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Biophys. J. BioFAST: First Published December 30, 2004. doi:10.1529/biophysj.104.054668
© 2004 by the Biophysical Society.

A more recent version of this article appeared on March 1, 2005.
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Naoyoshi Sakaki
Rieko Shimo-Kon
Kengo Adachi
Hiroyasu Itoh
Shou Furuike
Eiro Muneyuki
Masasuke Yoshida
Kazuhiko Kinosita, Jr.
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PROTEINS

One Rotary Mechanism for F1-ATPase over ATP Concentrations from Millimolar down to Nanomolar

Naoyoshi Sakaki 1, Rieko Shimo-Kon 2, Kengo Adachi 2, Hiroyasu Itoh 3, Shou Furuike 2, Eiro Muneyuki 4, Masasuke Yoshida 4 and Kazuhiko Kinosita, Jr. 5*

1 Graduate University of Advanced Studies
2 Okazaki Institite for Integrative Bioscience
3 Hamamatsu Photonics KK.
4 Tokyo Institute of Technology
5 National Institutes of Natural Sciences

* To whom correspondence should be addressed. E-mail: kazuhiko{at}ims.ac.jp.

Submitted on October 28, 2004
Revised on November 30, 2004
Accepted on 16 December 2004


  Abstract
F1-ATPase is a rotary molecular motor in which the central {gamma} subunit rotates inside a cylinder made of {alpha}3{beta}3 subunits. The rotation is driven by ATP hydrolysis in three catalytic sites on the {beta} subunits. How many of the three catalytic sites are filled with a nucleotide during the course of rotation is an important yet unsettled question. Here we inquire whether F1 rotates at extremely low ATP concentrations where the site occupancy is expected to be low. We observed under an optical microscope rotation of individual F1 molecules that carried a bead duplex on the {gamma} subunit. Time-averaged rotation rate was proportional to the ATP concentration down to 200 pM, giving an apparent rate constant for ATP binding of 2x107 M-1s-1. A similar rate constant characterized bulk ATP hydrolysis in solution, which obeyed a simple Michaelis-Menten scheme between 6 mM and 60 nM ATP. F1 produced the same torque of ~40 pN·nm at 2 mM, 60 nM, and 2 nM ATP. These results point to one rotary mechanism governing the entire range of nanomolar to millimolar ATP, although a switchover between two mechanisms cannot be dismissed. Below 1 nM ATP, we observed less regular rotations, indicative of the appearance of another reaction scheme.

Key Words: Chemo-mechanical energy conversion, Molecular motor, Optical microscopy, Single-molecule imaging, Torque




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Copyright © 2004 by the Biophysical Society.