GSH Partitioning Between the Nucleus and Cytosol in Arabidopsis thaliana

Simone, Ambra De; Dong, Yingping; Vivancos, Pedro Diaz; Foyer, Christine H.

doi:10.1007/978-3-319-20137-5_4

Cited by 3 publications

(2 citation statements)

References 36 publications

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“…GSH co-localizes with nuclear DNA during cell proliferation in animals (8) and plants (5,6,96,107). In such studies, the nuclear GSH pool has been monitored largely by cconfocal microscopy using a double staining procedure involving Hoechst 33342 (Hoechst; blue stain) to localize nuclear DNA and CellTracker green 5-chloromethylfluorescein diacetate (CMFDA; green stain) to detect GSH (5,6,86,107).…”

Section: The Nuclear Glutathione Poolmentioning

confidence: 99%

Glutathione – linking cell proliferation to oxidative stress

Díaz‐Vivancos

Simone

Kiddle³

et al. 2015

Free Radical Biology and Medicine

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291

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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Section: The Nuclear Glutathione Poolmentioning

confidence: 99%

Glutathione – linking cell proliferation to oxidative stress

Díaz‐Vivancos

Simone

Kiddle³

et al. 2015

Free Radical Biology and Medicine

Self Cite

291

177

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“…The nuclear localization of various proteins coincides with the presence of redox systems for the respective thiol/disulfide exchange reactions thought to occur within the nucleus ( 36 ). Trx, glutaredoxins, and nucleoredoxins together with the NTRs, as well as the small thiol GSH, are localized in the cytosol and nucleus ( 35 , 114 , 115 , 159 ). The redoxins were found to bind to a large number of proteins in nuclear extracts, many of them with moonlighting functions ( e.g.…”

Section: Cellular Compartmentation Is Even More Complex Due To Metabolonsmentioning

confidence: 99%

Central Metabolism in Mammals and Plants as a Hub for Controlling Cell Fate

Selinski

Scheibe

2021

Antioxidants & Redox Signaling

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Significance: The importance of oxidoreductases in energy metabolism together with the occurrence of enzymes of central metabolism in the nucleus gave rise to the active research field aiming to understand moonlighting enzymes that undergo post-translational modifications (PTMs) before carrying out new tasks. Recent Advances: Cytosolic enzymes were shown to induce gene transcription after PTM and concomitant translocation to the nucleus. Changed properties of the oxidized forms of cytosolic glyceraldehyde 3-phosphate dehydrogenase, and also malate dehydrogenases and others, are the basis for a hypothesis suggesting moonlighting functions that directly link energy metabolism to adaptive responses required for maintenance of redox-homeostasis in all eukaryotes. Critical Issues: Small molecules, such as metabolic intermediates, coenzymes, or reduced glutathione, were shown to fine-tune the redox switches, interlinking redox state, metabolism, and induction of new functions via nuclear gene expression. The cytosol with its metabolic enzymes connecting energy fluxes between the various cell compartments can be seen as a hub for redox signaling, integrating the different signals for graded and directed responses in stressful situations. Future Directions: Enzymes of central metabolism were shown to interact with p53 or the assumed plant homologue suppressor of gamma response 1 (SOG1), an NAM, ATAF, and CUC transcription factor involved in the stress response upon ultraviolet exposure. Metabolic enzymes serve as sensors for imbalances, their inhibition leading to changed energy metabolism, and the adoption of transcriptional coactivator activities. Depending on the intensity of the impact, rerouting of energy metabolism, proliferation, DNA repair, cell cycle arrest, immune responses, or cell death will be induced. Antioxid. Redox Signal. 34, 1025–1047.

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