Thioredoxin and Glutaredoxin Systems II

A special issue of Antioxidants (ISSN 2076-3921).

Deadline for manuscript submissions: closed (20 July 2022) | Viewed by 26704

Special Issue Editors


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Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy
Interests: carbon metabolism; redox homeostasis; thiol-dependent post-transalational modifications
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
The Faculty of Sciences and Technologies, University of Lorraine, INRAE, IAM, F-54000 Nancy, France
Interests: sulfur trafficking; sulfurtransferase; cysteine desulfurase; rhodanese; protein persulfidation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Following the successful publication of volume 1 of the Special Issue “Thioredoxin and Glutaredoxin Systems”, we are now launching the second volume to collect updated data on the roles and mechanisms of action of these redox systems. In the first volume, a meaningful number of colleagues contributed both research papers (11) and review articles (5) covering redox-related topics ranging from structural, functional, and proteomic studies of thioredoxin/glutaredoxin (TRX/GRX) systems to the thiol-switching regulation of metabolic and antioxidant enzymes, and to the role of redox mechanisms in stress adaptation and development. 

The current understanding of the TRX and GRX systems has highlighted their role in controlling a wide variety of cellular processes by modulating the redox states of target proteins in all living organisms. Mounting evidence, however, has pointed out that the two systems have distinct roles, and their redox functions are rather specific and linked to reactive molecular species. Moreover, the known molecular mechanisms underlying their regulatory role are still limited to dozens of proteins, while several hundreds have been identified as potential targets. 

Therefore, we invite you to submit your research findings to this Special Issue, which aims to present updated data on new and established regulatory pathways involving TRX/GRX systems and their interconnections with other cysteine-dependent redox modifications that entail reactive oxygen, nitrogen and sulfur species (ROS, RNS and RSS, respectively). The research can include both in vitro and in vivo studies exploiting the structural/functional characterization of TRX/GRX and related targets, and the importance of redox mechanisms under cell growth and development but also in response to stress conditions in all living organisms. Original research articles and review articles are welcome.

Dr. Mirko Zaffagnini
Dr. Jeremy Couturier
Guest Editors

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Published Papers (12 papers)

