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Published on April 27, 2007; 10.1104/pp.106.094060

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Received December 3, 2006
Accepted April 17, 2007

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

Robert van Lis *, Guillermo Mendoza-Hernández , Georg Groth , and Ariane Atteia

Institut für Biochemie der Pflanzen, Heinrich Heine Universität Düsseldorf, Universitätsstrasse 1, Düsseldorf D-40225, Germany; Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México D.F., 04510, México; Laboratoire de Physiologie Cellulaire Végétale, CNRS; CEA; INRA; Université Joseph Fourier; 17 rue des Martyrs, F-38054 Grenoble, France

* Corresponding author; email: rvanlis{at}yahoo.fr.

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 {alpha} and {beta} 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 kDa have homologues 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 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 1600 kDa into subcomplexes of 800 kDa and 400 kDa, assigned as the ATP synthase monomer and F1-ATPase, respectively. Whereas no ASA subunits were found in the F1-ATPase, in the monomer all but two were present. ASA6 (12 kDa) and ASA9 (9 kDa), 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.






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