Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast

Muthuramalingam M, Seidel T, Laxa M, de Miranda SMN, Gaertner F, Stroeher E, Kandlbinder A, Dietz K-J (2009)
MOLECULAR PLANT 2(6): 1273-1288.

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Abstract
In plants, the highly abundant 2-cysteine peroxiredoxin (2-CysPrx) is associated with the chloroplast and involved in protecting photosynthesis. This work addresses the multiple 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 isomerase Cyclophilin 20-3 (Cyp20-3) and other components of the photosynthetic apparatus. Co-expression in protoplasts and quantification of fluorescence resonance energy transfer (FRET) efficiency in vivo confirmed 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 complexes that could enable FRET. Likewise, changes in FRET of fluorescently labeled 2-CysPrx in vitro and in vivo proved redox dependent dynamics 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 treatment. This activity was partly inhibited by Cyp20-3. As a new interaction partner of decameric 2-CysPrx, photosystem II could be identified after chloroplast fractionation and in pull-down assays after reconstitution. In summary, the data indicate a dynamic function of plant 2-CysPrx as redox sensor, chaperone, and regulator in the chloroplast with diverse functions beyond its role as thiol peroxidase.
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Muthuramalingam M, Seidel T, Laxa M, et al. Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT. 2009;2(6):1273-1288.
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S. M. N., Gaertner, F., Stroeher, E., Kandlbinder, A., et al. (2009). Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT, 2(6), 1273-1288.
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S. M. N., Gaertner, F., Stroeher, E., Kandlbinder, A., and Dietz, K. - J. (2009). Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT 2, 1273-1288.
Muthuramalingam, M., et al., 2009. Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT, 2(6), p 1273-1288.
M. Muthuramalingam, et al., “Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast”, MOLECULAR PLANT, vol. 2, 2009, pp. 1273-1288.
Muthuramalingam, M., Seidel, T., Laxa, M., de Miranda, S.M.N., Gaertner, F., Stroeher, E., Kandlbinder, A., Dietz, K.-J.: Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast. MOLECULAR PLANT. 2, 1273-1288 (2009).
Muthuramalingam, Meenakumari, Seidel, Thorsten, Laxa, Miriam, de Miranda, Susana M. Nunes, Gaertner, Florian, Stroeher, Elke, Kandlbinder, Andrea, and Dietz, Karl-Josef. “Multiple Redox and Non-Redox Interactions Define 2-Cys Peroxiredoxin as a Regulatory Hub in the Chloroplast”. MOLECULAR PLANT 2.6 (2009): 1273-1288.
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