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Research

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12 pages, 1814 KiB  
Article
Relationships between the Reversible Oxidation of the Single Cysteine Residue and the Physiological Function of the Mitochondrial Glutaredoxin S15 from Arabidopsis thaliana
by Loïck Christ, Jérémy Couturier and Nicolas Rouhier
Antioxidants 2023, 12(1), 102; https://doi.org/10.3390/antiox12010102 - 31 Dec 2022
Cited by 1 | Viewed by 1578
Abstract
Glutaredoxins (GRXs) are widespread proteins catalyzing deglutathionylation or glutathionylation reactions or serving for iron-sulfur (Fe-S) protein maturation. Previous studies highlighted a role of the Arabidopsis thaliana mitochondrial class II GRXS15 in Fe-S cluster assembly, whereas only a weak glutathione-dependent oxidation activity was detected [...] Read more.
Glutaredoxins (GRXs) are widespread proteins catalyzing deglutathionylation or glutathionylation reactions or serving for iron-sulfur (Fe-S) protein maturation. Previous studies highlighted a role of the Arabidopsis thaliana mitochondrial class II GRXS15 in Fe-S cluster assembly, whereas only a weak glutathione-dependent oxidation activity was detected with the non-physiological roGFP2 substrate in vitro. Still, the protein must exist in a reduced form for both redox and Fe-S cluster binding functions. Therefore, this study aimed at examining the redox properties of AtGRXS15. The acidic pKa of the sole cysteine present in AtGRXS15 indicates that it should be almost totally under a thiolate form at mitochondrial pH and thus possibly subject to oxidation. Oxidizing treatments revealed that this cysteine reacts with H2O2 or with oxidized glutathione forms. This leads to the formation of disulfide-bridge dimers and glutathionylated monomers which have redox midpoint potentials of −304 mV and −280 mV, respectively. Both oxidized forms are reduced by glutathione and mitochondrial thioredoxins. In conclusion, it appears that AtGRXS15 is prone to oxidation, forming reversible oxidation forms that may be seen either as a catalytic intermediate of the oxidoreductase activity and/or as a protective mechanism preventing irreversible oxidation and allowing Fe-S cluster binding upon reduction. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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22 pages, 2185 KiB  
Article
Analysis of Thioredoxins and Glutaredoxins in Soybean: Evidence of Translational Regulation under Water Restriction
by María Martha Sainz, Carla Valeria Filippi, Guillermo Eastman, José Sotelo-Silveira, Omar Borsani and Mariana Sotelo-Silveira
Antioxidants 2022, 11(8), 1622; https://doi.org/10.3390/antiox11081622 - 21 Aug 2022
Cited by 7 | Viewed by 1973 | Correction
Abstract
Soybean (Glycine max (L.) Merr.) establishes symbiosis with rhizobacteria, developing the symbiotic nodule, where the biological nitrogen fixation (BNF) occurs. The redox control is key for guaranteeing the establishment and correct function of the BNF process. Plants have many antioxidative systems involved [...] Read more.
Soybean (Glycine max (L.) Merr.) establishes symbiosis with rhizobacteria, developing the symbiotic nodule, where the biological nitrogen fixation (BNF) occurs. The redox control is key for guaranteeing the establishment and correct function of the BNF process. Plants have many antioxidative systems involved in ROS homeostasis and signaling, among them a network of thio- and glutaredoxins. Our group is particularly interested in studying the differential response of nodulated soybean plants to water-deficit stress. To shed light on this phenomenon, we set up an RNA-seq experiment (for total and polysome-associated mRNAs) with soybean roots comprising combined treatments including the hydric and the nodulation condition. Moreover, we performed the initial identification and description of the complete repertoire of thioredoxins (Trx) and glutaredoxins (Grx) in soybean. We found that water deficit altered the expression of a greater number of differentially expressed genes (DEGs) than the condition of plant nodulation. Among them, we identified 12 thioredoxin (Trx) and 12 glutaredoxin (Grx) DEGs, which represented a significant fraction of the detected GmTrx and GmGrx in our RNA-seq data. Moreover, we identified an enriched network in which a GmTrx and a GmGrx interacted with each other and associated through several types of interactions with nitrogen metabolism enzymes. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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17 pages, 27021 KiB  
