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J. Biol. Chem., Vol. 279, Issue 32, 33409-33412, August 6, 2004

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ATP Synthase that Lacks F₀a-Subunit

ISOLATION, PROPERTIES, AND INDICATION OF F₀b₂-SUBUNITS AS AN ANCHOR RAIL OF A ROTATING c-RING^*

Sakurako Ono, Nobuhito Sone, Masasuke Yoshida¶, and Toshiharu Suzuki

From the Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan and ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation, Nagatsuta 5800-3, Yokohama 226-0026, Japan

In a rotary motor F₁F₀-ATP synthase, F₀ works as a proton motor; the oligomer ring of F₀c-subunits (c-ring) rotates relative to the F₀ab₂ domain as protons pass through F₀ down the gradient. F₀ab₂ must exert dual functions during rotation, that is, sliding the c-ring (motor drive) while keeping the association with the c-ring (anchor rail). Here we have isolated thermophilic F₁F₀(-a) which lacks F₀a. F₁F₀(-a) has no proton transport activity, and F₀(-a) does not work as a proton channel. Interestingly, ATPase activity of F₁F₀(-a) is greatly suppressed, even though its F₁ sector is intact. Most likely, F₀b₂ associates with the c-ring as an anchor rail in the intact F₁F₀; without F₀a, this association prevents rotation of the c-ring (and hence the -subunit), which disables ATP hydrolysis at F₁. Functional F₁F₀ is easily reconstituted from purified F₀a and F₁F₀(-a), and thus F₀a can bind to its proper location on F₁F₀(-a) without a large rearrangement of other-subunits.

Received for publication, May 5, 2004 , and in revised form, June 2, 2004.

^* 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. Tel.: 81-45-924-5233; Fax: 81-45-924-5277; E-mail: myoshida{at}res.titech.ac.jp.

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