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Single kinesin molecules studied with a molecular force clamp.

K Visscher¹, M J Schnitzer, S M Block

¹Department of Molecular Biology, Princeton Materials Institute, Princeton University, New Jersey 08544, USA.

|July 17, 1999

Summary

Kinesin motor proteins use ATP to move along microtubules. New research reveals that kinesin

Area of Science:

Molecular motor protein function
Mechanochemistry of kinesin motors
Cellular transport mechanisms

Background:

Kinesin is an ATP-driven motor protein that moves along microtubules in 8 nm steps.
The precise coupling mechanism between ATP hydrolysis and mechanical movement in kinesin is not fully understood.
Understanding this process is crucial for comprehending intracellular transport.

Purpose of the Study:

To investigate the mechanochemical details of kinesin motor protein function.
To elucidate how chemical energy from ATP is converted into mechanical work.
To analyze kinesin's response to varying ATP concentrations and external loads.

Main Methods:

Development of a novel force clamp instrument using a feedback-driven optical trap.

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Measurement of single kinesin motor motion under controlled, constant loads.

Analysis of kinesin's mechanochemical behavior across different ATP concentrations and forces.

Main Results:

Kinesin stepping is tightly coupled to ATP hydrolysis (one hydrolysis per 8 nm step) across a broad force range.
The kinesin stall force is dependent on ATP concentration.
Increased mechanical loads reduce maximum velocity and increase the Michaelis-Menten constant, indicating load-dependent transitions in the kinesin cycle.

Conclusions:

The kinesin motor cycle involves at least one load-dependent transition affecting ATP binding and hydrolysis commitment.
Another load-dependent rate likely influences the overall turnover number.
These findings necessitate a revised understanding of kinesin motor mechanics and function.