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Volume 271, Number 31, Issue of August 2, 1996 pp. 18843-18852
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Subunit Structure and Organization of the Genes of the A₁A₀ ATPase from the Archaeon Methanosarcina mazei Gö1

(Received for publication, November 28, 1995, and in revised form, May 7, 1996)

From the Institut für Mikrobiologie der Georg-August-Universität, Grisebachstraße 8, D-37077 Göttingen, Germany

The proton-translocating A₁A₀ ATP synthase/hydrolase of Methanosarcina mazei Gö1 was purified and shown to consist of six subunits of molecular masses of 65, 49, 40, 36, 25, and 7 kDa. Electron microscopy revealed that this enzyme is organized in two domains, the hydrophilic A₁ and the hydrophobic A₀ domain, which are connected by a stalk. Genes coding for seven hydrophilic subunits were cloned and sequenced. From these data it is evident that the 65-, 49-, 40- and 25-kDa subunits are encoded by ahaA, ahaB, ahaC, and ahaD, respectively; they are part of the A₁ domain or the stalk. In addition there are three more genes, ahaE, ahaF, and ahaG, encoding hydrophilic subunits, which were apparently lost during the purification of the protein. The A₀ domain consists of at least the 7-kDa proteolipid and the 36-kDa subunit for which the genes have not yet been found. In summary, it is proposed that the A₁A₀ ATPase of Methanosarcina mazei Gö1 contains at least nine subunits, of which seven are located in A₁ and/or the stalk and two in A₀.

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