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Antioxidants
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Redox in Plants
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Redox in Plants

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "ROS, RNS and RSS".

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 25338

Special Issue Editors

Prof. Dr. María Cruz González

E-Mail Website1 Website2
Guest Editor
Institute of Plant Biochemistry and Photosynthesis, University of Seville and Spanish National Research Council (Consejo Superior de Investigaciones Científicas- CSIC), Avda. Americo Vespucio 49, 41092-Sevilla, Spain
Interests: redox signalling in plants; redox regulation; NADPH thioredoxin reductase C (NTRC); thioredoxins; chloroplast morphology; transmision and scanning electron microcroscopy; proteomics; carbohydrate metabolism; redox sensors
Prof. Dr. Antonio Jesús Serrato

E-Mail Website
Guest Editor
Estación Experimental del Zaidín-CSIC, Granada, Spain
Interests: thioredoxins; redox regulation; fructose-1,6-bisphosphatase; carbohydrate metabolism; disulphide; photosynthesis

Special Issue Information

Dear Colleagues,

Although redox regulation is not restricted to plants, but present in all kingdoms of life, the sessile nature of plants results in a heightening of this regulation. The exposition to an ever-changing environment requires a dynamic adaptation in plant metabolism. Changes in light intensity, temperature, and water availability result in the generation of reactive oxygen or nitrogen species (ROS/RNS) in mitochondria and especially in the chloroplast, leading to stress situations or even cell death. That is, depending on their concentration, ROS/RNS can either play a signaling role or be cell-damaging. The importance of redox regulation in plants is reflected by the diversity of mechanisms controlling ROS/RNS levels, including both non-enzymatic and enzymatic antioxidant systems, as well as the existence of redox signaling pathways adapted to their life styles. The regulation of a great number of metabolic reactions in plants is based on dithiol-disulphide exchange, relying on proteins as thioredoxins and glutaredoxins, which reduce and consequently activate redox-sensitive proteins in the chloroplast under illumination. Moreover, some thioredoxins act as oxidants under darkness conditions. Although, as mentioned, redox regulation is key in organelles such as the chloroplast or mitochondria, plant cells have developed efficient redox-sensing mechanisms which are present in all subcellular compartments. In fact, a connection between chloroplast metabolism and mitochondrial ROS production through malate circulation and chloroplast to cytosol export of citrate under active photosynthesis has been proposed, reflecting the interplay between different organelles to maintain energy homeostasis in the cell.

The aim of this Special Issue on “Redox in Plants” is to gain more insight into plant redox processes, in the broadest sense, including sensing and signaling pathways, post-translational modifications, ROS/RNS scavenging or redox-based activity or gene expression regulation. In addition, novel redox methodologies focused on plant research will also be considered. Full review articles are also welcome.

Prof. Dr. María Cruz González
Prof. Dr. Antonio Jesús Serrato
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antioxidants is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Reactive oxygen and nitrogen species (ROS/RNS)
  • Thioredoxins
  • Oxidative stress
  • Antioxidant enzymes
  • Redox signaling
  • Redox sensing
  • Glutaredoxins
  • Retrograde signaling

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Published Papers (7 papers)

