Cysteine–based redox regulation and signaling in plants

Couturier, Jérémy; Chibani, Kamel; Jacquot, Jean‐Pierre; Rouhier, Nicolas

doi:10.3389/fpls.2013.00105

Cited by 122 publications

(90 citation statements)

References 57 publications

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“…Cys2 in ERF-VII TFs is a regulatory Cys (Formenko et al, 2010;Couturier et al, 2013). Its thiol group is highly susceptible to oxidation (Reddie and Carroll, 2008) by oxygen, ROS, and reactive nitrogen species, and it can be used in a variety of redox reactions (Giles et al, 2003) and can undergo additional enzymatic modifications, such as S-acylation and N-acetylation (Polevoda and Sherman, 2003;Hwang et al, 2010).…”

Section: N-terminal Cys Modificationsmentioning

confidence: 99%

Group VII Ethylene Response Factors in Arabidopsis: Regulation and Physiological Roles

Giuntoli

Perata

2017

Plant Physiol.

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Section: N-terminal Cys Modificationsmentioning

confidence: 99%

Group VII Ethylene Response Factors in Arabidopsis: Regulation and Physiological Roles

Giuntoli

Perata

2017

Plant Physiol.

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“…This process is relatively well characterised in relation to function in animals but remains poorly characterised in plants, often because of technological challenges (21). Since GSH is the most abundant low molecular weight thiol in plant cells (22,23), glutathionylation has the potential to be a major form of S-thiolation-dependent regulation (21).…”

mentioning

confidence: 99%

Glutathione – linking cell proliferation to oxidative stress

Díaz‐Vivancos

Simone

Kiddle³

et al. 2015

Free Radical Biology and Medicine

278

177

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Significance:The multifaceted functions of reduced glutathione (gamma-glutamyl-cysteinyl-glycine; GSH) continue to fascinate plants and animal scientists, not least because of the dynamic relationships between GSH and reactive oxygen species (ROS) that underpin reduction/oxidation (redox) regulation and signalling. Here we consider the respective roles of ROS and GSH in the regulation of plant growth, with a particular focus on regulation of the plant cell cycle. Glutathione is discussed not only as a crucial low molecular weight redox buffer that shields nuclear processes against oxidative challenge but also a flexible regulator of genetic and epigenetic functions. Recent Advances:The intracellular compartmentalization of GSH during the cell cycle is remarkably consistent in plants and animals. Moreover, measurements of in vivo glutathione redox potentials reveal that the cellular environment is much more reducing than predicted from GSH/GSSG ratios measured in tissue extracts. The redox potential of the cytosol and nuclei of non-dividing plant cells is about -300 mV. This relatively low redox potential is maintained even in cells experiencing oxidative stress by a number of mechanisms including vacuolar sequestration of GSSG. We propose that regulated ROS production linked to glutathione-mediated signalling events are the hallmark of viable cells within a changing and challenging environment. Critical Issues:The concept that the cell cycle in animals is subject to redox controls is well established but little is known about how ROS and GSH regulate this process in plants. However, it is increasingly likely that similar redox controls exist in plants, 3 although possibly through different pathways. Moreover, redox-regulated proteins that function in cell cycle checkpoints remain to be identified in plants. While GSHresponsive genes have now been identified, the mechanisms that mediate and regulate protein glutathionylation in plants remain poorly defined.Future Directions: The nuclear GSH pool provides an appropriate redox environment for essential nuclear functions. Future work will function on how this essential thiol interacts with the nuclear thioredoxin system and nitric oxide to regulate genetic and epigenetic mechanisms. The characterization of redox-regulated cell cycle proteins in plants, and the elucidation of mechanisms that facilitate GSH accumulation in the nucleus are keep steps to unravelling the complexities of nuclear redox controls.Diaz 4

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“…To fulfill these functions, chloroplast metabolism needs to adjust rapidly to unpredictable changes of light availability. In this regard, the thiol-dependent redox regulation of enzyme activity plays a relevant role (Couturier et al, 2013;Balsera et al, 2014), the disulfide reductase activity of thioredoxins (Trxs) being central for this regulatory mechanism (Meyer et al, 2012;Serrato et al, 2013).…”

mentioning

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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Cysteine–based redox regulation and signaling in plants

Cited by 122 publications

References 57 publications

Group VII Ethylene Response Factors in Arabidopsis: Regulation and Physiological Roles

Group VII Ethylene Response Factors in Arabidopsis: Regulation and Physiological Roles

Glutathione – linking cell proliferation to oxidative stress

NADPH Thioredoxin Reductase C and Thioredoxins Act Concertedly in Seedling Development

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