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m.ltiple Redox and Non-Redox Interactions define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast

m.lecular Plant 2009年第6期2卷 1273-1288页

作者： meenakumari muthuramalingam thorsten seidel miriam laxa susana m. nunes de miranda florian gartner elke stroher andrea kandlbinder karl-josef dietz Biochem.stry and Physiology of Plants W5-134 Bielefeld University 33501 Bielefeld Germany

In plants, the highly abundant 2-cysteine peroxiredoxin （2-CysPrx） is associated with the chloroplast and involved in protecting photosynthesis. This work addresses the m.ltiple interactions of the 2-CysPrx in the chloroplast, which depend on its redox state. Transcript co-regulation analysis showed a strong linkage to the peptidyl-prolyl-cis/trans isom.rase Cyclophilin 20-3 （Cyp20-3） and other com.onents of the photosynthetic apparatus. Co-expression in protoplasts and quantification of fluorescence resonance energy transfer （FRET） efficiency in vivo confirm.d protein interactions of 2-CysPrx with Cyp20-3 as well as NADPH-dependent thioredoxin reductase C （NTRC）, while thioredoxin x （Trx-x） did not form.com.lexes that could enable FRET. Likewise, changes in FRET of fluorescently labeled 2-CysPrx in vitro and in vivo proved redox dependent dynam.cs of 2-CysPrx. Addition of Cyp20-3 to an in vitro peroxidase assay with 2-CysPrx had no significant effect on peroxide reduction. Also, in the presence of NTRC, addition of Cyp20-3 did not further enhance peroxide reduction. In addition, 2-CysPrx functioned as chaperone and inhibited aggregation of citrate synthase during heat treatm.nt. This activity was partly inhibited by Cyp20-3. As a new interaction partner of decam.ric 2-CysPrx, photosystem.Ⅱ could be identified after chloroplast fractionation and in pull-down assays after reconstitution. In sum.ary, the data indicate a dynam.c function of plant 2-CysPrx as redox sensor, chaperone, and regulator in the chloroplast with diverse functions beyond its role as thiol peroxidase.

关键词： Oxidative and photo-oxidative stress photosynthesis chloroplast biology Arabidopsis cyclophilin peroxiredoxin thioredoxin.

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