The Role of Glutathione in Photosynthetic Organisms: Emerging Functions for Glutaredoxins and Glutathionylation

Rouhier, Nicolas; Lemaire, Stéphane D.; Jacquot, Jean‐Pierre

doi:10.1146/annurev.arplant.59.032607.092811

Cited by 495 publications

(375 citation statements)

References 113 publications

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“…A comparison of the transcript profiles of Arabidopsis cell at stages in the cell cycle where GSH was predominantly localised in the nuclei compared to when GSH was compartmentalised evenly between the cytosol and nucleus revealed that defence-related transcripts were less abundant at times when the nuclear GSH pool was larger than that of the cytosol (9,10). This finding is in agreement with the results of other studies showing that cytosolic GSH pool is important in transducing oxidative signals linked to hormone-dependent defences against biotic and abiotic stresses (11-13; 37, 116).…”

Section: The Nuclear Glutathione Poolmentioning

confidence: 99%

“…It is rather surprising therefore that the nuclear GSH pool is much more resistant to depletion than the cytosolic pool, a property that is particularly important during cell proliferation (5)(6)(7)(8). Although relatively little is known about the nuclear thioredoxins (TRX) and glutaredoxins (GRXs) or their functions in plants (9) it is probable that these redox proteins participate in the plethora of thiol-dependent redox regulation mechanisms and post-translational modifications that are required for plant growth and development, particularly through functions in the nuclei.The many important roles of glutathione in plants have been well documented in recent reviews (1,2,10) and hence the following discussion will focus on how GSH functions as a regulator of plant development, with a particular focus on the nuclear GSH and the regulation of mitosis.…”

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confidence: 99%

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Glutathione – linking cell proliferation to oxidative stress

Díaz‐Vivancos

Simone

Kiddle³

et al. 2015

Free Radical Biology and Medicine

255

158

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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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Section: The Nuclear Glutathione Poolmentioning

confidence: 99%

mentioning

confidence: 99%

Glutathione – linking cell proliferation to oxidative stress

Díaz‐Vivancos

Simone

Kiddle³

et al. 2015

Free Radical Biology and Medicine

255

158

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“…Besides TRX-dependent regulation of the redox state of protein disulfide bonds, glutathionylation has recently emerged, among other thiol-based post-translational modifications, as an important redox-based signaling mechanism (3)(4)(5). This modification consists in the formation of a mixed disulfide between an accessible free thiol on a protein and a molecule of glutathione.…”

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confidence: 99%

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

Bedhomme

Zaffagnini

Marchand

et al. 2009

Journal of Biological Chemistry

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Post-translational modification of protein cysteine residues is emerging as an important regulatory and signaling mechanism. We have identified numerous putative targets of redox regulation in the unicellular green alga Chlamydomonas reinhardtii. One enzyme, isocitrate lyase (ICL), was identified both as a putative thioredoxin target and as an S-thiolated protein in vivo. ICL is a key enzyme of the glyoxylate cycle that allows growth on acetate as a sole source of carbon. The aim of the present study was to clarify the molecular mechanism of the redox regulation of Chlamydomonas ICL using a combination of biochemical and biophysical methods. The results clearly show that purified C. reinhardtii ICL can be inactivated by glutathionylation and reactivated by glutaredoxin, whereas thioredoxin does not appear to regulate ICL activity, and no inter-or intramolecular disulfide bond could be formed under any of the conditions tested. Glutathionylation of the protein was investigated by mass spectrometry analysis, Western blotting, and site-directed mutagenesis. The enzyme was found to be protected from irreversible oxidative inactivation by glutathionylation of its catalytic Cys 178 , whereas a second residue, Cys 247 , becomes artifactually glutathionylated after prolonged incubation with GSSG. The possible functional significance of this post-translational modification of ICL in Chlamydomonas and other organisms is discussed.

