Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts
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...
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Published in | Journal of experimental botany Vol. 61; no. 14; pp. 4043 - 4054 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Oxford University Press
01.09.2010
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Subjects | |
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Abstract | 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 Δ2cp) with <5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc, trxx, and Δ2cp, 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 Fv/Fm, indicating additional functions of NTRC. |
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AbstractList | 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 Δ2cp) with <5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc, trxx, and Δ2cp, 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, CO 2 fixation, and F v /F m , indicating additional functions of NTRC. 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 Δ2cp) with <5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc, trxx, and Δ2cp, 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 Fv/Fm, indicating additional functions of NTRC. 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 Δ2cp ) with <5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc , trxx , and Δ2cp , 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, CO 2 fixation, and F v / F m , indicating additional functions of NTRC. 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 chi 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 chi 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 chi or 2-Cys Prxs as determined by growth, pigment content, CO(2) fixation, and F(v)/F(m), indicating additional functions of NTRC. 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 Δ2cp) with <5% of 2-Cys Prx content has been generated. The phenotypes of the three mutants, ntrc, trxx, and Δ2cp, 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 Fv/Fm, indicating additional functions of NTRC. |
Author | Sandalio, Luisa María Dietz, Karl-Josef González, Maricruz Sahrawy, Mariam Pascual, María Belén Cejudo, Francisco Javier Spínola, María Cristina Kirchsteiger, Kerstin Guinea, Manuel Pulido, Pablo |
AuthorAffiliation | 1 Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla and CSIC, Avda Américo Vespucio 49, 41092-Sevilla, Spain 2 Departamento de Bioquímica y Biología Molecular de Plantas, Estación Experimental del Zaidín, CSIC, C/Profesor Alvareda, 18008-Granada, Spain 3 Biochemistry and Physiology of Plants, W5-134, Bielefeld University, D-33501, Germany |
AuthorAffiliation_xml | – name: 3 Biochemistry and Physiology of Plants, W5-134, Bielefeld University, D-33501, Germany – name: 1 Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla and CSIC, Avda Américo Vespucio 49, 41092-Sevilla, Spain – name: 2 Departamento de Bioquímica y Biología Molecular de Plantas, Estación Experimental del Zaidín, CSIC, C/Profesor Alvareda, 18008-Granada, Spain |
Author_xml | – sequence: 1 fullname: Pulido, Pablo – sequence: 2 fullname: Spínola, María Cristina – sequence: 3 fullname: Kirchsteiger, Kerstin – sequence: 4 fullname: Guinea, Manuel – sequence: 5 fullname: Pascual, María Belén – sequence: 6 fullname: Sahrawy, Mariam – sequence: 7 fullname: Sandalio, Luisa María – sequence: 8 fullname: Dietz, Karl-Josef – sequence: 9 fullname: González, Maricruz – sequence: 10 fullname: Cejudo, Francisco Javier |
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IngestDate | Tue Sep 17 21:05:36 EDT 2024 Thu Sep 12 19:53:17 EDT 2024 Tue Oct 15 23:38:00 EDT 2024 Sun Oct 22 16:08:25 EDT 2023 Sun Oct 20 12:37:53 EDT 2024 Sun Mar 31 11:38:34 EDT 2024 Wed Dec 27 19:18:44 EST 2023 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
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Issue | 14 |
Keywords | Arabidopsis thaliana Oxidative stress peroxiredoxin Cruciferae Dicotyledones Angiospermae Botany Spermatophyta Functional analysis Experimental plant Thioredoxin Chloroplast |
Language | English |
License | CC BY 4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
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Notes | ark:/67375/HXZ-ZLZ1LMKN-K These authors contributed equally to this work. istex:430E7560776072A15B0EFF58DFEE1C3EE91D23B9 Present address: Centre for Research on Agricultural Genomics (CRAG), 08034-Barcelona, Spain |
OpenAccessLink | https://pubmed.ncbi.nlm.nih.gov/PMC2935875 |
PMID | 20616155 |
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PublicationDate | 2010-09-01 |
PublicationDateYYYYMMDD | 2010-09-01 |
PublicationDate_xml | – month: 09 year: 2010 text: 2010-09-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | Oxford |
PublicationPlace_xml | – name: Oxford – name: England |
PublicationTitle | Journal of experimental botany |
PublicationTitleAlternate | J Exp Bot |
PublicationYear | 2010 |
Publisher | Oxford University Press |
Publisher_xml | – name: Oxford University Press |
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SubjectTerms | Antioxidants Antioxidants - metabolism Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - metabolism Biological and medical sciences Chloroplast Chloroplasts Chloroplasts - enzymology Chloroplasts - metabolism Cysteine - metabolism Darkness Enzymes Fundamental and applied biological sciences. Psychology Hydrogen Peroxide - metabolism Leaves Light NADP - metabolism Oxidation-Reduction Oxidative stress Oxidative Stress - physiology Peroxides peroxiredoxin Peroxiredoxins - metabolism Phenotypes Photosynthesis Plant physiology Plants Research Papers Thioredoxin Thioredoxin-Disulfide Reductase - metabolism Thioredoxins - metabolism |
Title | Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts |
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