Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis

Horling F, Lamkemeyer P, König J, Finkemeier I, Kandlbinder A, Baier M, Dietz K-J (2003)
Plant Physiology 131(1): 317-325.

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DOI
Autor*in
Horling, F.; Lamkemeyer, P.; König, JanineUniBi; Finkemeier, I.; Kandlbinder, AndreaUniBi; Baier, M.; Dietz, Karl-JosefUniBi
Einrichtung
Centrum für Biotechnologie > Arbeitsgruppe K.-J. Dietz
Fakultät für Biologie > Biochemie und Physiologie der Pflanzen
Centrum für Biotechnologie > Institut für Genomforschung und Systembiologie
Abstract / Bemerkung
Peroxiredoxins (prxs) are peroxidases with broad substrate specificity. The seven prx genes expressed in Arabidopsis shoots were analyzed for their expressional response to changing photon fluence rates, oxidative stress, and ascorbate application. The results reveal a highly variable and gene-specific response to reducing and oxidizing conditions. The steady-state transcript amounts of the chloroplast-targeted prxs, namely the two-cysteine (2-Cys) prxs, prx Q and prx II E, decreased upon application of ascorbate. prx Q also responded to peroxides and diamide treatment. prx II B was induced by tertiary butylhydroperoxide, but rather unaffected by ascorbate. The strongest responses were observed for prx II C, which was induced with all treatments. The two Arabidopsis 2-Cys Prxs and four Prx II proteins were expressed heterologously in Escherichia coli. In an in vitro test system, they all showed peroxidase activity, but could be distinguished by their ability to accept dithiothreitol and thioredoxin as electron donor in the regeneration reaction. The midpoint redox potentials (E-m') of Prx II B, Prx II C, and Prx II E were around -290 mV and, thus, less negative than E-m' of Prx II F, 2-Cys Prx A, and 2-Cys Prx B (-307 to -322 mV). The data characterize expression and function of the mitochondrial Prx II F and the chloroplast Prx II E for the first time, to our knowledge. Antibodies directed against 2-Cys Prx and Prx II C showed a slight up-regulation of Prx II protein in strong light and of 2-Cys Prx upon transfer both to high and low light. The results are discussed in context with the subcellular localization of the Prx gene products.
Stichworte
Peroxiredoxins Peroxidases/*genetics/metabolism Plant Shoots/metabolism Oxidative Stress/*physiology Oxidation-Reduction Gene Expression Regulation Enzymologic/drug effects/radiation effects Hydrogen Peroxide/pharmacology Multigene Family/genetics Light Plant/drug effects/radiation effects Gene Expression Regulation Ascorbic Acid/*pharmacology Arabidopsis Proteins/*genetics/metabolism Arabidopsis/drug effects/*genetics/radiation effects
Erscheinungsjahr
2003
Zeitschriftentitel
Plant Physiology
Band
131
Ausgabe
1
Seite(n)
317-325
ISSN
0032-0889
eISSN
1532-2548
Page URI
https://pub.uni-bielefeld.de/record/1612610

Zitieren

Horling F, Lamkemeyer P, König J, et al. Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiology. 2003;131(1):317-325.
Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M., & Dietz, K. - J. (2003). Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiology, 131(1), 317-325. https://doi.org/10.1104/pp.010017
Horling, F., Lamkemeyer, P., König, Janine, Finkemeier, I., Kandlbinder, Andrea, Baier, M., and Dietz, Karl-Josef. 2003. “Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis”. Plant Physiology 131 (1): 317-325.
Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M., and Dietz, K. - J. (2003). Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiology 131, 317-325.
Horling, F., et al., 2003. Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiology, 131(1), p 317-325.
F. Horling, et al., “Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis”, Plant Physiology, vol. 131, 2003, pp. 317-325.
Horling, F., Lamkemeyer, P., König, J., Finkemeier, I., Kandlbinder, A., Baier, M., Dietz, K.-J.: Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiology. 131, 317-325 (2003).
Horling, F., Lamkemeyer, P., König, Janine, Finkemeier, I., Kandlbinder, Andrea, Baier, M., and Dietz, Karl-Josef. “Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis”. Plant Physiology 131.1 (2003): 317-325.