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“…Glutathione (GSH) plays an important role in the heavy metal detoxification mechanism of plants [4]. GSH is a ubiquitous molecule with several roles in cell metabolism, including reactive oxygen species processing, redox state regulation, transport of amino acids, and sulfur storage [5], [6]. A function of GSH could be the chelation of toxic Cd (II) ions during their transport through the cytoplasm [7].…”

Section: Introductionmentioning

confidence: 99%

Cu and Cd induced Cytotoxicity Involving Lipid Peroxidation and Sulfhydryl Compounds in the Hyperaccumulator and Nonaccumulator Varieties of Commelina Communis

Hai-ou¹

2013

IJESD

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Abstract-The ability to accumulate Cu and Cd was investigated in Cu hyperaccumulator and nonaccumulator varieties of Commelina communis. Furthermore, the role of malondialdehyde (MDA), glutathione (GSH), and phytochelatin (PC) in the detoxification mechanisms used by the hyperaccumulator C. communis to cope with heavy metals were investigated. Results showed that Cu and Cd contents of both leaves and roots in the hyperaccumulator were higher than those in the nonaccumulator. However, the hyperaccumulator variety could have a more powerful ability to transport Cu and Cd from roots to shoots, thus decreasing the toxicity risk. Meanwhile, the MDA, GSH, and PC contents in the hyperaccumulator were significantly lower than those in the nonaccumulator under Cu and Cd stress, indicating that the former can utilize these sulfhydryl compounds to reduce toxicity caused by metal ions. Thus, the hyperaccumulator can tolerate heavy metal-induced toxicity better than the nonaccumulator.Index Terms-Heavy metals, malondialdehyde, glutathione, phytochelatin. I. INTRODUCTIONCu is an essential micronutrient for plants, a component of several electron transport enzymes, and is involved in catalyzing redox reactions in mitochondria and chloroplasts [1]. However, Cu also induces toxicity at tissue concentrations slightly above its optimal levels [2]. It can produce a mass of reactive oxygen species, damage cell membranes, and accumulate peroxide [3]. Glutathione (GSH) plays an important role in the heavy metal detoxification mechanism of plants [4]. GSH is a ubiquitous molecule with several roles in cell metabolism, including reactive oxygen species processing, redox state regulation, transport of amino acids, and sulfur storage [5], [6]. A function of GSH could be the chelation of toxic Cd (II) ions during their transport through the cytoplasm [7]. GSH is also used to synthesize phytochelatin (PC) [8]- [10]. Numerous physiological studies have indicated that the roles of PC include heavy metal detoxification [11] and maintenance of the homeostasis of intracellular levels of essential metal ions [12]. Malondialdehyde (MDA) is often used as an indicator of Manuscript received January 14, 2013; revised March 14, 2013 Commelina communis is commonly known in China as an annual multibranched herb with erect stems in its upper part and creeping stems in its lower part. Many studies have been performed to illustrate the hyperaccumulating mechanism of the hyperaccumulator variety of C. communis. Reports that describe the reaction of MDA, GSH, and PC to Cu, however, number much less. Moreover, scholars widely hypothesize that the hyperaccumulator can accumulate more than one kind of heavy metal. As such, two of varieties of C. communis were studied in our experiment as to whether or not they could also accumulate Cd in addition to Cu. The movement of MDA, GSH, and PC in the two varieties was further investigated under Cu-and Cd-induced stress. The study is an attempt to understand the mechanism by which the hyperaccumulator variety can tolera...

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The Role of Glutathione in Photosynthetic Organisms: Emerging Functions for Glutaredoxins and Glutathionylation

Cited by 495 publications

References 113 publications

Glutathione – linking cell proliferation to oxidative stress

Glutathione – linking cell proliferation to oxidative stress

Regulation by Glutathionylation of Isocitrate Lyase from Chlamydomonas reinhardtii

Cu and Cd induced Cytotoxicity Involving Lipid Peroxidation and Sulfhydryl Compounds in the Hyperaccumulator and Nonaccumulator Varieties of Commelina Communis

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