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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
Abnormal Regulation of Photosynthetic Electron Transport in a
Chloroplast ycf9 Inactivation Mutant*
Elena
Baena-González ,
John C.
Gray§,
Esa
Tyystjärvi ,
Eva-Mari
Aro ¶, and
Pirkko
Mäenpää
From the 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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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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