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Function and Regulation of Chloroplast Peroxiredoxin IIE

Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany
Applied Biochemistry Group, Leibniz Institute for Plant Genetics and Crop Plant Research (IPK), 06466 Gatersleben, Germany
Author to whom correspondence should be addressed.
Shared first authorship due to equal contribution to this research.
Current affiliation: Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Current affiliation: Australian Research Council Centre of Excellence in Plant Cell Walls, University of Adelaide, Adelaide, SA 5064, Australia.
Academic Editor: Mirko Zaffagnini
Antioxidants 2021, 10(2), 152;
Received: 4 November 2020 / Revised: 28 December 2020 / Accepted: 13 January 2021 / Published: 21 January 2021
(This article belongs to the Special Issue Peroxiredoxin)
Peroxiredoxins (PRX) are thiol peroxidases that are highly conserved throughout all biological kingdoms. Increasing evidence suggests that their high reactivity toward peroxides has a function not only in antioxidant defense but in particular in redox regulation of the cell. Peroxiredoxin IIE (PRX-IIE) is one of three PRX types found in plastids and has previously been linked to pathogen defense and protection from protein nitration. However, its posttranslational regulation and its function in the chloroplast protein network remained to be explored. Using recombinant protein, it was shown that the peroxidatic Cys121 is subjected to multiple posttranslational modifications, namely disulfide formation, S-nitrosation, S-glutathionylation, and hyperoxidation. Slightly oxidized glutathione fostered S-glutathionylation and inhibited activity in vitro. Immobilized recombinant PRX-IIE allowed trapping and subsequent identification of interaction partners by mass spectrometry. Interaction with the 14-3-3 υ protein was confirmed in vitro and was shown to be stimulated under oxidizing conditions. Interactions did not depend on phosphorylation as revealed by testing phospho-mimicry variants of PRX-IIE. Based on these data it is proposed that 14-3-3υ guides PRX‑IIE to certain target proteins, possibly for redox regulation. These findings together with the other identified potential interaction partners of type II PRXs localized to plastids, mitochondria, and cytosol provide a new perspective on the redox regulatory network of the cell. View Full-Text
Keywords: peroxiredoxin; AT3G52960; glutathione; S-glutathionylation; glutaredoxin; 14-3-3 protein; phosphorylation; posttranslational modification; redox regulatory network peroxiredoxin; AT3G52960; glutathione; S-glutathionylation; glutaredoxin; 14-3-3 protein; phosphorylation; posttranslational modification; redox regulatory network
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    Doi: 10.5447/ipk/2021/0
    Description: Raw Data of the MS measurements are available at the eDAL System as mentioned in the materials and method section of the main text.
MDPI and ACS Style

Dreyer, A.; Treffon, P.; Basiry, D.; Jozefowicz, A.M.; Matros, A.; Mock, H.-P.; Dietz, K.-J. Function and Regulation of Chloroplast Peroxiredoxin IIE. Antioxidants 2021, 10, 152.

AMA Style

Dreyer A, Treffon P, Basiry D, Jozefowicz AM, Matros A, Mock H-P, Dietz K-J. Function and Regulation of Chloroplast Peroxiredoxin IIE. Antioxidants. 2021; 10(2):152.

Chicago/Turabian Style

Dreyer, Anna, Patrick Treffon, Daniel Basiry, Anna Maria Jozefowicz, Andrea Matros, Hans-Peter Mock, and Karl-Josef Dietz. 2021. "Function and Regulation of Chloroplast Peroxiredoxin IIE" Antioxidants 10, no. 2: 152.

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