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Protective Function of Chloroplast 2-Cysteine Peroxiredoxin in Photosynthesis. Evidence from Transgenic Arabidopsis1

Margarete Baier and Karl-Josef Dietz*

Stoffwechselphysiologie und Biochemie der Pflanzen, Universität Bielefeld, Universitätsstrasse 25, 33615 Bielefeld, Germany

2-Cysteine peroxiredoxins (2-CPs) constitute a ubiquitous group of peroxidases that reduce cell-toxic alkyl hydroperoxides to their corresponding alcohols. Recently, we cloned 2-CP cDNAs from plants and characterized them as chloroplast proteins. To elucidate the physiological function of the 2-CP in plant metabolism, we generated antisense mutants in Arabidopsis. In the mutant lines a 2-CP deficiency developed during early leaf and plant development and eventually the protein accumulated to wild-type levels. In young mutants with reduced amounts of 2-CP, photosynthesis was impaired and the levels of D1 protein, the light-harvesting protein complex associated with photosystem II, chloroplast ATP synthase, and ribulose-1,5-bisphosphate carboxylase/oxygenase were decreased. Photoinhibition was particularly pronounced after the application of the protein synthesis inhibitor, lincomycin. We concluded that the photosynthetic machinery needs high levels of 2-CP during leaf development to protect it from oxidative damage and that the damage is reduced by the accumulation of 2-CP protein, by the de novo synthesis and replacement of damaged proteins, and by the induction of other antioxidant defenses in 2-CP mutants.

1   This work was supported by the Deutsche Forschungsgemeinschaft (grant no. Di 346/6L).
*   Corresponding author; e-mail karl-josef.dietz{at}biologie.uni-bielefeld.de; fax 49-0-521-106-6039.

Plant Physiol. (1999) 119: 1407-1414
Copyright Clearance Center:   0032-0889/99/119//08
© 1999 American Society of Plant Physiologists




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