Author response: The chloroplast 2-cysteine peroxiredoxin functions as thioredoxin oxidase in redox regulation of chloroplast metabolism

Vaseghi, Mohamad-Javad; Chibani, Kamel; Telman, Wilena; Liebthal, Michael; Gerken, Melanie; Schnitzer, Helena; Mueller, Sara Mareike; Dietz, Karl‐Josef

doi:10.7554/elife.38194.038

Cited by 4 publications

(3 citation statements)

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“…ROS-mediated changes play a fundamental role in cell signalling and this function also includes a direct or indirect role as retrograde signals in the chloroplast-cytosol/nucleus communication [49][50][51]. ROS function in retrograde signalling by three mechanisms: (i) H 2 O 2 may be transferred to the extra-chloroplast space by aquaporin-mediated transport [52] or diffusive leakage; (ii) ROS alter metabolic activities in the chloroplast, leading, e.g., to different metabolite levels and ratios, which then deliver information to the extrachloroplast space; (iii) ROS react with reactive chloroplast molecules like lipids or peptides and the generated reaction products leave the chloroplast and affect extrachloroplast processes like transcription, translation and metabolism to enable the acclimation process [50,51 [54]. Under more severe stress, they may trigger oxidative stress responses which in turn liberate retrograde signalling via signalling metabolites such as haem, MEcPP and PAP [55].…”

Section: Reaction Products Of Chloroplast-originated Reactive Oxygen mentioning

confidence: 99%

“…Work with redox and ROS mutants like alx8, xm2 and xm3 demonstrated that SAL1 functions as an oxidative sensor in the chloroplast. ROS accumulation under stress alters the redox poise of the stroma and oxidizes thiols of target proteins either directly [85] or, e.g., via TRX oxidation [54]. Oxidized SAL1 is inhibited and this triggers PAP accumulation in the chloroplast and cytosol.…”

Section: Retrograde Signals From Overreduced Psi (A) Retrograde Signalling Via Methylerythritol Cyclodiphosphatementioning

confidence: 99%

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Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling

Ünal

García‐Caparrós

Kumar

et al. 2020

Phil. Trans. R. Soc. B

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Chloroplasts compose about one-quarter of the mesophyll cell volume and contain about 60% of the cell protein. Photosynthetic carbon assimilation is the dominating metabolism in illuminated leaves. To optimize the resource expenditure in these costly organelles and to control and adjust chloroplast metabolism, an intensive transfer of information between nucleus–cytoplasm and chloroplasts occurs in both directions as anterograde and retrograde signalling. Recent research identified multiple retrograde pathways that use metabolite transfer and include reaction products of lipids and carotenoids with reactive oxygen species (ROS). Other pathways use metabolites of carbon, sulfur and nitrogen metabolism, low molecular weight antioxidants and hormone precursors to carry information between the cell compartments. This review focuses on redox- and ROS-related retrograde signalling pathways. In analogy to the microbe-associated molecular pattern, we propose the term ‘chloroplast-associated molecular pattern' which connects chloroplast performance to extrachloroplast processes such as nuclear gene transcription, posttranscriptional processing, including translation, and RNA and protein fate. This article is part of the theme issue ‘Retrograde signalling from endosymbiotic organelles'.

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Section: Reaction Products Of Chloroplast-originated Reactive Oxygen mentioning

confidence: 99%

Section: Retrograde Signals From Overreduced Psi (A) Retrograde Signalling Via Methylerythritol Cyclodiphosphatementioning

confidence: 99%

Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling

Ünal

García‐Caparrós

Kumar

et al. 2020

Phil. Trans. R. Soc. B

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“…The best understood plant PRX is the 2-CysPRX, which has been scrutinized with respect to its catalytic properties, redox-dependent conformational dynamics, regeneration by electron transmitters such as TRX and GRX/GSH and its role in the redox regulatory network of the chloroplast [5][6][7][8]. In contrast PRX-Q and PRX-IIE have been studied for their peroxidatic property, regeneration mechanism and their function in mutant plants with decreased protein amounts [9,10].…”

Section: Introductionmentioning

confidence: 99%

Function and regulation of chloroplast peroxiredoxin IIE

Dreyer

Treffon

Basiry

et al. 2020

Preprint

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Peroxiredoxins (PRX) are thiol peroxidases which 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 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.

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The Induction of Pyrenoid Synthesis by Hyperoxia and its Implications for the Natural Diversity of Photosynthetic Responses inChlamydomonas

Neofotis

Temple

Tessmer

et al. 2021

Preprint

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In algae, it is well established that the pyrenoid, a component of the carbon-concentrating mechanism (CCM), is essential for efficient photosynthesis at low CO2. However, the signal that triggers the formation of the pyrenoid has remained elusive. Here, we show that, in Chlamydomonas reinhardtii, the pyrenoid is strongly induced by hyperoxia, even at high CO2 or bicarbonate levels. These results suggest that the pyrenoid can be induced by a common product of photosynthesis specific to low CO2 or hyperoxia. Consistent with this view, the photorespiratory by-product, H2O2, induced the pyrenoid, suggesting that it acts as a signal. Finally, we show evidence for linkages between genetic variations in hyperoxia tolerance, H2O2 signaling, and pyrenoid morphologies.

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Author response: The chloroplast 2-cysteine peroxiredoxin functions as thioredoxin oxidase in redox regulation of chloroplast metabolism

Cited by 4 publications

References 0 publications

Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling

Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling

Function and regulation of chloroplast peroxiredoxin IIE

The Induction of Pyrenoid Synthesis by Hyperoxia and its Implications for the Natural Diversity of Photosynthetic Responses inChlamydomonas

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