Redox‐control of chlorophyll biosynthesis mainly depends on thioredoxins

Richter, Andreas; Pérez-Ruiz, Juan Manuel; Cejudo, Francisco Javier; Grimm, Bernhard

doi:10.1002/1873-3468.13216

Cited by 25 publications

(18 citation statements)

References 15 publications

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“…The analysis of the redox state of Trxs f , FBPase and PRK in the suppressed line fully confirmed this hypothesis hence uncovering the central function of 2-Cys Prxs in chloroplast redox regulation (Pérez-Ruiz et al, 2017). Moreover, the suppressed line also recovered wild type levels of chlorophyll biosynthesis enzymes (Richter et al, 2018), indicating that the suppressor effect caused by decreased levels of 2-Cys Prxs is exerted beyond the enzymes of the CBC. Based on these results, we proposed a model according to which the redox balance of 2-Cys Prxs, which is maintained by NTRC and NADPH, modulates the light-dependent reduction of redox regulated enzymes based on Fdx reduced by the photosynthetic electron transport chain, which is fueled to stromal Trxs via the action of FTR (Pérez-Ruiz et al, 2017).…”

Section: The Central Role Of 2-cys Prxs: Integrating Antioxidant and mentioning

confidence: 97%

Chloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darkness

et al. 2019

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Light is probably the most important environmental stimulus for plant development. As sessile organisms, plants have developed regulatory mechanisms that allow the rapid adaptation of their metabolism to changes in light availability. Redox regulation based on disulfide-dithiol exchange constitutes a rapid and reversible post-translational modification, which affects protein conformation and activity. This regulatory mechanism was initially discovered in chloroplasts when it was identified that enzymes of the Calvin-Benson cycle (CBC) are reduced and active during the day and become rapidly inactivated by oxidation in the dark. At present, the large number of redox-sensitive proteins identified in chloroplasts extend redox regulation far beyond the CBC. The classic pathway of redox regulation in chloroplasts establishes that ferredoxin (Fdx) reduced by the photosynthetic electron transport chain fuels reducing equivalents to the large set of thioredoxins (Trxs) of this organelle via the activity of a Fdx-dependent Trx reductase (FTR), hence linking redox regulation to light. In addition, chloroplasts harbor an NADPH-dependent Trx reductase with a joint Trx domain, termed NTRC. The presence in chloroplasts of this NADPH-dependent redox system raises the question of the functional relationship between NTRC and the Fdx-FTR-Trx pathways. Here, we update the current knowledge of these two redox systems focusing on recent evidence showing their functional interrelationship through the action of the thiol-dependent peroxidase, 2-Cys peroxiredoxin (2-Cys Prx). The relevant role of 2-Cys Prxs in chloroplast redox homeostasis suggests that hydrogen peroxide may exert a key function to control the redox state of stromal enzymes. Indeed, recent reports have shown the participation of 2-Cys Prxs in enzyme oxidation in the dark, thus providing an explanation for the long-lasting question of photosynthesis deactivation during the light-dark transition.

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Section: The Central Role Of 2-cys Prxs: Integrating Antioxidant and mentioning

confidence: 97%

Chloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darkness

et al. 2019

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“…It has been shown that a deficiency of f- and m-type TRX variants and NTRC leads to an obvious pale-green leaf phenotype and multiple defects in the TBS pathway [ 10 , 11 ]. Thus far, four TBS enzymes have been proved to be targets of TRX and NTRC for the reduction of thiol bonds: the rate-limiting enzyme glutamyl-tRNA reductase (GluTR) [ 10 , 12 ], magnesium protoporphyrin IX methyltransferase (CHLM) [ 10 , 12 , 13 , 14 ], the I subunit of magnesium chelatase (CHLI) [ 11 , 15 ] and the Mg–protoporphyrin monomethylester cyclase (CHL27) [ 16 ]. Among other TBS enzymes, glutamate 1-semialdehyde aminotransferase (GSAAT), 5-aminolevulinic acid dehydratase (ALAD), protoporphyrinogen oxidase (PPOX) and protochlorophyllide oxidoreductase (POR) were suggested to be the potential interacting partner of TRXs and NTRC [ 17 , 18 ].…”

