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Plant Physiol, October 2000, Vol. 124, pp. 823-832
Antisense Suppression of 2-Cysteine Peroxiredoxin in Arabidopsis
Specifically Enhances the Activities and Expression of Enzymes
Associated with Ascorbate Metabolism But Not Glutathione
Metabolism1
Margarete
Baier,2*
Graham
Noctor,
Christine H.
Foyer, and
Karl-Josef
Dietz
Stoffwechselphysiologie und Biochemie der Pflanzen,
Universität Bielefeld, Universitätsstra e 25, 33615 Bielefeld, Germany (M.B., K.-J.D.); and Biochemistry and Physiology
Department, IACR Rothamsted, Harpenden, Hertfordshire AL5 2JQ, United
Kingdom (G.N., C.H.F.)
The aim of this study was to characterize the effect of decreased
2-cysteine peroxiredoxin (2-CP) on the leaf anti-oxidative system in
Arabidopsis. At three stages of leaf development, two lines of
transgenic Arabidopsis mutants with decreased contents of chloroplast
2-CP were compared with wild type and a control line transformed with
an empty vector. Glutathione contents and redox state were similar in
all plants, and no changes in transcript levels for enzymes involved in
glutathione metabolism were observed. Transcript levels for
chloroplastic glutathione peroxidase were much lower than those for
2-CP, and both cytosolic and chloroplastic glutathione peroxidase were
not increased in the mutants. In contrast, the foliar ascorbate pool
was more oxidized in the mutants, although the difference decreased
with plant age. The activities of thylakoid and stromal ascorbate
peroxidase and particularly monodehydroascorbate reductase were
increased as were transcripts for these enzymes. No change in
dehydroascorbate reductase activity was observed, and effects on
transcript abundance for glutathione reductase, catalase, and
superoxide dismutase were slight or absent. The results demonstrate
that 2-CP forms an integral part of the anti-oxidant network of
chloroplasts and is functionally interconnected with other defense
systems. Suppression of 2-CP leads to increased expression of other
anti-oxidative genes possibly mediated by increased oxidation state of
the leaf ascorbate pool.
1
This work was supported by a European Molecular
Biology Organization fellowship that allowed a short term stay at IACR
Rothamsted (to M.B.), by the Universität Bielefeld (grant nos.
FIF OZ 20944.20 and FIF OZ 20920), and by the Deutsche
Forschungsgemeinschaft (grant no. Di 346/6).
2
Present address: Department of Molecular Genetics, John
Innes Centre, Norwich, Norfolk NR4 7UH, UK.
*
Corresponding author; e-mail margarete.baier{at}biologie.uni-bielefeld.de; fax 49-521-106-6039.
© 2000 American Society of Plant Physiologists
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