The function of peroxiredoxins in plant organelle redox metabolism

Dietz K-J, Jacob S, Oelze M-L, Laxa M, Tognetti V, de Miranda SMN, Baier M, Finkemeier I (2006)
Journal of Experimental Botany 57(8): 1697-1709.

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Abstract / Bemerkung
In 1996, cDNA sequences referred to as plant peroxiredoxins (Prx), i.e. a 1-Cys Prx and a 2-Cys Prx, were reported from barley. Ten years of research have advanced our understanding of plant Prx as thiol-based peroxide reductases with a broad substrate specificity, ranging from hydrogen peroxide to alkyl hydroperoxides and peroxinitrite. Prx have several features in common. (i) They are abundant proteins that are routinely detected in proteomics approaches. (ii) They interact with proteins such as glutaredoxins, thioredoxins, and cyclophilins as reductants, but also non-dithioldisulphide exchange proteins. By work with transgenic plants, their activity was shown to (iii) affect metabolic integrity, (iv) protect DNA from damage in vitro and as shown here in vivo, and (v) modulate intracellular signalling related to reactive oxygen species and reactive nitrogen species. (vi) In all organisms Prx are encoded by small gene families that are of particular complexity in higher plants. A comparison of the Prx gene families in rice and Arabidopsis thaliana supports previous suggestions on Prx function in specific subcellular and metabolic context. (vii) Prx gene expression and activity are subjected to complex regulation realized by an integration of various signalling pathways. 2-Cys Prx expression depends on redox signals, abscisic acid, and protein kinase cascades. Besides these general properties, the chloroplast Prx have acquired specific roles in the context of photosynthesis. The thioredoxin-dependent peroxidase activity can be measured in crude plant extracts and contributes significantly to the overall H2O2 detoxification capacity. Thus organellar Prx proteins enable an alternative water-water cycle for detoxification of photochemically produced H2O2, which acts independently from the ascorbate-dependent Asada-Halliwell-Foyer cycle. 2-Cys Prx and Prx Q associate with thylakoid membrane components. The mitochondrial PrAII F is essential for root growth under stress. Following a more general introduction, the paper summarizes present knowledge on plant organellar Prx, addressing Prx in signalling, and also suggests some lines for future research.
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57
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8
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1697-1709
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Dietz K-J, Jacob S, Oelze M-L, et al. The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany. 2006;57(8):1697-1709.
Dietz, K. - J., Jacob, S., Oelze, M. - L., Laxa, M., Tognetti, V., de Miranda, S. M. N., Baier, M., et al. (2006). The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany, 57(8), 1697-1709. doi:10.1093/jxb/erj160
Dietz, K. - J., Jacob, S., Oelze, M. - L., Laxa, M., Tognetti, V., de Miranda, S. M. N., Baier, M., and Finkemeier, I. (2006). The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany 57, 1697-1709.
Dietz, K.-J., et al., 2006. The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany, 57(8), p 1697-1709.
K.-J. Dietz, et al., “The function of peroxiredoxins in plant organelle redox metabolism”, Journal of Experimental Botany, vol. 57, 2006, pp. 1697-1709.
Dietz, K.-J., Jacob, S., Oelze, M.-L., Laxa, M., Tognetti, V., de Miranda, S.M.N., Baier, M., Finkemeier, I.: The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany. 57, 1697-1709 (2006).
Dietz, Karl-Josef, Jacob, S, Oelze, Marie-Luise, Laxa, M, Tognetti, V, de Miranda, SMN, Baier, M, and Finkemeier, I. “The function of peroxiredoxins in plant organelle redox metabolism”. Journal of Experimental Botany 57.8 (2006): 1697-1709.

