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J. Biol. Chem., Vol. 278, Issue 26, 23714-23719, June 27, 2003

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Subunit Rotation of Vacuolar-type Proton Pumping ATPase

RELATIVE ROTATION OF THE G AND c SUBUNITS^*,">

Tomoyuki Hirata  , Atsuko Iwamoto-Kihara ¶, Ge-Hong Sun-Wada , Toshihide Okajima , Yoh Wada  and Masamitsu Futai   ||

From the Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Osaka 567-0047, the Nanoscience and Nanotechnology Center, Institute of Scientific and Industrial Research, Osaka University and Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Corporation, Ibaraki, Osaka 567-0047, and ^¶Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan

Vacuolar-type ATPases V₁V₀ (V-ATPases) are found ubiquitously in the endomembrane organelles of eukaryotic cells. In this study, we genetically introduced a His tag and a biotin tag onto the c and G subunits, respectively, of Saccharomyces cerevisiae V-ATPase. Using this engineered enzyme, we observed directly the continuous counter-clockwise rotation of an actin filament attached to the G subunit when the enzyme was immobilized on a glass surface through the c subunit. V-ATPase generated essentially the same torque as the F-ATPase (ATP synthase). The rotation was inhibited by concanamycin and nitrate but not by azide. These results demonstrated that the V- and F-ATPase carry out a common rotational catalysis.

Received for publication, March 18, 2003 , and in revised form, April 1, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^"> The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

^|| To whom correspondence should be addressed. Tel.: 81-6-6879-8480; Fax: 81-6-6875–5724; E-mail: m-futai{at}sanken.osaka-u.ac.jp.

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