Section: Introductionmentioning

confidence: 99%

Towards Initial Indications for a Thiol-Based Redox Control of Arabidopsis 5-Aminolevulinic Acid Dehydratase

et al. 2018

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Thiol-based redox control is one of the important posttranslational mechanisms of the tetrapyrrole biosynthesis pathway. Many enzymes of the pathway have been shown to interact with thioredoxin (TRX) and Nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase C (NTRC). We examined the redox-dependency of 5-aminolevulinic acid dehydratase (ALAD), which catalyzed the conjugation of two 5-aminolevulinic acid (ALA) molecules to porphobilinogen. ALAD interacted with TRX f, TRX m and NTRC in chloroplasts. Consequently, less ALAD protein accumulated in the trx f1, ntrc and trx f1/ntrc mutants compared to wild-type control resulting in decreased ALAD activity. In a polyacrylamide gel under non-reducing conditions, ALAD monomers turned out to be present in reduced and two oxidized forms. The reduced and oxidized forms of ALAD differed in their catalytic activity. The addition of TRX stimulated ALAD activity. From our results it was concluded that (i) deficiency of the reducing power mainly affected the in planta stability of ALAD; and (ii) the reduced form of ALAD displayed increased enzymatic activity.

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“…Major biological functions of plant thioredoxins include posttranslational redox regulation of a wide array of proteins, participation in antioxidative scavenging and signaling networks, overcoming oxidative damages to macromolecules as well as intercellular communication [ 6 , 25 , 26 ]. Several isoforms of thioredoxins ( f -, m -, x -, y -, and z -type) have been identified in chloroplasts, and their main biological role is associated with modulation of activity of target proteins involved in photosynthesis process [ 27 , 28 ].…”

Section: Discussionmentioning

confidence: 99%

“…According to these authors, the two thioredoxin systems present in chloroplasts work together in order to regulate the plant growth under diverse light conditions. Richter et al [ 6 ] claimed that redox-control biogenesis of chlorophylls in higher plants is mainly linked to functioning of a wide spectrum of thioredoxins. In addition, A. thaliana seedlings with inactivated expression of three m -type thioredoxins-encoding genes (i.e., Trxm1 , Trxm2 , Trxm3 ) had a lower content of chlorophylls and their metabolites in relation to the wild-type plants [ 38 ].…”

Section: Discussionmentioning

confidence: 99%

“…Thioredoxins are localized at different cellular compartments (e.g., chloroplasts, mitochondria, peroxisomes, nucleus, cytosol, plasma membrane, extracellular matrix) and they may be classified into several groups: trx f -, h -, m -, o -, x -, y -, and z -type) [ 3 , 4 , 5 ]. A wide range of trx isoforms enables integration of genes’ expression and metabolic pathways, regulation variety of physiological processes (e.g., flowering, seed germination, seedling growth) as well as stress tolerance and defense responses to environmental stimuli [ 3 , 6 , 7 ]. The oxidized thioredoxins may undergo a reversible reduction reaction catalyzed by thioredoxin reductases (TrxRs).…”

Section: Introductionmentioning

confidence: 99%

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Expression of Thioredoxin/Thioredoxin Reductase System Genes in Aphid-Challenged Maize Seedlings

Sytykiewicz

Łukasik

Goławska

et al. 2020

IJMS

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Thioredoxins (Trxs) and thioredoxin reductases (TrxRs) encompass a highly complex network involved in sustaining thiol-based redox homeostasis in plant tissues. The purpose of the study was to gain a new insight into transcriptional reprogramming of the several genes involved in functioning of Trx/TrxR system in maize (Zea mays L.) seedlings, exposed to the bird cherry-oat aphid (Rhopalosiphum padi L.) or the rose-grass aphid (Metopolophium dirhodum Walk.) infestation. The biotests were performed on two maize genotypes (susceptible Złota Karłowa and relatively resistant Waza). The application of real-time qRT-PCR technique allowed to identify a molecular mechanism triggered in more resistant maize plants, linked to upregulation of thioredoxins-encoding genes (Trx-f, Trx-h, Trx-m, Trx-x) and thioredoxin reductase genes (Ftr1, Trxr2). Significant enhancement of TrxR activity in aphid-infested Waza seedlings was also demonstrated. Furthermore, we used an electrical penetration graph (EPG) recordings of M. dirhodum stylet activities in seedlings of the two studied maize varieties. Duration of phloem phase (E1 and E2 models) of rose-grass aphids was about three times longer while feeding in Waza plants, compared to Złota Karłowa cv. The role of activation of Trx/TrxR system in maintaining redox balance and counteracting oxidative-induced damages of macromolecules in aphid-stressed maize plants is discussed.

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Redox‐control of chlorophyll biosynthesis mainly depends on thioredoxins

Cited by 25 publications

References 15 publications

Chloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darkness

Chloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darkness

Towards Initial Indications for a Thiol-Based Redox Control of Arabidopsis 5-Aminolevulinic Acid Dehydratase

Expression of Thioredoxin/Thioredoxin Reductase System Genes in Aphid-Challenged Maize Seedlings

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