Article
Comprehensive Expression Analyses of Plastidial Thioredoxins of Arabidopsis thaliana Indicate a Main Role of Thioredoxin m2 in Roots
by Mariam Sahrawy, Juan Fernández-Trijueque, Paola Vargas and Antonio J. Serrato
Antioxidants 2022, 11(7), 1365; https://doi.org/10.3390/antiox11071365 - 14 Jul 2022
Cited by 4 | Viewed by 1819
Abstract
Thioredoxins (TRXs) f and m are redox proteins that regulate key chloroplast processes. The existence of several isoforms of TRXs f and m indicates that these redox players have followed a specialization process throughout evolution. Current research efforts are focused on discerning the [...] Read more.
Thioredoxins (TRXs) f and m are redox proteins that regulate key chloroplast processes. The existence of several isoforms of TRXs f and m indicates that these redox players have followed a specialization process throughout evolution. Current research efforts are focused on discerning the signalling role of the different TRX types and their isoforms in chloroplasts. Nonetheless, little is known about their function in non-photosynthetic plastids. For this purpose, we have carried out comprehensive expression analyses by using Arabidopsis thaliana TRXf (f1 and f2) and TRXm (m1, m2, m3 and m4) genes translationally fused to the green fluorescence protein (GFP). These analyses showed that TRX m has different localisation patterns inside chloroplasts, together with a putative dual subcellular localisation of TRX f1. Apart from mesophyll cells, these TRXs were also observed in reproductive organs, stomatal guard cells and roots. We also investigated whether photosynthesis, stomatal density and aperture or root structure were affected in the TRXs f and m loss-of-function Arabidopsis mutants. Remarkably, we immunodetected TRX m2 and the Calvin–Benson cycle fructose-1,6-bisphosphatase (cFBP1) in roots. After carrying out in vitro redox activation assays of cFBP1 by plastid TRXs, we propose that cFBP1 might be activated by TRX m2 in root plastids. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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21 pages, 4920 KiB  
Article
Deciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO
by Vitor S. Almeida, Lara L. Miller, João P. G. Delia, Augusto V. Magalhães, Icaro P. Caruso, Anwar Iqbal and Fabio C. L. Almeida
Antioxidants 2022, 11(7), 1236; https://doi.org/10.3390/antiox11071236 - 24 Jun 2022
Cited by 1 | Viewed by 1467
Abstract
Nitric oxide (NO) is a free radical with a signaling capacity. Its cellular functions are achieved mainly through S-nitrosation where thioredoxin (hTrx) is pivotal in the S-transnitrosation to specific cellular targets. In this study, we use NMR spectroscopy and mass spectrometry to follow [...] Read more.
Nitric oxide (NO) is a free radical with a signaling capacity. Its cellular functions are achieved mainly through S-nitrosation where thioredoxin (hTrx) is pivotal in the S-transnitrosation to specific cellular targets. In this study, we use NMR spectroscopy and mass spectrometry to follow the mechanism of S-(trans)nitrosation of hTrx. We describe a site-specific path for S-nitrosation by measuring the reactivity of each of the 5 cysteines of hTrx using cysteine mutants. We showed the interdependence of the three cysteines in the nitrosative site. C73 is the most reactive and is responsible for all S-transnitrosation to other cellular targets. We observed NO internal transfers leading to C62 S-nitrosation, which serves as a storage site for NO. C69-SNO only forms under nitrosative stress, leading to hTrx nuclear translocation. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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15 pages, 4369 KiB  
Article
Thioredoxin-1 Ameliorates Oxygen-Induced Retinopathy in Newborn Mice through Modulation of Proinflammatory and Angiogenic Factors
by Junichi Ozawa, Kosuke Tanaka, Yukio Arai, Mitsuhiro Haga, Naoyuki Miyahara, Ai Miyamoto, Eri Nishimura and Fumihiko Namba
Antioxidants 2022, 11(5), 899; https://doi.org/10.3390/antiox11050899 - 30 Apr 2022
