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Originally published In Press as doi:10.1074/jbc.M101255200 on March 20, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20795-20802, June 8, 2001
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Abnormal Regulation of Photosynthetic Electron Transport in a Chloroplast ycf9 Inactivation Mutant*

Elena Baena-GonzálezDagger , John C. Gray§, Esa TyystjärviDagger , Eva-Mari AroDagger , and Pirkko MäenpääDagger

From the Dagger  Department of Biology, Plant Physiology and Molecular Biology, University of Turku, FIN-20014 Turku, Finland and the § Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA, United Kingdom

The ycf9 (orf62) gene of the plastid genome encodes a 6.6-kDa protein (ORF62) of thylakoid membranes. To elucidate the role of the ORF62 protein, the coding region of the gene was disrupted with an aadA cassette, yielding mutant plants that were nearly (more than 95%) homoplasmic for ycf9 inactivation. The ycf9 mutant had no altered phenotype under standard growth conditions, but its growth rate was severely reduced under suboptimal irradiances. On the other hand, it was less susceptible to photodamage than the wild type. ycf9 inactivation resulted in a clear reduction in protein amounts of CP26, the NAD(P)H dehydrogenase complex, and the plastid terminal oxidase. Furthermore, depletion of ORF62 led to a faster flow of electrons to photosystem I without a change in the maximum electron transfer capacity of photosystem II. Despite the reduction of CP26 in the mutant thylakoids, no differences in PSII oxygen evolution rates were evident even at low light intensities. On the other hand, the ycf9 mutant presented deficiencies in the capacity for PSII-independent electron transport (ferredoxin-dependent cyclic electron transport and NAD(P)H dehydrogenase-mediated plastoquinone reduction). Altogether, it is shown that depletion of ORF62 leads to anomalies in the photosynthetic electron transfer chain and in the regulation of electron partitioning among the different routes of electron transport.


* This work was supported by grants from the Academy of Finland (to E.-M. A.), the Emil Aaltonen foundation (to E. B.-G.), The Royal Society, London, UK, and Robinson College, Cambridge, UK (to P. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Plant Physiology and Molecular Biology, Dept. of Biology, University of Turku, FIN-20014 Turku, Finland. Tel.: 358-2-333-5931; Fax: 358-2-333-5549; E-mail: evaaro@utu.fi.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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