Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts
Pulido P, Cristina Spinola M, Kirchsteiger K, Guinea M, Belen Pascual M, Sahrawy M, Maria Sandalio L, Dietz K-J, Gonzalez M, Javier Cejudo F (2010)
JOURNAL OF EXPERIMENTAL BOTANY 61(14): 4043-4054.
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Autor*in
Pulido, Pablo;
Cristina Spinola, Maria;
Kirchsteiger, Kerstin;
Guinea, Manuel;
Belen Pascual, Maria;
Sahrawy, Mariam;
Maria Sandalio, Luisa;
Dietz, Karl-JosefUniBi;
Gonzalez, Maricruz;
Javier Cejudo, Francisco
Einrichtung
Abstract / Bemerkung
Photosynthesis is a process that inevitably produces reactive oxygen species, such as hydrogen peroxide, which is reduced by chloroplast-localized detoxification mechanisms one of which involves 2-Cys peroxiredoxins (2-Cys Prxs). Arabidopsis chloroplasts contain two very similar 2-Cys Prxs (denoted A and B). These enzymes are reduced by two pathways: NADPH thioredoxin reductase C (NTRC), which uses NADPH as source of reducing power; and plastidial thioredoxins (Trxs) coupled to photosynthetically reduced ferredoxin of which Trx x is the most efficient reductant in vitro. With the aim of establishing the functional relationship between NTRC, Trx x, and 2-Cys Prxs in vivo, an Arabidopsis Trx x knock-out mutant has been identified and a double mutant (denoted delta 2cp) with < 5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc, trxx, and delta 2cp, were compared under standard growth conditions and in response to continuous light or prolonged darkness and oxidative stress. Though all mutants showed altered redox homeostasis, no difference was observed in response to oxidative stress treatment. Moreover, the redox status of the 2-Cys Prx was imbalanced in the ntrc mutant but not in the trxx mutant. These results show that NTRC is the most relevant pathway for chloroplast 2-Cys Prx reduction in vivo, but the antioxidant function of this system is not essential. The deficiency of NTRC caused a more severe phenotype than the deficiency of Trx x or 2-Cys Prxs as determined by growth, pigment content, CO2 fixation, and F-v/F-m, indicating additional functions of NTRC.
Stichworte
oxidative stress;
Chloroplast;
peroxiredoxin;
thioredoxin
Erscheinungsjahr
2010
Zeitschriftentitel
JOURNAL OF EXPERIMENTAL BOTANY
Band
61
Ausgabe
14
Seite(n)
4043-4054
ISSN
0022-0957
eISSN
1460-2431
Page URI
https://pub.uni-bielefeld.de/record/1793927
Zitieren
Pulido P, Cristina Spinola M, Kirchsteiger K, et al. Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. JOURNAL OF EXPERIMENTAL BOTANY. 2010;61(14):4043-4054.
Pulido, P., Cristina Spinola, M., Kirchsteiger, K., Guinea, M., Belen Pascual, M., Sahrawy, M., Maria Sandalio, L., et al. (2010). Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. JOURNAL OF EXPERIMENTAL BOTANY, 61(14), 4043-4054. https://doi.org/10.1093/jxb/erq218
Pulido, Pablo, Cristina Spinola, Maria, Kirchsteiger, Kerstin, Guinea, Manuel, Belen Pascual, Maria, Sahrawy, Mariam, Maria Sandalio, Luisa, Dietz, Karl-Josef, Gonzalez, Maricruz, and Javier Cejudo, Francisco. 2010. “Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts”. JOURNAL OF EXPERIMENTAL BOTANY 61 (14): 4043-4054.
Pulido, P., Cristina Spinola, M., Kirchsteiger, K., Guinea, M., Belen Pascual, M., Sahrawy, M., Maria Sandalio, L., Dietz, K. - J., Gonzalez, M., and Javier Cejudo, F. (2010). Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. JOURNAL OF EXPERIMENTAL BOTANY 61, 4043-4054.
Pulido, P., et al., 2010. Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. JOURNAL OF EXPERIMENTAL BOTANY, 61(14), p 4043-4054.
P. Pulido, et al., “Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts”, JOURNAL OF EXPERIMENTAL BOTANY, vol. 61, 2010, pp. 4043-4054.
Pulido, P., Cristina Spinola, M., Kirchsteiger, K., Guinea, M., Belen Pascual, M., Sahrawy, M., Maria Sandalio, L., Dietz, K.-J., Gonzalez, M., Javier Cejudo, F.: Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. JOURNAL OF EXPERIMENTAL BOTANY. 61, 4043-4054 (2010).
Pulido, Pablo, Cristina Spinola, Maria, Kirchsteiger, Kerstin, Guinea, Manuel, Belen Pascual, Maria, Sahrawy, Mariam, Maria Sandalio, Luisa, Dietz, Karl-Josef, Gonzalez, Maricruz, and Javier Cejudo, Francisco. “Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts”. JOURNAL OF EXPERIMENTAL BOTANY 61.14 (2010): 4043-4054.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
4 Einträge gefunden, die diesen Artikel zitieren
Thioredoxin X, chloroplastic (UNIPROT: Q8LD49)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
2-Cys peroxiredoxin BAS1-like, chloroplastic (UNIPROT: Q9C5R8)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
2-Cys peroxiredoxin BAS1, chloroplastic (UNIPROT: Q96291)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
NADPH-dependent thioredoxin reductase 3 (UNIPROT: O22229)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
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Penuelas J, Munne-Bosch S., Trends Plant Sci. 10(4), 2005
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A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity.
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Perez-Ruiz JM, Cejudo FJ., FEBS Lett. 583(9), 2009
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Perez-Ruiz JM, Spinola MC, Kirchsteiger K, Moreno J, Sahrawy M, Cejudo FJ., Plant Cell 18(9), 2006
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Petersson UA, Kieselbach T, Garcia-Cerdan JG, Schroder WP., FEBS Lett. 580(26), 2006
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Rascher U, Nedbal L., Curr. Opin. Plant Biol. 9(6), 2006
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Rodriguez Milla MA, Maurer A, Rodriguez Huete A, Gustafson JP., Plant J. 36(5), 2003
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S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
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Rouhier N, Jacquot JP., Photosyn. Res. 74(3), 2002
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Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase–thioredoxin h system from wheat
Serrato AJ, Pérez-Ruiz JM, Cejudo FJ., 2002
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A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana.
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NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg-protoporphyrin monomethyl ester cyclase.
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Unraveling the tapestry of networks involving reactive oxygen species in plants.
Van Breusegem F, Bailey-Serres J, Mittler R., Plant Physiol. 147(3), 2008
PMID: 18612075
Van Breusegem F, Bailey-Serres J, Mittler R., Plant Physiol. 147(3), 2008
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The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana.
Wagner D, Przybyla D, Op den Camp R, Kim C, Landgraf F, Lee KP, Wursch M, Laloi C, Nater M, Hideg E, Apel K., Science 306(5699), 2004
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Wagner D, Przybyla D, Op den Camp R, Kim C, Landgraf F, Lee KP, Wursch M, Laloi C, Nater M, Hideg E, Apel K., Science 306(5699), 2004
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Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.
Wood ZA, Poole LB, Karplus PA., Science 300(5619), 2003
PMID: 12714747
Wood ZA, Poole LB, Karplus PA., Science 300(5619), 2003
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