Cited by 1 | Viewed by 2316
Abstract
Oxygen-induced retinopathy (OIR) is an animal model for retinopathy of prematurity, which is a leading cause of blindness in children. Thioredoxin-1 (TRX) is a small redox protein that has cytoprotective and anti-inflammatory properties in response to oxidative stress. The purpose of this study [...] Read more.
Oxygen-induced retinopathy (OIR) is an animal model for retinopathy of prematurity, which is a leading cause of blindness in children. Thioredoxin-1 (TRX) is a small redox protein that has cytoprotective and anti-inflammatory properties in response to oxidative stress. The purpose of this study was to determine the effect of TRX on OIR in newborn mice. From postnatal day 7, C57BL/6 wild type (WT) and TRX transgenic (TRX-Tg) mice were exposed to either 21% or 75% oxygen for 5 days. Avascular and neovascular regions of the retinas were investigated using fluorescence immunostaining. Fluorescein isothiocyanate-dextran and Hoechst staining were used to measure retinal vascular leakage. mRNA expression levels of proinflammatory and angiogenic factors were analyzed using quantitative polymerase chain reaction. Retinal histological changes were detected using immunohistochemistry. In room air, the WT mice developed well-organized retinas. In contrast, exposing WT newborn mice to hyperoxia hampered retinal development, increasing the retinal avascular and neovascular areas. After hyperoxia exposure, TRX-Tg mice had enhanced retinal avascularization compared with WT mice. TRX-Tg mice had lower retinal neovascularization and retinal permeability during recovery from hyperoxia compared with WT mice. In the early stages after hyperoxia exposure, VEGF-A and CXCL-2 expression levels decreased, while IL-6 expression levels increased in WT newborn mice. Conversely, no differences in gene expressions were observed in the TRX-Tg mouse retina. IGF-1 and Angpt1 levels did not decrease during recovery from hyperoxia in TRX-Tg newborn mice. As a result, overexpression of TRX improves OIR in newborn mice by modulating proinflammatory and angiogenic factors. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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22 pages, 4714 KiB  
Article
OPDAylation of Thiols of the Redox Regulatory Network In Vitro
by Madita Knieper, Lara Vogelsang, Tim Guntelmann, Jens Sproß, Harald Gröger, Andrea Viehhauser and Karl-Josef Dietz
Antioxidants 2022, 11(5), 855; https://doi.org/10.3390/antiox11050855 - 27 Apr 2022
Cited by 9 | Viewed by 2105
Abstract
cis-(+)-12-Oxophytodienoic acid (OPDA) is a reactive oxylipin produced by catalytic oxygenation of polyunsaturated α-linolenic acid (18:3 (ω − 3)) in the chloroplast. Apart from its function as precursor for jasmonic acid synthesis, OPDA serves as a signaling molecule and regulator on its own, [...] Read more.
cis-(+)-12-Oxophytodienoic acid (OPDA) is a reactive oxylipin produced by catalytic oxygenation of polyunsaturated α-linolenic acid (18:3 (ω − 3)) in the chloroplast. Apart from its function as precursor for jasmonic acid synthesis, OPDA serves as a signaling molecule and regulator on its own, namely by tuning enzyme activities and altering expression of OPDA-responsive genes. A possible reaction mechanism is the covalent binding of OPDA to thiols via the addition to the C=C double bond of its α,β-unsaturated carbonyl group in the cyclopentenone ring. The reactivity allows for covalent modification of accessible cysteinyl thiols in proteins. This work investigated the reaction of OPDA with selected chloroplast and cytosolic thioredoxins (TRX) and glutaredoxins (GRX) of Arabidopsis thaliana. OPDA reacted with TRX and GRX as detected by decreased m-PEG maleimide binding, consumption of OPDA, reduced ability for insulin reduction and inability to activate glyceraldehyde-3-phosphate dehydrogenase and regenerate glutathione peroxidase (GPXL8), and with lower efficiency, peroxiredoxin IIB (PRXIIB). OPDAylation of certain protein thiols occurs quickly and efficiently in vitro and is a potent post-translational modification in a stressful environment. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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19 pages, 3343 KiB  
Article
