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Related Experiment Videos

A mechanistic model for Ncd directionality.

K A Foster1, A T Mackey, S P Gilbert

  • 1Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.

The Journal of Biological Chemistry
|March 30, 2001
PubMed
Summary

Ncd motor proteins move along microtubules towards their minus-ends. This study reveals asymmetric motor domains and a two-ATP mechanism for directional movement, crucial for cellular transport.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Ncd (Ncd) is a dimeric kinesin motor protein responsible for minus-end directed microtubule transport.
  • Understanding the ATPase mechanism and cooperative interactions of Ncd motor domains is crucial for elucidating its function in cellular processes.

Purpose of the Study:

  • To investigate the cooperative interactions between the motor domains of the dimeric Ncd (MC1) protein.
  • To elucidate the ATPase mechanism underlying Ncd's minus-end directed movement along microtubules.

Main Methods:

  • Pre-steady-state kinetic experiments were utilized to analyze the ATPase activity and motor domain interactions.
  • Kinetic analysis focused on ADP release rates and the influence of microtubule binding.

Main Results:

  • Dimeric Ncd exhibits non-equivalent active sites, with differing affinities for ADP in solution.
  • Microtubule binding induces differential ADP release: 18 s(-1) from the first head and 1.4 s(-1) from the second.
  • Two ATP molecules are required per step for force generation and minus-end directed movement.

Conclusions:

  • The motor domain with lower ADP affinity likely binds microtubules first, establishing directional bias.
  • ATP binding and hydrolysis at one head are essential for the second head's microtubule interaction and force generation.
  • Ncd functions as a non-processive dimeric motor requiring two ATP molecules for directional transport.

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