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Mane ShrinivasraoP, Robinet CeciliaVasquez, Ulanov Alexander, Schafleitner Roland, Tincopa Luz, Gaudin Amelie, Nomberto Giannina, Alvarado Carlos, Solis Christian, Bolivar LuisAvila, Blas Raul, Ortega Oscar, Solis Julio, Panta Ana, Rivera Cristina, Samolski Ilanit, Carbajulca DorisH, Bonierbale Meredith, Pati Amrita, Heath LenwoodS, Bohnert HansJ, Grene Ruth., Funct Plant Biol 35(8), 2008
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Ozone risk assessment for plants: central role of metabolism-dependent changes in reducing power.
Dizengremel P, Le Thiec D, Bagard M, Jolivet Y., Environ Pollut 156(1), 2008
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The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii.
Dayer R, Fischer BB, Eggen RI, Lemaire SD., Genetics 179(1), 2008
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Consequences of C4 differentiation for chloroplast membrane proteomes in maize mesophyll and bundle sheath cells.
Majeran W, Zybailov B, Ytterberg AJ, Dunsmore J, Sun Q, van Wijk KJ., Mol Cell Proteomics 7(9), 2008
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The ferredoxin/thioredoxin system of oxygenic photosynthesis.
Schürmann P, Buchanan BB., Antioxid Redox Signal 10(7), 2008
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Functional analysis and expression characteristics of chloroplastic Prx IIE.
Gama F, Bréhélin C, Gelhaye E, Meyer Y, Jacquot JP, Rey P, Rouhier N., Physiol Plant 133(3), 2008
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Redox signal integration: from stimulus to networks and genes.
Dietz KJ., Physiol Plant 133(3), 2008
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Knockout of major leaf ferredoxin reveals new redox-regulatory adaptations in Arabidopsis thaliana.
Voss I, Koelmann M, Wojtera J, Holtgrefe S, Kitzmann C, Backhausen JE, Scheibe R., Physiol Plant 133(3), 2008
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Knockout of major leaf ferredoxin reveals new redox-regulatory adaptations in Arabidopsis thaliana
Voss I, Koelmann M, Wojtera J, Holtgrefe S, Kitzmann C, Backhausen JE, Scheibe R., Physiol Plant 133(3), 2008
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Functional analysis and expression characteristics of chloroplastic Prx IIE
Gama F, Bréhélin C, Gelhaye E, Meyer Y, Jacquot JP, Rey P, Rouhier N., Physiol Plant 133(3), 2008
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NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg-protoporphyrin monomethyl ester cyclase.
Stenbaek A, Hansson A, Wulff RP, Hansson M, Dietz KJ, Jensen PE., FEBS Lett 582(18), 2008
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Photosynthetic electron flow affects H2O2 signaling by inactivation of catalase in Chlamydomonas reinhardtii.
Shao N, Beck CF, Lemaire SD, Krieger-Liszkay A., Planta 228(6), 2008
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Redox regulation and antioxidative defence in Arabidopsis leaves viewed from a systems biology perspective.
Wormuth D, Heiber I, Shaikali J, Kandlbinder A, Baier M, Dietz KJ., J Biotechnol 129(2), 2007
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Oxidative modifications to cellular components in plants.
Møller IM, Jensen PE, Hansson A., Annu Rev Plant Biol 58(), 2007
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The mitochondrial type II peroxiredoxin from poplar
Gama F, Keech O, Eymery F, Finkemeier I, Gelhaye E, Gardeström P, Dietz KJ, Rey P, Jacquot JP, Rouhier N., Physiol Plant 129(1), 2007
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The peroxiredoxin repair proteins.
Jönsson TJ, Lowther WT., Subcell Biochem 44(), 2007
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The redox imbalanced mutants of Arabidopsis differentiate signaling pathways for redox regulation of chloroplast antioxidant enzymes.
Heiber I, Ströher E, Raatz B, Busse I, Kahmann U, Bevan MW, Dietz KJ, Baier M., Plant Physiol 143(4), 2007
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Thioredoxins in chloroplasts.
Lemaire SD, Michelet L, Zaffagnini M, Massot V, Issakidis-Bourguet E., Curr Genet 51(6), 2007
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Proteomic analysis reveals differences between Vitis vinifera L. cv. Chardonnay and cv. Cabernet Sauvignon and their responses to water deficit and salinity.
Vincent D, Ergül A, Bohlman MC, Tattersall EA, Tillett RL, Wheatley MD, Woolsey R, Quilici DR, Joets J, Schlauch K, Schooley DA, Cushman JC, Cramer GR., J Exp Bot 58(7), 2007
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Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.
Barranco-Medina S, Krell T, Finkemeier I, Sevilla F, Lázaro JJ, Dietz KJ., Plant Physiol Biochem 45(10-11), 2007
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The C-type Arabidopsis thioredoxin reductase ANTR-C acts as an electron donor to 2-Cys peroxiredoxins in chloroplasts.
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Hydroperoxide reduction by thioredoxin-specific glutathione peroxidase isoenzymes of Arabidopsis thaliana.
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