Loss and Recovery of Glutaredoxin 5 Is Inducible by Diet in a Murine Model of Diabesity and Mediated by Free Fatty Acids In Vitro
by Sebastian Friedrich Petry, Axel Römer, Divya Rawat, Lara Brunner, Nina Lerch, Mengmeng Zhou, Rekha Grewal, Fatemeh Sharifpanah, Heinrich Sauer, Gunter Peter Eckert and Thomas Linn
Antioxidants 2022, 11(4), 788; https://doi.org/10.3390/antiox11040788 - 15 Apr 2022
Cited by 3 | Viewed by 3018
Abstract
Free fatty acids (FFA), hyperglycemia, and inflammatory cytokines are major mediators of β-cell toxicity in type 2 diabetes mellitus, impairing mitochondrial metabolism. Glutaredoxin 5 (Glrx5) is a mitochondrial protein involved in the assembly of iron–sulfur clusters required for complexes of the respiratory chain. [...] Read more.
Free fatty acids (FFA), hyperglycemia, and inflammatory cytokines are major mediators of β-cell toxicity in type 2 diabetes mellitus, impairing mitochondrial metabolism. Glutaredoxin 5 (Glrx5) is a mitochondrial protein involved in the assembly of iron–sulfur clusters required for complexes of the respiratory chain. We have provided evidence that islet cells are deprived of Glrx5, correlating with impaired insulin secretion during diabetes in genetically obese mice. In this study, we induced diabesity in C57BL/6J mice in vivo by feeding the mice a high-fat diet (HFD) and modelled the diabetic metabolism in MIN6 cells through exposure to FFA, glucose, or inflammatory cytokines in vitro. qRT-PCR, ELISA, immunohisto-/cytochemistry, bioluminescence, and respirometry were employed to study Glrx5, insulin secretion, and mitochondrial biomarkers. The HFD induced a depletion of islet Glrx5 concomitant with an obese phenotype, elevated FFA in serum and reactive oxygen species in islets, and impaired glucose tolerance. Exposure of MIN6 cells to FFA led to a loss of Glrx5 in vitro. The FFA-induced depletion of Glrx5 coincided with significantly altered mitochondrial biomarkers. In summary, we provide evidence that Glrx5 is regulated by FFA in type 2 diabetes mellitus and is linked to mitochondrial dysfunction and blunted insulin secretion. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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8 pages, 1349 KiB  
Communication
Verification of the Relationship between Redox Regulation of Thioredoxin Target Proteins and Their Proximity to Thylakoid Membranes
by Yuka Fukushi, Yuichi Yokochi, Ken-ichi Wakabayashi, Keisuke Yoshida and Toru Hisabori
Antioxidants 2022, 11(4), 773; https://doi.org/10.3390/antiox11040773 - 13 Apr 2022
Cited by 1 | Viewed by 1669
Abstract
Thioredoxin (Trx) is a key protein of the redox regulation system in chloroplasts, where it modulates various enzyme activities. Upon light irradiation, Trx reduces the disulfide bonds of Trx target proteins (thereby turning on their activities) using reducing equivalents obtained from the photosynthetic [...] Read more.
Thioredoxin (Trx) is a key protein of the redox regulation system in chloroplasts, where it modulates various enzyme activities. Upon light irradiation, Trx reduces the disulfide bonds of Trx target proteins (thereby turning on their activities) using reducing equivalents obtained from the photosynthetic electron transport chain. This reduction process involves a differential response, i.e., some Trx target proteins in the stroma respond slowly to the change in redox condition caused by light/dark changes, while the ATP synthase γ subunit (CF1-γ) located on the surface of thylakoid membrane responds with high sensitivity. The factors that determine this difference in redox kinetics are not yet known, although here, we hypothesize that it is due to each protein’s localization in the chloroplast, i.e., the reducing equivalents generated under light conditions can be transferred more efficiently to the proteins on thylakoid membrane than to stromal proteins. To explore this possibility, we anchored SBPase, one of the stromal Trx target proteins, to the thylakoid membrane in Arabidopsis thaliana. Analyses of the redox behaviors of the anchored and unanchored proteins showed no significant difference in their reduction kinetics, implying that protein sensitivity to redox regulation is determined by other factors. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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Review

