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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

New Insights into the Unique Structure of the F₀F₁-ATP Synthase from the Chlamydomonad Algae Polytomella sp. and Chlamydomonas reinhardtii¹

Institut für Biochemie der Pflanzen, Heinrich Heine Universität Düsseldorf, Duesseldorf D–40225, Germany (R.v.L., G.G.); Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico (G.M-H.); and Laboratoire de Physiologie Cellulaire Végétale, Centre National de la Recherche Scientifique, Commissariat à l'Energie Atomique, Institut National de la Recherche Agronomique, Université Joseph Fourier, F–38054 Grenoble, France (A.A.)

In this study, we investigate the structure of the mitochondrial F₀F₁-ATP synthase of the colorless alga Polytomella sp. with respect to the enzyme of its green close relative Chlamydomonas reinhardtii. It is demonstrated that several unique features of the ATP synthase in C. reinhardtii are also present in Polytomella sp. The - and -subunits of the ATP synthase from both algae are highly unusual in that they exhibit extensions at their N- and C-terminal ends, respectively. Several subunits of the Polytomella ATP synthase in the range of 9 to 66 kD have homologs in the green alga but do not have known equivalents as yet in mitochondrial ATP synthases of mammals, plants, or fungi. The largest of these so-called ASA (ATP Synthase-Associated) subunits, ASA1, is shown to be an extrinsic protein. Short heat treatment of isolated Polytomella mitochondria unexpectedly dissociated the otherwise highly stable ATP synthase dimer of 1,600 kD into subcomplexes of 800 and 400 kD, assigned as the ATP synthase monomer and F₁-ATPase, respectively. Whereas no ASA subunits were found in the F₁-ATPase, all but two were present in the monomer. ASA6 (12 kD) and ASA9 (9 kD), predicted to be membrane bound, were not detected in the monomer and are thus proposed to be involved in the formation or stabilization of the enzyme. A hypothetical configuration of the Chlamydomonad dimeric ATP synthase portraying its unique features is provided to spur further research on this topic.

² Present address: Laboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, CNRS, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Robert van Lis (rvanlis{at}yahoo.fr).

www.plantphysiol.org/cgi/doi/10.1104/pp.106.094060

^* Corresponding author; e-mail rvanlis{at}yahoo.fr; fax 33–4–9116–4578.

Received December 3, 2006; accepted April 17, 2007; published April 20, 2007.