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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
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Force production of human cytoplasmic dynein is limited by its processivity

Sibylle Brenner1, Florian Berger2, Lu Rao1

  • 1Department of Anatomy and Structural Biology and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA.

Science Advances
|April 15, 2020
PubMed

Insights

Human cytoplasmic dynein, a motor protein, has limited force generation due to low processivity. Researchers determined its true stall force is ~2 pN using optical tweezers, providing a new model for motor protein analysis.

Area of Science:

  • Molecular biology
  • Biophysics
  • Cellular mechanics

Background:

  • Cytoplasmic dynein is a crucial motor protein.
  • It moves towards the minus end of microtubules.
  • Its force generation is limited by low processivity.

Purpose of the Study:

  • To determine the true maximal force (stall force) of human dynein.
  • To understand how low processivity affects dynein's force generation.
  • To develop a theoretical model for weakly processive molecular motors.

Main Methods:

  • Utilized optical tweezers to measure dynein's force.
  • Employed high trap stiffness to analyze motor behavior.
  • Derived an analytical equation to model motor force generation.

Main Results:

  • Human dynein's stall force was determined to be approximately 2 pN.
  • Low processivity limits dynein's force generation due to premature microtubule dissociation.
  • A hyperbolic force-stiffness curve was observed, plateauing at the stall force.

Conclusions:

  • The study clarifies the stall force and processivity of human dynein.
  • A new theoretical paradigm for analyzing weakly processive molecular motors was established.
  • The findings offer insights into the mechanics of molecular motor force generation.

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