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Research

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24 pages, 3465 KiB  
Article
Autophagy Is Involved in the Viability of Overexpressing Thioredoxin o1 Tobacco BY-2 Cells under Oxidative Conditions
by Sabrina De Brasi-Velasco, Omar López-Vidal, María Carmen Martí, Ana Ortiz-Espín, Francisca Sevilla and Ana Jiménez
Antioxidants 2021, 10(12), 1884; https://doi.org/10.3390/antiox10121884 - 25 Nov 2021
Cited by 3 | Viewed by 2349
Abstract
Autophagy is an essential process for the degradation of non-useful components, although the mechanism involved in its regulation is less known in plants than in animal systems. Redox regulation of autophagy components is emerging as a possible key mechanism with thioredoxins (TRXs) proposed [...] Read more.
Autophagy is an essential process for the degradation of non-useful components, although the mechanism involved in its regulation is less known in plants than in animal systems. Redox regulation of autophagy components is emerging as a possible key mechanism with thioredoxins (TRXs) proposed as involved candidates. In this work, using overexpressing PsTRXo1 tobacco cells (OEX), which present higher viability than non-overexpressing cells after H2O2 treatment, we examine the functional interaction of autophagy and PsTRXo1 in a collaborative response. OEX cells present higher gene expression of the ATG (Autophagy related) marker ATG4 and higher protein content of ATG4, ATG8, and lipidated ATG8 as well as higher ATG4 activity than control cells, supporting the involvement of autophagy in their response to H2O2. In this oxidative situation, autophagy occurs in OEX cells as is evident from an accumulation of autolysosomes and ATG8 immunolocalization when the E-64d autophagy inhibitor is used. Interestingly, cell viability decreases in the presence of the inhibitor, pointing to autophagy as being involved in cell survival. The in vitro interaction of ATG4 and PsTRXo1 proteins is confirmed by dot-blot and co-immunoprecipitation assays as well as the redox regulation of ATG4 activity by PsTRXo1. These findings extend the role of TRXs in mediating the redox regulation of the autophagy process in plant cells. Full article
(This article belongs to the Special Issue Redox in Plants)
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28 pages, 2740 KiB  
Article
GSNOR Contributes to Demethylation and Expression of Transposable Elements and Stress-Responsive Genes
by Eva Esther Rudolf, Patrick Hüther, Ignasi Forné, Elisabeth Georgii, Yongtao Han, Rüdiger Hell, Markus Wirtz, Axel Imhof, Claude Becker, Jörg Durner and Christian Lindermayr
Antioxidants 2021, 10(7), 1128; https://doi.org/10.3390/antiox10071128 - 15 Jul 2021
Cited by 12 | Viewed by 3910
Abstract
In the past, reactive nitrogen species (RNS) were supposed to be stress-induced by-products of disturbed metabolism that cause oxidative damage to biomolecules. However, emerging evidence demonstrates a substantial role of RNS as endogenous signals in eukaryotes. In plants, S-nitrosoglutathione (GSNO) is the dominant [...] Read more.
In the past, reactive nitrogen species (RNS) were supposed to be stress-induced by-products of disturbed metabolism that cause oxidative damage to biomolecules. However, emerging evidence demonstrates a substantial role of RNS as endogenous signals in eukaryotes. In plants, S-nitrosoglutathione (GSNO) is the dominant RNS and serves as the •NO donor for S-nitrosation of diverse effector proteins. Remarkably, the endogenous GSNO level is tightly controlled by S-nitrosoglutathione reductase (GSNOR) that irreversibly inactivates the glutathione-bound NO to ammonium. Exogenous feeding of diverse RNS, including GSNO, affected chromatin accessibility and transcription of stress-related genes, but the triggering function of RNS on these regulatory processes remained elusive. Here, we show that GSNO reductase-deficient plants (gsnor1-3) accumulate S-adenosylmethionine (SAM), the principal methyl donor for methylation of DNA and histones. This SAM accumulation triggered a substantial increase in the methylation index (MI = [SAM]/[S-adenosylhomocysteine]), indicating the transmethylation activity and histone methylation status in higher eukaryotes. Indeed, a mass spectrometry-based global histone profiling approach demonstrated a significant global increase in H3K9me2, which was independently verified by immunological detection using a selective antibody. Since H3K9me2-modified regions tightly correlate with methylated DNA regions, we also determined the DNA methylation status of gsnor1-3 plants by whole-genome bisulfite sequencing. DNA methylation in the CG, CHG, and CHH contexts in gsnor1-3 was significantly enhanced compared to the wild type. We propose that GSNOR1 activity affects chromatin accessibility by controlling the transmethylation activity (MI) required for maintaining DNA methylation and the level of the repressive chromatin mark H3K9me2. Full article
(This article belongs to the Special Issue Redox in Plants)
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12 pages, 2151 KiB  
Article
NTRC Effects on Non-Photochemical Quenching Depends on PGR5
by Belen Naranjo, Jan-Ferdinand Penzler, Thilo Rühle and Dario Leister
Antioxidants 2021, 10(6), 900; https://doi.org/10.3390/antiox10060900 - 3 Jun 2021
Cited by 11 | Viewed by 3781
Abstract
Non-photochemical quenching (NPQ) protects plants from the detrimental effects of excess light. NPQ is rapidly induced by the trans-thylakoid proton gradient during photosynthesis, which in turn requires PGR5/PGRL1-dependent cyclic electron flow (CEF). Thus, Arabidopsis thaliana plants lacking either protein cannot induce transient NPQ [...] Read more.
Non-photochemical quenching (NPQ) protects plants from the detrimental effects of excess light. NPQ is rapidly induced by the trans-thylakoid proton gradient during photosynthesis, which in turn requires PGR5/PGRL1-dependent cyclic electron flow (CEF). Thus, Arabidopsis thaliana plants lacking either protein cannot induce transient NPQ and die under fluctuating light conditions. Conversely, the NADPH-dependent thioredoxin reductase C (NTRC) is required for efficient energy utilization and plant growth, and in its absence, transient and steady-state NPQ is drastically increased. How NTRC influences NPQ and functionally interacts with CEF is unclear. Therefore, we generated the A. thaliana line pgr5 ntrc, and found that the inactivation of PGR5 suppresses the high transient and steady-state NPQ and impaired growth phenotypes observed in the ntrc mutant under short-day conditions. This implies that NTRC negatively influences PGR5 activity and, accordingly, the lack of NTRC is associated with decreased levels of PGR5, possibly pointing to a mechanism to restrict upregulation of PGR5 activity in the absence of NTRC. When exposed to high light intensities, pgr5 ntrc plants display extremely impaired photosynthesis and growth, indicating additive effects of lack of both proteins. Taken together, these findings suggest that the interplay between NTRC and PGR5 is relevant for photoprotection and that NTRC might regulate PGR5 activity. Full article