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20 pages, 3364 KiB  
Review
Focus on Nitric Oxide Homeostasis: Direct and Indirect Enzymatic Regulation of Protein Denitrosation Reactions in Plants
by Patrick Treffon and Elizabeth Vierling
Antioxidants 2022, 11(7), 1411; https://doi.org/10.3390/antiox11071411 - 21 Jul 2022
Cited by 8 | Viewed by 2333
Abstract
Protein cysteines (Cys) undergo a multitude of different reactive oxygen species (ROS), reactive sulfur species (RSS), and/or reactive nitrogen species (RNS)-derived modifications. S-nitrosation (also referred to as nitrosylation), the addition of a nitric oxide (NO) group to reactive Cys thiols, can alter [...] Read more.
Protein cysteines (Cys) undergo a multitude of different reactive oxygen species (ROS), reactive sulfur species (RSS), and/or reactive nitrogen species (RNS)-derived modifications. S-nitrosation (also referred to as nitrosylation), the addition of a nitric oxide (NO) group to reactive Cys thiols, can alter protein stability and activity and can result in changes of protein subcellular localization. Although it is clear that this nitrosative posttranslational modification (PTM) regulates multiple signal transduction pathways in plants, the enzymatic systems that catalyze the reverse S-denitrosation reaction are poorly understood. This review provides an overview of the biochemistry and regulation of nitro-oxidative modifications of protein Cys residues with a focus on NO production and S-nitrosation. In addition, the importance and recent advances in defining enzymatic systems proposed to be involved in regulating S-denitrosation are addressed, specifically cytosolic thioredoxins (TRX) and the newly identified aldo-keto reductases (AKR). Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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19 pages, 3168 KiB  
Review
Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria
by Manuel J. Mallén-Ponce, María José Huertas and Francisco J. Florencio
Antioxidants 2022, 11(4), 654; https://doi.org/10.3390/antiox11040654 - 28 Mar 2022
Cited by 9 | Viewed by 3201
Abstract
Cyanobacteria evolved the ability to perform oxygenic photosynthesis using light energy to reduce CO2 from electrons extracted from water and form nutrients. These organisms also developed light-dependent redox regulation through the Trx system, formed by thioredoxins (Trxs) and thioredoxin reductases (TRs). Trxs [...] Read more.
Cyanobacteria evolved the ability to perform oxygenic photosynthesis using light energy to reduce CO2 from electrons extracted from water and form nutrients. These organisms also developed light-dependent redox regulation through the Trx system, formed by thioredoxins (Trxs) and thioredoxin reductases (TRs). Trxs are thiol-disulfide oxidoreductases that serve as reducing substrates for target enzymes involved in numerous processes such as photosynthetic CO2 fixation and stress responses. We focus on the evolutionary diversity of Trx systems in cyanobacteria and discuss their phylogenetic relationships. The study shows that most cyanobacteria contain at least one copy of each identified Trx, and TrxA is the only one present in all genomes analyzed. Ferredoxin thioredoxin reductase (FTR) is present in all groups except Gloeobacter and Prochlorococcus, where there is a ferredoxin flavin-thioredoxin reductase (FFTR). Our data suggest that both TRs may have coexisted in ancestral cyanobacteria together with other evolutionarily related proteins such as NTRC or DDOR, probably used against oxidative stress. Phylogenetic studies indicate that they have different evolutionary histories. As cyanobacteria diversified to occupy new habitats, some of these proteins were gradually lost in some groups. Finally, we also review the physiological relevance of redox regulation in cyanobacteria through the study of target enzymes. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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32 pages, 3262 KiB  
Review
Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance
by Arjan de Groot, Laurence Blanchard, Nicolas Rouhier and Pascal Rey
Antioxidants 2022, 11(3), 561; https://doi.org/10.3390/antiox11030561 - 16 Mar 2022
Cited by 5 | Viewed by 2621
Abstract
Deinococcus species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour catalytic cysteines modulating the redox status of Cys and Met in partner proteins. [...] Read more.
Deinococcus species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour catalytic cysteines modulating the redox status of Cys and Met in partner proteins. We present here a detailed description of Deinococcus TRs regarding gene occurrence, sequence features, and physiological functions that remain poorly characterised in this genus. Two NADPH-dependent thiol-based systems are present in Deinococcus. One involves thioredoxins, disulfide reductases providing electrons to protein partners involved notably in peroxide scavenging or in preserving protein redox status. The other is based on bacillithiol, a low-molecular-weight redox molecule, and bacilliredoxin, which together protect Cys residues against overoxidation. Deinococcus species possess various types of thiol peroxidases whose electron supply depends either on NADPH via thioredoxins or on NADH via lipoylated proteins. Recent data gained on deletion mutants confirmed the importance of TRs in Deinococcus tolerance to oxidative treatments, but additional investigations are needed to delineate the redox network in which they operate, and their precise physiological roles. The large palette of Deinococcus TR representatives very likely constitutes an asset for the maintenance of redox homeostasis in harsh stress conditions. Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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Other

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2 pages, 819 KiB  
Correction
Correction: Sainz et al. Analysis of Thioredoxins and Glutaredoxins in Soybean: Evidence of Translational Regulation under Water Restriction. Antioxidants 2022, 11, 1622
by María Martha Sainz, Carla Valeria Filippi, Guillermo Eastman, José Sotelo-Silveira, Omar Borsani and Mariana Sotelo-Silveira
Antioxidants 2023, 12(7), 1377; https://doi.org/10.3390/antiox12071377 - 3 Jul 2023
Viewed by 551
Abstract
In the original publication [...] Full article
(This article belongs to the Special Issue Thioredoxin and Glutaredoxin Systems II)
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