Knock-out of the genes coding for the Rieske protein and the ATP-synthase delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein composition, and nuclear chloroplast gene expression

• Published in: Plant physiology (Bethesda) Vol. 133; no. 1; pp. 191 - 202
• Main Authors: Maiwald, D, Dietzmann, A, Jahns, P, Pesaresi, P, Joliot, P, Joliot, A, Levin, J.Z, Salamini, F, Leister, D
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Biologists 01-09-2003; American Society of Plant Physiologists
• Subjects: adenosinetriphosphatase; alleles; Arabidopsis; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; AtpD gene; Bioenergetics and Photosynthesis; Biological and medical sciences; cell nucleus; Chlorophyll - metabolism; chloroplast ATP synthase; Chloroplast Proton-Translocating ATPases - genetics; Chloroplast Proton-Translocating ATPases - metabolism; Chloroplasts; cytochrome b; Cytochrome b6f Complex - genetics; Cytochrome b6f Complex - metabolism; cytochrome f; Cytochromes; electron transfer; Electron Transport - genetics; Electron Transport - physiology; Electron Transport Complex III - genetics; Electron Transport Complex III - metabolism; Fundamental and applied biological sciences. Psychology; gene expression; Gene Expression Profiling; Genes; Genetic mutation; Iron-Sulfur Proteins - genetics; Iron-Sulfur Proteins - metabolism; knockout mutants; Luminous intensity; messenger RNA; Metabolism; molecular sequence data; Mutation; nucleotide sequences; Oxidation-Reduction; PetC gene; Photons; Photosynthesis; Photosynthesis - genetics; Photosynthesis - physiology; Photosynthesis, respiration. Anabolism, catabolism; Photosynthetic Reaction Center Complex Proteins - genetics; Photosynthetic Reaction Center Complex Proteins - metabolism; photosystem I; photosystem II; Phylogeny; Pigments, Biological - metabolism; Plant Leaves - genetics; Plant Leaves - metabolism; Plant physiology and development; plant pigments; plant proteins; Plants; protein composition; protein synthesis; Protons; rieske protein; RNA, Chloroplast - genetics; RNA, Chloroplast - metabolism; RNA, Messenger - genetics; RNA, Messenger - metabolism; Signal Transduction - genetics; Signal Transduction - physiology; Thylakoids; Thylakoids - metabolism; transport proteins; Redox state; Enzyme; Arabidopsis; Adenosinetriphosphatase; Electron transfer; Subunit; Photosynthetic system; Arabidopsis thaliana; Cruciferae; Dicotyledones; Angiospermae; Hydrolases; Spermatophyta; Chemical composition; Mutation; Photosynthesis; Chloroplast; Proton transport
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.103.024190

In Arabidopsis, the nuclear genes PetC and AtpD code for the Rieske protein of the cytochrome b6/f (cyt b6/f) complex and the δ-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 QA in photosystem II and the reaction center Chl P700 in photosystem I. Absence of cpATPase-δ 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.