(This article belongs to the Special Issue Redox in Plants)
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24 pages, 4305 KiB  
Article
Thioredoxin h2 and o1 Show Different Subcellular Localizations and Redox-Active Functions, and Are Extrachloroplastic Factors Influencing Photosynthetic Performance in Fluctuating Light
by Liang-Yu Hou, Martin Lehmann and Peter Geigenberger
Antioxidants 2021, 10(5), 705; https://doi.org/10.3390/antiox10050705 - 29 Apr 2021
Cited by 10 | Viewed by 3018
Abstract
Arabidopsis contains eight different h-type thioredoxins (Trx) being distributed in different cell organelles. Although Trx h2 is deemed to be confined to mitochondria, its subcellular localization and function are discussed controversially. Here, cell fractionation studies were used to clarify this question, [...] Read more.
Arabidopsis contains eight different h-type thioredoxins (Trx) being distributed in different cell organelles. Although Trx h2 is deemed to be confined to mitochondria, its subcellular localization and function are discussed controversially. Here, cell fractionation studies were used to clarify this question, showing Trx h2 protein to be exclusively localized in microsomes rather than mitochondria. Furthermore, Arabidopsis trxo1, trxh2 and trxo1h2 mutants were analyzed to compare the role of Trx h2 with mitochondrial Trx o1. Under medium light, trxo1 and trxo1h2 showed impaired growth, while trxh2 was similar to wild type. In line with this, trxo1 and trxo1h2 clustered differently from wild type with respect to nocturnal metabolite profiles, revealing a decrease in ascorbate and glutathione redox states. Under fluctuating light, these genotypic differences were attenuated. Instead, the trxo1h2 double mutant showed an improved NADPH redox balance, compared to wild type, accompanied by increased photosynthetic efficiency, specifically in the high-light phases. Conclusively, Trx h2 and Trx o1 are differentially localized in microsomes and mitochondria, respectively, which is associated with different redox-active functions and effects on plant growth in constant light, while there is a joint role of both Trxs in regulating NADPH redox balance and photosynthetic performance in fluctuating light. Full article
(This article belongs to the Special Issue Redox in Plants)
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20 pages, 3834 KiB  
Article
Crosstalk between Brassinosteroid and Redox Signaling Contributes to the Activation of CBF Expression during Cold Responses in Tomato
by Pingping Fang, Yu Wang, Mengqi Wang, Feng Wang, Cheng Chi, Yanhong Zhou, Jie Zhou, Kai Shi, Xiaojian Xia, Christine Helen Foyer and Jingquan Yu
Antioxidants 2021, 10(4), 509; https://doi.org/10.3390/antiox10040509 - 25 Mar 2021
Cited by 19 | Viewed by 3724
Abstract
Brassinosteroids (BRs) play a critical role in plant responses to stress. However, the interplay of BRs and reactive oxygen species signaling in cold stress responses remains unclear. Here, we demonstrate that a partial loss of function in the BR biosynthesis gene DWARF resulted [...] Read more.
Brassinosteroids (BRs) play a critical role in plant responses to stress. However, the interplay of BRs and reactive oxygen species signaling in cold stress responses remains unclear. Here, we demonstrate that a partial loss of function in the BR biosynthesis gene DWARF resulted in lower whilst overexpression of DWARF led to increased levels of C-REPEAT BINDING FACTOR (CBF) transcripts. Exposure to cold stress increased BR synthesis and led to an accumulation of brassinazole-resistant 1 (BZR1), a central component of BR signaling. Mutation of BZR1 compromised the cold- and BR-dependent increases in CBFs and RESPIRATORY BURST OXIDASE HOMOLOG 1(RBOH1) transcripts, as well as preventing hydrogen peroxide (H2O2) accumulation in the apoplast. Cold- and BR-induced BZR1 bound to the promoters of CBF1, CBF3 and RBOH1 and promoted their expression. Significantly, suppression of RBOH1 expression compromised cold- and BR-induced accumulation of BZR1 and related increases in CBF transcripts. Moreover, RBOH1-dependent H2O2 production regulated BZR1 accumulation and the levels of CBF transcripts by influencing glutathione homeostasis. Taken together, these results demonstrate that crosstalk between BZR1 and reactive oxygen species mediates cold- and BR-activated CBF expression, leading to cold tolerance in tomato (Solanum lycopersicum). Full article
(This article belongs to the Special Issue Redox in Plants)
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15 pages, 12813 KiB  
Article
Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis
by Fernanda Lazzarotto, Khadija Wahni, Maiara Piovesana, Felipe Maraschin, Joris Messens and Marcia Margis-Pinheiro
Antioxidants 2021, 10(1), 65; https://doi.org/10.3390/antiox10010065 - 7 Jan 2021
Cited by 14 | Viewed by 3534
Abstract
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide, thus minimizing cell injury and modulating signaling pathways as response to this reactive oxygen species. Using a phylogenetic approach, we previously identified a new peroxidase family composed of a small subset of ascorbate [...] Read more.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide, thus minimizing cell injury and modulating signaling pathways as response to this reactive oxygen species. Using a phylogenetic approach, we previously identified a new peroxidase family composed of a small subset of ascorbate peroxidase (APx) homologs with distinguished features, which we named ascorbate peroxidase-related (APx-R). In this study, we showed that APx-R is an ascorbate-independent heme peroxidase. Despite being annotated as a cytosolic protein in public databases, transient expression of AtAPx-R-YFP in Arabidopsis thaliana protoplasts and stable overexpression in plants showed that the protein is targeted to plastids. To characterize APx-R participation in the antioxidant metabolism, we analyzed loss-of-function mutants and AtAPx-R overexpressing lines. Molecular analysis showed that glutathione peroxidase 7 (GPx07) is specifically induced to compensate the absence of APx-R. APx-R overexpressing lines display faster germination rates, further confirming the involvement of APx-R in seed germination. The constitutive overexpression of AtAPx-R-YFP unraveled the existence of a post-translational mechanism that eliminates APx-R from most tissues, in a process coordinated with photomorphogenesis. Our results show a direct role of APx-R during germinative and post-germinative development associated with etioplasts differentiation. Full article
(This article belongs to the Special Issue Redox in Plants)
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Review

