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Intersubunit coordination in a homomeric ring ATPase.

Jeffrey R Moffitt¹, Yann R Chemla, K Aathavan

¹Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, California 94720, USA.

|January 9, 2009

Summary

This summary is machine-generated.

Researchers directly observed the DNA packaging motor of bacteriophage phi29, a ring ATPase. They discovered it packages DNA in coordinated 2.5 base pair steps, totaling 10 base pairs per cycle, revealing a novel coordination mechanism.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Homomeric ring ATPases are crucial molecular motors involved in diverse cellular processes.
Understanding their mechanisms, particularly intersubunit coordination and step size, is key to elucidating their functions.

Purpose of the Study:

To directly observe and quantify the intersubunit coordination and step size of the bacteriophage phi29 DNA packaging motor.
To investigate the mechanism of DNA translocation at a single-molecule level.

Main Methods:

Utilized high-resolution optical tweezers to apply force and measure the precise movements of the phi29 motor.
Performed statistical analysis of dwell times and applied high force to resolve individual steps.

Main Results:

Observed DNA packaging in discrete increments of 10 base pairs (bp).
Revealed that each 10-bp increment is composed of four coordinated 2.5-bp steps.
Demonstrated that multiple ATP molecules bind and hydrolyze during each packaging dwell.

Conclusions:

The phi29 motor exhibits a highly coordinated hydrolysis cycle among its subunits, a novel mechanism for ring ATPases.
The non-integer step size necessitates the development of new models for motor-DNA interactions.