The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts

© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 66(2015), 10 vom: 01. Mai, Seite 2957-66
1. Verfasser: Puerto-Galán, Leonor (VerfasserIn)
Weitere Verfasser: Pérez-Ruiz, Juan M, Guinea, Manuel, Cejudo, Francisco Javier
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't 2-Cys peroxiredoxin Arabidopsis thaliana chloroplast overoxidation redox regulation sulfiredoxin thioredoxin reductase. Arabidopsis Proteins mehr... Peroxiredoxins EC 1.11.1.15 Oxidoreductases Acting on Sulfur Group Donors EC 1.8.- Thioredoxin-Disulfide Reductase EC 1.8.1.9 sulfiredoxin protein, Arabidopsis EC 1.8.98.2 Cysteine K848JZ4886
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245 1 4 |a The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts 
264 1 |c 2015 
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520 |a © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. 
520 |a Hydrogen peroxide is a harmful by-product of photosynthesis, which also has important signalling activity. Therefore, the level of hydrogen peroxide needs to be tightly controlled. Chloroplasts harbour different antioxidant systems including enzymes such as the 2-Cys peroxiredoxins (2-Cys Prxs). Under oxidizing conditions, 2-Cys Prxs are susceptible to inactivation by overoxidation of their peroxidatic cysteine, which is enzymatically reverted by sulfiredoxin (Srx). In chloroplasts, the redox status of 2-Cys Prxs is highly dependent on NADPH-thioredoxin reductase C (NTRC) and Srx; however, the relationship of these activities in determining the level of 2-Cys Prx overoxidation is unknown. Here we have addressed this question by a combination of genetic and biochemical approaches. An Arabidopsis thaliana double knockout mutant lacking NTRC and Srx shows a phenotype similar to the ntrc mutant, while the srx mutant resembles wild-type plants. The deficiency of NTRC causes reduced overoxidation of 2-Cys Prxs, whereas the deficiency of Srx has the opposite effect. Moreover, in vitro analyses show that the disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation, thus explaining the dominant role of NTRC on the level of 2-Cys Prx overoxidation in vivo. The overoxidation of chloroplast 2-Cys Prxs shows no circadian oscillation, in agreement with the fact that neither the NTRC nor the SRX genes show circadian regulation of expression. Additionally, the low level of 2-Cys Prx overoxidation in the ntrc mutant is light dependent, suggesting that the redox status of 2-Cys Prxs in chloroplasts depends on light rather than the circadian clock 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a 2-Cys peroxiredoxin 
650 4 |a Arabidopsis thaliana 
650 4 |a chloroplast 
650 4 |a overoxidation 
650 4 |a redox regulation 
650 4 |a sulfiredoxin 
650 4 |a thioredoxin reductase. 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Peroxiredoxins  |2 NLM 
650 7 |a EC 1.11.1.15  |2 NLM 
650 7 |a Oxidoreductases Acting on Sulfur Group Donors  |2 NLM 
650 7 |a EC 1.8.-  |2 NLM 
650 7 |a Thioredoxin-Disulfide Reductase  |2 NLM 
650 7 |a EC 1.8.1.9  |2 NLM 
650 7 |a sulfiredoxin protein, Arabidopsis  |2 NLM 
650 7 |a EC 1.8.98.2  |2 NLM 
650 7 |a Cysteine  |2 NLM 
650 7 |a K848JZ4886  |2 NLM 
700 1 |a Pérez-Ruiz, Juan M  |e verfasserin  |4 aut 
700 1 |a Guinea, Manuel  |e verfasserin  |4 aut 
700 1 |a Cejudo, Francisco Javier  |e verfasserin  |4 aut 
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773 1 8 |g volume:66  |g year:2015  |g number:10  |g day:01  |g month:05  |g pages:2957-66 
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