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Structural studies of kinesin-nucleotide intermediates

S S Rosenfeld1, J J Correia, J Xing

  • 1Department of Neurology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA. s_rosenfeld@email.neuro.uab.edu

The Journal of Biological Chemistry
|November 22, 1996
PubMed
Summary

Kinesin molecular motors undergo structural changes during their ATPase cycle. A flexible internal "hinge" becomes more rigid in strong nucleotide binding states and more flexible in weak binding states.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Kinesin is a crucial molecular motor involved in intracellular transport.
  • Understanding the structural dynamics of kinesin during its ATPase cycle is key to elucidating its mechanism of action.

Purpose of the Study:

  • To investigate the structural alterations in kinesin during its ATPase cycle.
  • To correlate these structural changes with different nucleotide-bound states.

Main Methods:

  • Utilized bacterially expressed human kinesin constructs.
  • Employed sedimentation velocity, sedimentation equilibrium, fluorescence solute quenching, fluorescence anisotropy decay, and limited proteolysis.
  • Analyzed structural changes as a function of nucleotide intermediates in the active site.

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Main Results:

  • Molecular weight and tryptic cleavage patterns remained unaffected by nucleotide intermediates.
  • Significant changes in rotational correlation time of fluorescently labeled kinesin were detected.
  • Identified varying flexibility in an internal kinesin "hinge" depending on the nucleotide binding state.

Conclusions:

  • Kinesin possesses an internal hinge with nucleotide-dependent flexibility.
  • Strong nucleotide binding states exhibit a rigid hinge, while weak binding states show increased flexibility.
  • Suggests a shared mechanism of segmental flexibility in weak binding states between kinesin and myosin.