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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 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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Proteomic analysis of leaf proteins during dehydration of the resurrection plant Xerophyta viscosa.
Ingle RA, Schmidt UG, Farrant JM, Thomson JA, Mundree SG., Plant Cell Environ 30(4), 2007
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A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome.
Marmagne A, Ferro M, Meinnel T, Bruley C, Kuhn L, Garin J, Barbier-Brygoo H, Ephritikhine G., Mol Cell Proteomics 6(11), 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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Wheat (Triticum aestivum L.) root proteome and differentially expressed root proteins between hybrid and parents.
Song X, Ni Z, Yao Y, Xie C, Li Z, Wu H, Zhang Y, Sun Q., Proteomics 7(19), 2007
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Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii.
Naumann B, Busch A, Allmer J, Ostendorf E, Zeller M, Kirchhoff H, Hippler M., Proteomics 7(21), 2007
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S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
Romero-Puertas MC, Laxa M, Mattè A, Zaninotto F, Finkemeier I, Jones AM, Perazzolli M, Vandelle E, Dietz KJ, Delledonne M., Plant Cell 19(12), 2007
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Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence.
Groten K, Dutilleul C, van Heerden PD, Vanacker H, Bernard S, Finkemeier I, Dietz KJ, Foyer CH., FEBS Lett 580(5), 2006
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Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis.
Lamkemeyer P, Laxa M, Collin V, Li W, Finkemeier I, Schöttler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, Miginiac-Maslow M, Dietz KJ., Plant J 45(6), 2006
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Molecular and functional characterization of sulfiredoxin homologs from higher plants.
Liu XP, Liu XY, Zhang J, Xia ZL, Liu X, Qin HJ, Wang DW., Cell Res 16(3), 2006
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Metabolic signalling in defence and stress: the central roles of soluble redox couples.
Noctor G., Plant Cell Environ 29(3), 2006
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Photoprotection mutants of Arabidopsis thaliana acclimate to high light by increasing photosynthesis and specific antioxidants.
Golan T, Müller-Moulé P, Niyogi KK., Plant Cell Environ 29(5), 2006
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Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum.
Barranco-Medina S, López-Jaramillo FJ, Bernier-Villamor L, Sevilla F, Lázaro JJ., Acta Crystallogr Sect F Struct Biol Cryst Commun 62(pt 7), 2006
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Analysis of oxidative signalling induced by ozone in Arabidopsis thaliana.
Mahalingam R, Jambunathan N, Gunjan SK, Faustin E, Weng H, Ayoubi P., Plant Cell Environ 29(7), 2006
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Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-Cycle enzymes during early seedling development of Arabidopsis thaliana.
Pena-Ahumada A, Kahmann U, Dietz KJ, Baier M., Photosynth Res 89(2-3), 2006
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Proteomic analysis of the etioplast inner membranes of wheat (Triticum aestivum) by two-dimensional electrophoresis and mass spectrometry
Blomqvist LA, Ryberg M, Sundqvist C., Physiol Plant 128(2), 2006
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The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome.
Petersson UA, Kieselbach T, García-Cerdán JG, Schröder WP., FEBS Lett 580(26), 2006
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A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress.
Kiba A, Nishihara M, Tsukatani N, Nakatsuka T, Kato Y, Yamamura S., Plant Cell Physiol 46(6), 2005
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Chloroplasts as source and target of cellular redox regulation: a discussion on chloroplast redox signals in the context of plant physiology.
Baier M, Dietz KJ., J Exp Bot 56(416), 2005
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Identification of plant glutaredoxin targets.
Rouhier N, Villarejo A, Srivastava M, Gelhaye E, Keech O, Droux M, Finkemeier I, Samuelsson G, Dietz KJ, Jacquot JP, Wingsle G., Antioxid Redox Signal 7(7-8), 2005
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Proteomics viewed on stress response of thermophilic bacterium Bacillus stearothermophilus TLS33.
