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BIOENERGETICS AND PHOTOSYNTHESIS

Knock-Out of the Genes Coding for the Rieske Protein and the ATP-Synthase -Subunit of Arabidopsis. Effects on Photosynthesis, Thylakoid Protein Composition, and Nuclear Chloroplast Gene Expression^1,[w]

Abteilung für Pflanzenzüchtung und Ertragsphysiologie, Max-Planck-Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, D-50829 Köln, Germany (D.M., A.D., P.P., F.S., D.L.); Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, D-40225 Düsseldorf, Germany (P.J.); Institut de Biologie Physico-Chimique Service de Photosynthèse/Unité Propre de Recherche-Centre National de la Recherche Scientifique 1261, 13, rue Pierre et Marie Curie, 75005 Paris, France (P.J., A.J.); and Syngenta Biotechnology, Inc., 3054 Cornwallis Road, Research Triangle Park, North Carolina 27709 (J.Z.L.)

In Arabidopsis, the nuclear genes PetC and AtpD code for the Rieske protein of the cytochrome b₆/f (cyt b₆/f) complex and the -subunit of the chloroplast ATP synthase (cpATPase), respectively. Knock-out alleles for each of these loci have been identified. Greenhouse-grown petc-2 and atpd-1 mutants are seedling lethal, whereas heterotrophically propagated plants display a high-chlorophyll (Chl)-fluorescence phenotype, indicating that the products of PetC and AtpD are essential for photosynthesis. Additional effects of the mutations in axenic culture include altered leaf coloration and increased photosensitivity. Lack of the Rieske protein affects the stability of cyt b₆/f and influences the level of other thylakoid proteins, particularly those of photosystem II. In petc-2, linear electron flow is blocked, leading to an altered redox state of both the primary quinone acceptor Q_A in photosystem II and the reaction center Chl P700 in photosystem I. Absence of cpATPase- destabilizes the entire cpATPase complex, whereas residual accumulation of cyt b₆/f and of the photosystems still allows linear electron flow. In atpd-1, the increase in non-photochemical quenching of Chl fluorescence and a higher de-epoxidation state of xanthophyll cycle pigments under low light is compatible with a slower dissipation of the transthylakoid proton gradient. Further and clear differences between the two mutations are evident when mRNA expression profiles of nucleus-encoded chloroplast proteins are considered, suggesting that the physiological states conditioned by the two mutations trigger different modes of plastid signaling and nuclear response.

^[w] The online version of this article contains Web-only data.

^* Corresponding author; e-mail leister{at}mpiz-koeln.mpg.de; fax 49-221-5062-413.

Received March 25, 2003; returned for revision April 24, 2003; accepted June 17, 2003.

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