The function of the NADPH thioredoxin reductase C‐2‐Cys peroxiredoxin system in plastid redox regulation and signalling

Cejudo, Francisco Javier; Ferrández, Julia; Cano, Beatriz; Puerto-Galán, Leonor; Guinea, Manuel

doi:10.1016/j.febslet.2012.07.003

Cited by 61 publications

(53 citation statements)

References 60 publications

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“…A key component of the rapid adjustment of chloroplast metabolism to ever-fluctuating light conditions is the redox regulation of enzyme activity, which relies on two thiol redox systems, the NADPHdependent NTRC and the Fdx-dependent FTR/Trx pathways (Spínola et al, 2008;Cejudo et al, 2012). Thus, a central issue in understanding chloroplast redox regulation is to establish the functional relationship between these two redox systems and the relevance of chloroplast redox regulation to plant development.…”

Section: Discussion Ntrc Acts In Concert With Different Types Of Trxsmentioning

confidence: 99%

NADPH Thioredoxin Reductase C and Thioredoxins Act Concertedly in Seedling Development

et al. 2017

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ORCID IDs: 0000-0001-8141-9679 (M.G.); 0000-0002-9570-9746 (A.J.S.); 0000-0001-9512-349X (P.G.); 0000-0002-3936-5491 (F.J.C.).Thiol-dependent redox regulation of enzyme activity plays a central role in the rapid acclimation of chloroplast metabolism to ever-fluctuating light availability. This regulatory mechanism relies on ferredoxin reduced by the photosynthetic electron transport chain, which fuels reducing power to thioredoxins (Trxs) via a ferredoxin-dependent Trx reductase. In addition, chloroplasts harbor an NADPH-dependent Trx reductase, which has a joint Trx domain at the carboxyl terminus, termed NTRC. Thus, a relevant issue concerning chloroplast function is to establish the relationship between these two redox systems and its impact on plant development. To address this issue, we generated Arabidopsis (Arabidopsis thaliana) mutants combining the deficiency of NTRC with those of Trxs f, which participate in metabolic redox regulation, and that of Trx x, which has antioxidant function. The ntrc-trxf1f2 and, to a lower extent, ntrc-trxx mutants showed severe growth-retarded phenotypes, decreased photosynthesis performance, and almost abolished light-dependent reduction of fructose-1,6-bisphosphatase. Moreover, the combined deficiency of both redox systems provokes aberrant chloroplast ultrastructure. Remarkably, both the ntrc-trxf1f2 and ntrc-trxx mutants showed high mortality at the seedling stage, which was overcome by the addition of an exogenous carbon source. Based on these results, we propose that NTRC plays a pivotal role in chloroplast redox regulation, being necessary for the activity of diverse Trxs with unrelated functions. The interaction between the two thiol redox systems is indispensable to sustain photosynthesis performed by cotyledons chloroplasts, which is essential for early plant development.

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Section: Discussion Ntrc Acts In Concert With Different Types Of Trxsmentioning

confidence: 99%

NADPH Thioredoxin Reductase C and Thioredoxins Act Concertedly in Seedling Development

et al. 2017

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“…Plants and some algae possess an additional NTR enzyme, called NTRC, which contains a small-type NTR domain at the N-terminus and a Trx domain at the C-terminus (Serrato et al 2004). Previous studies demonstrated that NTRs play an essential role in various biological processes such as stress tolerance, development, and metabolism including the biosynthesis of starch and chlorophyll (Cha et al 2014;Reichheld et al 2007;Cejudo et al 2012).…”

Section: The Thioredoxin Superfamily Proteinsmentioning

confidence: 99%

Biochemistry and Physiology of Reactive Oxygen Species in Euglena

Ishikawa¹,

Tamaki²,

Maruta³

et al. 2017

Advances in Experimental Medicine and Biology

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Reactive oxygen species (ROS) such as superoxide and hydrogen peroxide are by-products of various metabolic processes in aerobic organisms including Euglena. Chloroplasts and mitochondria are the main sites of ROS generation by photosynthesis and respiration, respectively, through the active electron transport chain. An efficient antioxidant network is required to maintain intracellular ROS pools at optimal conditions for redox homeostasis. A comparison with the networks of plants and animals revealed that Euglena has acquired some aspects of ROS metabolic process. Euglena lacks catalase and a typical selenocysteine containing animal-type glutathione peroxidase for hydrogen peroxide scavenging, but contains enzymes involved in ascorbate-glutathione cycle solely in the cytosol. Ascorbate peroxidase in Euglena, which plays a central role in the ascorbate-glutathione cycle, forms a unique intra-molecular dimer structure that is related to the recognition of peroxides. We recently identified peroxiredoxin and NADPH-dependent thioredoxin reductase isoforms in cellular compartments including chloroplasts and mitochondria, indicating the physiological significance of the thioredoxin system in metabolism of ROS. Besides glutathione, Euglena contains the unusual thiol compound trypanothione, an unusual form of glutathione involving two molecules of glutathione joined by a spermidine linker, which has been identified in pathogenic protists such as Trypanosomatida and Schizopyrenida. Furthermore, in contrast to plants, photosynthesis by Euglena is not susceptible to hydrogen peroxide because of resistance of the Calvin cycle enzymes fructose-1,6-bisphosphatse, NADP-glyceraldehyde-3-phosphatase, sedoheptulose-1,7-bisphosphatase, and phosphoribulokinase to hydrogen peroxide. Consequently, these characteristics of Euglena appear to exemplify a strategy for survival and adaptation to various environmental conditions during the evolutionary process of euglenoids.

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“…12 Compared to typical NTRA and NTRB, NTRC has been largely identified from biochemical reactions to physiological functions in Arabidopsis. 13 Loss-of function NTRC mutant in Arabidopsis showed obvious pale-green leaves and dwarf phenotypes due to defects of chloroplast biogenesis and auxin levels, respectively.…”

Section: Stress Defense Mechanisms Of Nadph-dependent Thioredoxin Redmentioning

confidence: 99%

“…Furthermore, electrons from NADPH produced in chloroplast transfer to 2Cys Prx via redox-active cysteins in TrxR and Trx domain in NTRC. 13,16,17 However, cytosolic NTRA and mitochondrial NTRB are acquired to cooperate with their relevant Trx counterparts. NTRA and NTRB also share redundant function in cytosol and mitochondria both in vitro and in vivo.…”

Section: Stress Defense Mechanisms Of Nadph-dependent Thioredoxin Redmentioning

confidence: 99%

Stress defense mechanisms of NADPH-dependent thioredoxin reductases (NTRs) in plants

Cha

Barman

Kim

et al. 2015

Plant Signaling & Behavior

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The function of the NADPH thioredoxin reductase C‐2‐Cys peroxiredoxin system in plastid redox regulation and signalling

Cited by 61 publications

References 60 publications

NADPH Thioredoxin Reductase C and Thioredoxins Act Concertedly in Seedling Development

NADPH Thioredoxin Reductase C and Thioredoxins Act Concertedly in Seedling Development

Biochemistry and Physiology of Reactive Oxygen Species in Euglena

Stress defense mechanisms of NADPH-dependent thioredoxin reductases (NTRs) in plants

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