Topanurak S, Sinchaikul S, Phutrakul S, Sookkheo B, Chen ST., Proteomics 5(14), 2005
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Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942 for the presence of peroxiredoxins and their transcript regulation under stress.
Stork T, Michel KP, Pistorius EK, Dietz KJ., J Exp Bot 56(422), 2005
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Thioredoxins in Arabidopsis and other plants.
Meyer Y, Reichheld JP, Vignols F., Photosynth Res 86(3), 2005
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Characterization of transformed Arabidopsis with altered alternative oxidase levels and analysis of effects on reactive oxygen species in tissue.
Umbach AL, Fiorani F, Siedow JN., Plant Physiol 139(4), 2005
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The accumulation of abundant soluble proteins changes early in the development of the primary roots of maize (Zea mays L.).
Hochholdinger F, Woll K, Guo L, Schnable PS., Proteomics 5(18), 2005
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The antioxidant status of photosynthesizing leaves under nutrient deficiency: redox regulation, gene expression and antioxidant activity in Arabidopsis thaliana.
Kandlbinder A, Finkemeier I, Wormuth D, Hanitzsch M, Dietz KJ., Physiol Plant 120(1), 2004
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In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database.
Friso G, Giacomelli L, Ytterberg AJ, Peltier JB, Rudella A, Sun Q, Wijk KJ., Plant Cell 16(2), 2004
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Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.
Rouhier N, Gelhaye E, Gualberto JM, Jordy MN, De Fay E, Hirasawa M, Duplessis S, Lemaire SD, Frey P, Martin F, Manieri W, Knaff DB, Jacquot JP., Plant Physiol 134(3), 2004
PMID: 14976238
Control of photosynthetic and high-light-responsive genes by the histidine kinase DspA: negative and positive regulation and interactions between signal transduction pathways.
Hsiao HY, He Q, Van Waasbergen LG, Grossman AR., J Bacteriol 186(12), 2004
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Specific changes in the Arabidopsis proteome in response to bacterial challenge: differentiating basal and R-gene mediated resistance.
Jones AM, Thomas V, Truman B, Lilley K, Mansfield J, Grant M., Phytochemistry 65(12), 2004
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The acceptor availability at photosystem I and ABA control nuclear expression of 2-Cys peroxiredoxin-A in Arabidopsis thaliana.
Baier M, Ströher E, Dietz KJ., Plant Cell Physiol 45(8), 2004
PMID: 15356325
Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex.
Kluge C, Seidel T, Bolte S, Sharma SS, Hanitzsch M, Satiat-Jeunemaitre B, Ross J, Sauer M, Golldack D, Dietz KJ., BMC Cell Biol 5(), 2004
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A method for diagnosis of plant environmental stresses by gene expression profiling using a cDNA macroarray.
Tamaoki M, Matsuyama T, Nakajima N, Aono M, Kubo A, Saji H., Environ Pollut 131(1), 2004
PMID: 15210282
Comparative proteome analysis of differentially expressed proteins induced by K+ deficiency in Arabidopsis thaliana.
Kang JG, Pyo YJ, Cho JW, Cho MH., Proteomics 4(11), 2004
PMID: 15449379
Molecular cloning and characterization of a stress-induced peroxiredoxin Q gene in halophyte Suaeda salsa.
Guo XL, Cao YR, Cao ZY, Zhao YX, Zhang H., Plant Sci 167(5), 2004
PMID: IND43645556
Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type.
Collin V, Lamkemeyer P, Miginiac-Maslow M, Hirasawa M, Knaff DB, Dietz KJ, Issakidis-Bourguet E., Plant Physiol 136(4), 2004
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Plant peroxiredoxins.
Dietz KJ., Annu Rev Plant Biol 54(), 2003
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Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii.
Lemaire SD, Collin V, Keryer E, Quesada A, Miginiac-Maslow M., FEBS Lett 543(1-3), 2003
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Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity.
Bréhélin C, Meyer EH, de Souris JP, Bonnard G, Meyer Y., Plant Physiol 132(4), 2003
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Zeaxanthin deficiency enhances the high light sensitivity of an ascorbate-deficient mutant of Arabidopsis.
Müller-Moulé P, Havaux M, Niyogi KK., Plant Physiol 133(2), 2003
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Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins.
Leyens G, Donnay I, Knoops B., Comp Biochem Physiol B Biochem Mol Biol 136(4), 2003
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