Interplay between the NADP-Linked Thioredoxin and Glutathione Systems in <i>Arabidopsis</i> Auxin Signaling

Bashandy, Talaat; Guilleminot, Jocelyne; Vernoux, Teva; Caparrós-Ruiz, David; Ljung, Karin; Meyer, Yves; Reichheld, Jean‐Philippe

doi:10.1105/tpc.109.071225

Cited by 284 publications

(282 citation statements)

References 73 publications

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“…The CC-type class expanded exclusively and strongly during the evolution of land plants, suggesting that this class of GRXs might have been recruited to participate in the evolution of more complex land plants (Xing et al, 2006;Ziemann et al, 2009). Contrasting with wide-ranging roles of plant thioredoxins in chloroplast and mitochondrial processes, seed development and germination, and auxin signaling (Buchanan and Balmer, 2005;Reichheld et al, 2007;Arsova et al, 2010;Bashandy et al, 2010), the biological and physiological functions of plant GRXs have remained largely elusive. Recently, two CC-type GRX genes, ROXY1 and ROXY2, were functionally characterized, revealing their functions during Arabidopsis flower development Xing and Zachgo, 2008;).…”

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confidence: 99%

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Gutsche

Zachgo

2011

Plant Physiology

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Glutaredoxins (GRXs) are small, ubiquitous, glutathione-dependent oxidoreductases that participate in redox-regulated processes associated with stress responses. Recently, GRXs have been shown to exert crucial functions during flower developmental processes. GRXs modulate their target protein activities by the reduction of protein disulfide bonds or deglutathionylation reactions. The Arabidopsis (Arabidopsis thaliana) GRX ROXY1 participates in petal primordia initiation and further petal morphogenesis. ROXY1 belongs to a land plant-specific class of GRXs with a CC-type active site motif, deviating from the ubiquitously occurring CPYC and CGFS GRX classes. ROXY1 was previously shown to interact with floral TGA transcription factors in the nucleus, and this interaction is a prerequisite for ROXY1 to exert its activity required for Arabidopsis petal development. Deletion analysis further identified the importance of the ROXY1 C terminus for the ROXY1/ TGA protein interactions and for the ROXY1 function in petal development. Here, by dissecting the ROXY1 C terminus, an a-helical L**LL motif immediately adjacent to the ROXY1 C-terminal eight amino acids was identified that is essential for the interaction with TGA transcription factors and crucial for the ROXY1 function in planta. Similar to the a-helical L**LL motifs binding to transcriptional coactivators with liganded nuclear receptors in animals, a hydrophobic face formed by the conserved leucines in the L**LL motif of ROXY1 possibly mediates the interaction with TGA transcription factors. Thus, the a-helical L**LL sequence is a conserved protein-protein interaction motif in both animals and plants. Furthermore, two separate TGA domains were identified by deletion experiments as being essential for mediating TGA protein interactions with ROXYs.

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confidence: 99%

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Gutsche

Zachgo

2011

Plant Physiology

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“…Translatome analysis also exposed that ABA, auxin and jasmonic acid (JA) biosynthesis, and signaling genes were activated during GSH treatment (Cheng et al 2015). A direct link between cellular redox status and auxin signaling has been reported during characterization of a triple mutant of Arabidopsis (Bashandy et al 2010). The GST and GPX activities were higher in the auxin autotrophic tobacco callus lines which were suggested to enhance salt stress (100 mmol/L NaCl) tolerance.…”

Section: Glutathione-induced Abiotic Stress Tolerance Salinitymentioning

confidence: 92%

Glutathione in plants: biosynthesis and physiological role in environmental stress tolerance

Hasanuzzaman

Nahar

Anee

et al. 2017

Physiol Mol Biol Plants

588

284

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Glutathione (GSH; c-glutamyl-cysteinyl-glycine) is a small intracellular thiol molecule which is considered as a strong non-enzymatic antioxidant. Glutathione regulates multiple metabolic functions; for example, it protects membranes by maintaining the reduced state of both a-tocopherol and zeaxanthin, it prevents the oxidative denaturation of proteins under stress conditions by protecting their thiol groups, and it serves as a substrate for both glutathione peroxidase and glutathione S-transferase. By acting as a precursor of phytochelatins, GSH helps in the chelating of toxic metals/metalloids which are then transported and sequestered in the vacuole. The glyoxalase pathway (consisting of glyoxalase I and glyoxalase II enzymes) for detoxification of methylglyoxal, a cytotoxic molecule, also requires GSH in the first reaction step. For these reasons, much attention has recently been directed to elucidation of the role of this molecule in conferring tolerance to abiotic stress. Recently, this molecule has drawn much attention because of its interaction with other signaling molecules and phytohormones. In this review, we have discussed the recent progress in GSH biosynthesis, metabolism and its role in abiotic stress tolerance.

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“…In contrast to roots, TRX able to replace GSH functions in the control shoot development (50,51). Studies on Arabidopsis cad2-1 ntra ntrb triple mutants that lack both functional cytosolic NADPH-THIOREDOXIN REDUCTASES (ntra,ntrbmutants) and have a decreased capacity for GSH synthesis (cad2-1) were found to grow in a similar manner to the wild type throughout vegetative development (51).…”

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confidence: 99%

“…Studies on Arabidopsis cad2-1 ntra ntrb triple mutants that lack both functional cytosolic NADPH-THIOREDOXIN REDUCTASES (ntra,ntrbmutants) and have a decreased capacity for GSH synthesis (cad2-1) were found to grow in a similar manner to the wild type throughout vegetative development (51). However, they were unable to sustain normal floral meristem development, producing instead a PIN- Moreover, the BSO-triggered inhibition of root growth is accompanied by a decreased expression of PIN proteins (46).…”

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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

274

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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Interplay between the NADP-Linked Thioredoxin and Glutathione Systems in Arabidopsis Auxin Signaling

Cited by 284 publications

References 73 publications

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

The ROXY1 C-Terminal L**LL Motif Is Essential for the Interaction with TGA Transcription Factors

Glutathione in plants: biosynthesis and physiological role in environmental stress tolerance

Glutathione – linking cell proliferation to oxidative stress

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