01. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres in NATURE
  • 1989-11. Movement of microtubules by single kinesin molecules in NATURE
  • 1993-10. Direct observation of kinesin stepping by optical trapping interferometry in NATURE
  • 1997-07. Coupling of kinesin steps to ATP hydrolysis in NATURE
  • 1990-11. Bead movement by single kinesin molecules studied with optical tweezers in NATURE
  • 2000-09-14. Force production by single kinesin motors in NATURE CELL BIOLOGY
  • 1999-04. The motor protein myosin-I produces its working stroke in two steps in NATURE
  • 1997-07. Kinesin hydrolyses one ATP per 8-nm step in NATURE
  • 1999-12. A structural change in the kinesin motor protein that drives motility in NATURE
  • 1999-07-08. Single kinesin molecules studied with a molecular force clamp in NATURE
  • 1998-01. Structure of the αβ tubulin dimer by electron crystallography in NATURE
  • 1999-08. Myosin-V is a processive actin-based motor in NATURE
  • 2001-03-19. Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules in NATURE CELL BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncb857

    DOI

    http://dx.doi.org/10.1038/ncb857

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038397822

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12360289


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