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Antioxidants
Special Issues
Redox Regulation of Transcription
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Redox Regulation of Transcription

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Antioxidant Enzyme Systems".

Deadline for manuscript submissions: closed (15 March 2022) | Viewed by 17234

Special Issue Editors

Prof. Dr. Ivan Gout

E-Mail Website
Guest Editor
Department of Structural and Molecular Biology, Darwin Building, Gower Street, London WC1E 6BT, UK
Interests: reactive oxygen species; oxidative and metabolic stress response; antioxidant function of coenzyme A; protein CoAlation
Special Issues, Collections and Topics in MDPI journals
Dr. Jerome Gouge

E-Mail Website
Guest Editor
Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, UK
Interests: oxidative stress response and its regulation; transcription; structural biology

Special Issue Information

Dear Colleagues,

Cellular functions are controlled by complex networks of signaling pathways, which transduce information from extracellular stimuli and stresses via extensive regulatory interactions and diverse posttranslational modifications. Transcription factors and transcriptional machinery are at the receiving end of signaling pathways controlling gene expression, and the mode of their regulation and action differs in health and disease. The redox state of cells, which reflects a precise balance between levels of oxidative and reductive reactions, is a crucial regulator of various cellular processes, including transcription. Cellular responses to exogenously and endogenously produced reactive oxygen species involve direct or indirect activation of transcription factors which coordinate the antioxidant response. Molecular mechanisms of redox sensing and regulation by transcription factors have been extensively studied in prokaryotes, and the research on this topic is gaining prominence in mammalian cells.

This Special Issue aims to highlight the current knowledge, recent developments and future perspectives on redox regulation of transcription in prokaryotic and eukaryotic cells, and we would like to invite you to submit your original research findings or review articles on this topic.

Prof. Dr. Ivan Gout
Dr. Jerome Gouge 
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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 species
  • Redox regulation
  • Transcription factors
  • Redox post-translational modifications
  • Gene expression

Published Papers (5 papers)

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Research

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18 pages, 3592 KiB  
Article
p53 Forms Redox-Dependent Protein–Protein Interactions through Cysteine 277
by Tao Shi, Paulien E. Polderman, Marc Pagès-Gallego, Robert M. van Es, Harmjan R. Vos, Boudewijn M. T. Burgering and Tobias B. Dansen
Antioxidants 2021, 10(10), 1578; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox10101578 - 06 Oct 2021
Cited by 7 | Viewed by 2420
Abstract
Reversible cysteine oxidation plays an essential role in redox signaling by reversibly altering protein structure and function. Cysteine oxidation may lead to intra- and intermolecular disulfide formation, and the latter can drastically stabilize protein–protein interactions in a more oxidizing milieu. The activity of [...] Read more.
Reversible cysteine oxidation plays an essential role in redox signaling by reversibly altering protein structure and function. Cysteine oxidation may lead to intra- and intermolecular disulfide formation, and the latter can drastically stabilize protein–protein interactions in a more oxidizing milieu. The activity of the tumor suppressor p53 is regulated at multiple levels, including various post-translational modification (PTM) and protein–protein interactions. In the past few decades, p53 has been shown to be a redox-sensitive protein, and undergoes reversible cysteine oxidation both in vitro and in vivo. It is not clear, however, whether p53 also forms intermolecular disulfides with interacting proteins and whether these redox-dependent interactions contribute to the regulation of p53. In the present study, by combining (co-)immunoprecipitation, quantitative mass spectrometry and Western blot we found that p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions. Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3θ and 53BP1. These interaction partners may play a role in fine-tuning p53 activity under oxidizing conditions. Full article
(This article belongs to the Special Issue Redox Regulation of Transcription)
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14 pages, 1848 KiB  
Article
Thioredoxin Dependent Changes in the Redox States of FurA from Anabaena sp. PCC 7120
by Jorge Guío, María Teresa Bes, Mónica Balsera, Laura Calvo-Begueria, Emma Sevilla, María Luisa Peleato and María F. Fillat
Antioxidants 2021, 10(6), 913; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox10060913 - 04 Jun 2021
Cited by 2 | Viewed by 2872
Abstract
FurA is a multifunctional regulator in cyanobacteria that contains five cysteines, four of them arranged into two CXXC motifs. Lack of a structural zinc ion enables FurA to develop disulfide reductase activity. In vivo, FurA displays several redox isoforms, and the oxidation state [...] Read more.
FurA is a multifunctional regulator in cyanobacteria that contains five cysteines, four of them arranged into two CXXC motifs. Lack of a structural zinc ion enables FurA to develop disulfide reductase activity. In vivo, FurA displays several redox isoforms, and the oxidation state of its cysteines determines its activity as regulator and its ability to bind different metabolites. Because of the relationship between FurA and the control of genes involved in oxidative stress defense and photosynthetic metabolism, we sought to investigate the role of type m thioredoxin TrxA as a potential redox partner mediating dithiol-disulfide exchange reactions necessary to facilitate the interaction of FurA with its different ligands. Both in vitro cross-linking assays and in vivo two-hybrid studies confirmed the interaction between FurA and TrxA. Light to dark transitions resulted in reversible oxidation of a fraction of the regulator present in Anabaena sp. PCC7120. Reconstitution of an electron transport chain using E. coli NADPH-thioredoxin-reductase followed by alkylation of FurA reduced cysteines evidenced the ability of TrxA to reduce FurA. Furthermore, the use of site-directed mutants allowed us to propose a plausible mechanism for FurA reduction. These results point to TrxA as one of the redox partners that modulates FurA performance. Full article
(This article belongs to the Special Issue Redox Regulation of Transcription)
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16 pages, 2735 KiB  
Article
Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A
by Jovana Baković, Bess Yi Kun Yu, Daniel Silva, Maria Baczynska, Sew Yeu Peak-Chew, Amy Switzer, Lynn Burchell, Sivaramesh Wigneshweraraj, Muralidharan Vandanashree, Balasubramanian Gopal, Valeriy Filonenko, Mark Skehel and Ivan Gout
Antioxidants 2021, 10(6), 841; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox10060841 - 25 May 2021
Cited by 9 | Viewed by 2971
Abstract
Staphylococcus aureus (S. aureus) is an aggressive opportunistic pathogen of prominent virulence and antibiotic resistance. These characteristics are due in part to the accessory gene regulator (agr) quorum-sensing system, which allows for the rapid adaptation of S. aureus to [...] Read more.
Staphylococcus aureus (S. aureus) is an aggressive opportunistic pathogen of prominent virulence and antibiotic resistance. These characteristics are due in part to the accessory gene regulator (agr) quorum-sensing system, which allows for the rapid adaptation of S. aureus to environmental changes and thus promotes virulence and the development of pathogenesis. AgrA is the agr system response regulator that binds to the P2 and P3 promoters and upregulates agr expression. In this study, we reveal that S. aureus AgrA is modified by covalent binding of CoA (CoAlation) in response to oxidative or metabolic stress. The sites of CoAlation were mapped by liquid chromatography tandem mass spectrometry (LC–MS/MS) and revealed that oxidation-sensing Cys199 is modified by CoA. Surface plasmon resonance (SPR) analysis showed an inhibitory effect of CoAlation on the DNA-binding activity, as CoAlated AgrA had significantly lower affinity towards the P2 and P3 promoters than non-CoAlated AgrA. Overall, this study provides novel insights into the mode of transcriptional regulation in S. aureus and further elucidates the link between the quorum-sensing and oxidation-sensing roles of the agr system. Full article
(This article belongs to the Special Issue Redox Regulation of Transcription)
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Review