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17 pages, 1505 KiB  
Review
Current Knowledge on Mechanisms Preventing Photosynthesis Redox Imbalance in Plants
by María-Cruz González, Francisco Javier Cejudo, Mariam Sahrawy and Antonio Jesús Serrato
Antioxidants 2021, 10(11), 1789; https://doi.org/10.3390/antiox10111789 - 9 Nov 2021
Cited by 11 | Viewed by 3717
Abstract
Photosynthesis includes a set of redox reactions that are the source of reducing power and energy for the assimilation of inorganic carbon, nitrogen and sulphur, thus generating organic compounds, and oxygen, which supports life on Earth. As sessile organisms, plants have to face [...] Read more.
Photosynthesis includes a set of redox reactions that are the source of reducing power and energy for the assimilation of inorganic carbon, nitrogen and sulphur, thus generating organic compounds, and oxygen, which supports life on Earth. As sessile organisms, plants have to face continuous changes in environmental conditions and need to adjust the photosynthetic electron transport to prevent the accumulation of damaging oxygen by-products. The balance between photosynthetic cyclic and linear electron flows allows for the maintenance of a proper NADPH/ATP ratio that is adapted to the plant’s needs. In addition, different mechanisms to dissipate excess energy operate in plants to protect and optimise photosynthesis under adverse conditions. Recent reports show an important role of redox-based dithiol–disulphide interchanges, mediated both by classical and atypical chloroplast thioredoxins (TRXs), in the control of these photoprotective mechanisms. Moreover, membrane-anchored TRX-like proteins, such as HCF164, which transfer electrons from stromal TRXs to the thylakoid lumen, play a key role in the regulation of lumenal targets depending on the stromal redox poise. Interestingly, not all photoprotective players were reported to be under the control of TRXs. In this review, we discuss recent findings regarding the mechanisms that allow an appropriate electron flux to avoid the detrimental consequences of photosynthesis redox imbalances. Full article
(This article belongs to the Special Issue Redox in Plants)
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