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J Biol Chem, Vol. 274, Issue 36, 25281-25284, September 3, 1999

The Proteolipid of the A₁A₀ ATP Synthase from Methanococcus jannaschii Has Six Predicted Transmembrane Helices but Only Two Proton-translocating Carboxyl Groups

Claudia Ruppert, Holger Kavermann, Sönke Wimmers, Roland Schmid^§, Joseph Kellermann^¶, Friedrich Lottspeich^¶, Harald Huber, Karl O. Stetter, and Volker Müller

From the  Lehrstuhl für Mikrobiologie der Ludwig-Maximilians-Universität München, Maria-Ward-Strasse 1a, 80638 München, Germany, ^§ FB5, AG Mikrobiologie, Universität Osnabrück, Barbarastrasse 11, 49069 Osnabrück, Germany, ^¶ Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Am Klopferspitz 18a, 82152 Martinsried, Germany, and  Lehrstuhl für Mikrobiologie, Universitätsstrasse 31, Universität Regensburg, 93053 Regensburg, Germany

The proteolipid, a hydrophobic ATPase subunit essential for ion translocation, was purified from membranes of Methanococcus jannaschii by chloroform/methanol extraction and gel chromatography and was studied using molecular and biochemical techniques. Its apparent molecular mass as determined in SDS-polyacrylamide gel electrophoresis varied considerably with the conditions applied. The N-terminal sequence analysis made it possible to define the open reading frame and revealed that the gene is a triplication of the gene present in bacteria. In some of the proteolipids, the N-terminal methionine is excised. Consequently, two forms with molecular masses of 21,316 and 21,183 Da were determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The molecular and biochemical data gave clear evidence that the mature proteolipid from M. jannaschii is a triplication of the 8-kDa proteolipid present in bacterial F₁F₀ ATPases and most archaeal A₁A₀ ATPases. Moreover, the triplicated form lacks a proton-translocating carboxyl group in the first of three pairs of transmembrane helices. This finding puts in question the current view of the evolution of H⁺ ATPases and has important mechanistic consequences for the structure and function of H⁺ ATPases in general.

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