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20 pages, 1754 KiB  
Review
Nrf2 in Cancer, Detoxifying Enzymes and Cell Death Programs
by Tabitha Jenkins and Jerome Gouge
Antioxidants 2021, 10(7), 1030; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox10071030 - 25 Jun 2021
Cited by 28 | Viewed by 5568
Abstract
Reactive oxygen species (ROS) play an important role in cell proliferation and differentiation. They are also by-products of aerobic living conditions. Their inherent reactivity poses a threat for all cellular components. Cells have, therefore, evolved complex pathways to sense and maintain the redox [...] Read more.
Reactive oxygen species (ROS) play an important role in cell proliferation and differentiation. They are also by-products of aerobic living conditions. Their inherent reactivity poses a threat for all cellular components. Cells have, therefore, evolved complex pathways to sense and maintain the redox balance. Among them, Nrf2 (Nuclear factor erythroid 2-related factor 2) plays a crucial role: it is activated under oxidative conditions and is responsible for the expression of the detoxification machinery and antiapoptotic factors. It is, however, a double edge sword: whilst it prevents tumorigenesis in healthy cells, its constitutive activation in cancer promotes tumour growth and metastasis. In addition, recent data have highlighted the importance of Nrf2 in evading programmed cell death. In this review, we will focus on the activation of the Nrf2 pathway in the cytoplasm, the molecular basis underlying Nrf2 binding to the DNA, and the dysregulation of this pathway in cancer, before discussing how Nrf2 contributes to the prevention of apoptosis and ferroptosis in cancer and how it is likely to be linked to detoxifying enzymes containing selenium. Full article
(This article belongs to the Special Issue Redox Regulation of Transcription)
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18 pages, 3014 KiB  
Review
How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes
by In-Gyun Lee and Bong-Jin Lee
Antioxidants 2021, 10(4), 502; https://0-doi-org.brum.beds.ac.uk/10.3390/antiox10040502 - 24 Mar 2021
Cited by 5 | Viewed by 2500
Abstract
Bacteria, like humans, face diverse kinds of stress during life. Oxidative stress, which is produced by cellular metabolism and environmental factors, can significantly damage cellular macromolecules, ultimately negatively affecting the normal growth of the cell. Therefore, bacteria have evolved a number of protective [...] Read more.
Bacteria, like humans, face diverse kinds of stress during life. Oxidative stress, which is produced by cellular metabolism and environmental factors, can significantly damage cellular macromolecules, ultimately negatively affecting the normal growth of the cell. Therefore, bacteria have evolved a number of protective strategies to defend themselves and respond to imposed stress by changing the expression pattern of genes whose products are required to convert harmful oxidants into harmless products. Structural biology combined with biochemical studies has revealed the mechanisms by which various bacterial redox sensor proteins recognize the cellular redox state and transform chemical information into structural signals to regulate downstream signaling pathways. Full article
(This article belongs to the Special Issue Redox Regulation of Transcription)
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