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J. Biol. Chem., Vol. 278, Issue 27, 24255-24258, July 4, 2003

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Rotation of the Proteolipid Ring in the V-ATPase^*

Ken Yokoyama  , Masahiro Nakano ¶, Hiromi Imamura , Masasuke Yoshida  ¶ and Masatada Tamakoshi ||

From the ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), 5800-3 Nagatsuta, Midori-ku, Yokohama 226-0026, Japan, ^¶Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, Japan, and ^||Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Tokyo 192-0392, Japan

V₀V₁-ATPase is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. We demonstrated recently the rotation of the central stalk subunits in V₁, a catalytic sector of V₀V₁-ATPase (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 2312–2315), but the rotation of the proteolipid ring, a predicted counterpart rotor in the membrane V₀ sector, has remained to be proven. V₀V₁-ATPase that retained sensitivity to N',N'-dicyclohexylcarbodiimide was isolated from Thermus thermophilus, immobilized onto a glass surface through the N termini of the A subunits of V₁, and decorated with a bead attached to a proteolipid subunit of V₀. Rotation of beads was observed in the presence of ATP, and direction of rotation was always counterclockwise viewed from the membrane side. The rotation proceeded at 3.0 rev/s in average at 4 mM ATP and was abolished by N',N'-dicyclohexylcarbodiimide treatment. Thus, the rotation of the central stalk in V₁ accompanies rotation of a proteolipid ring of V₀ in the functioning V₀V₁-ATPase.

Received for publication, March 26, 2003 , and in revised form, April 18, 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.

To whom correspondence should be addressed. Fax: 81-45-922-5239; E-mail: kyokoyama-ra{at}res.titech.ac.jp.

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