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Antioxidants
Special Issues
Redox-Based Regulation in Prokaryotes
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Redox-Based Regulation in Prokaryotes

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

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 10155

Special Issue Editor

Dr. Sung-Jae Lee

E-Mail Website
Guest Editor
Department of Biology, Kyung Hee University, Seoul 02447, Korea
Interests: transcriptional regulator; antioxidation; transposition of ISs; protein engineering

Special Issue Information

Dear Colleagues,

Redox sensing and control comprise various fundamental reactions that form part of the spectrum of cell phenomena. This includes the control of molecules and protein activity through biochemical interactions in addition to the many cellular physiological roles related to the control of gene expression, antioxidation responses, and so on. In particular, prokaryotes are extremely sensitive to environmental changes which are detected through the transfer, recognition, and signal transduction of extracellular substances and physicochemical factors. The resulting intracellular redox balance then has important roles, acting as a limiting factor and with global action criteria in cellular components such as molecules, proteins, and genome and membrane compartments. Thus, this subject provides us with a better understanding of cellular regulation in bacteria and archaea.

We invite you to submit your latest research findings or a review article to this Special Issue, which will bring together current research concerning redox-based regulation in prokaryotes. We welcome submissions concerning all manipulations of redox control in bacteria and archaea, biosynthesis of antioxidants, enzymatic activity under redox balance, transcriptional regulation, and certain physiological phenomena occurring through redox control in prokaryotes. We believe that this Special Issue, “Redox-Based Regulation in Prokaryotes”, will help to highlight the most recent advances on all aspects of gene expression, protein activity, and physiological aspects, including stress responses via redox control in bacteria and archaea.

We look forward to receiving your contributions.

Dr. Sung-Jae Lee
Guest Editor

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

  • redox sensing
  • gene expression control
  • biochemistry of redox potency
  • proteins and their regulation
  • redox-controlled prokaryotic physiology

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Published Papers (3 papers)

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Research

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15 pages, 2641 KiB  
Article
Structural and Biochemical Characterization of Thioredoxin-2 from Deinococcus radiodurans
by Min-Kyu Kim, Lei Zhao, Soyoung Jeong, Jing Zhang, Jong-Hyun Jung, Ho Seong Seo, Jong-il Choi and Sangyong Lim
Antioxidants 2021, 10(11), 1843; https://doi.org/10.3390/antiox10111843 - 20 Nov 2021
Cited by 14 | Viewed by 2583
Abstract
Thioredoxin (Trx), a ubiquitous protein showing disulfide reductase activity, plays critical roles in cellular redox control and oxidative stress response. Trx is a member of the Trx system, comprising Trx, Trx reductase (TrxR), and a cognate reductant (generally reduced nicotinamide adenine dinucleotide phosphate, [...] Read more.
Thioredoxin (Trx), a ubiquitous protein showing disulfide reductase activity, plays critical roles in cellular redox control and oxidative stress response. Trx is a member of the Trx system, comprising Trx, Trx reductase (TrxR), and a cognate reductant (generally reduced nicotinamide adenine dinucleotide phosphate, NADPH). Bacterial Trx1 contains only the Trx-fold domain, in which the active site CXXC motif that is critical for the disulfide reduction activity is located. Bacterial Trx2 contains an N-terminal extension, which forms a zinc-finger domain, including two additional CXXC motifs. The multi-stress resistant bacterium Deinococcus radiodurans encodes both Trx1 (DrTrx1) and Trx2 (DrTrx2), which act as members of the enzymatic antioxidant systems. In this study, we constructed Δdrtrx1 and Δdrtrx2 mutants and examined their survival rates under H2O2 treated conditions. Both drtrx1 and drtrx2 genes were induced following H2O2 treatment, and the Δdrtrx1 and Δdrtrx2 mutants showed a decrease in resistance toward H2O2, compared to the wild-type. Native DrTrx1 and DrTrx2 clearly displayed insulin and DTNB reduction activity, whereas mutant DrTrx1 and DrTrx2, which harbors the substitution of conserved cysteine to serine in its active site CXXC motif, showed almost no reduction activity. Mutations in the zinc binding cysteines did not fully eliminate the reduction activities of DrTrx2. Furthermore, we solved the crystal structure of full-length DrTrx2 at 1.96 Å resolution. The N-terminal zinc-finger domain of Trx2 is thought to be involved in Trx-target interaction and, from our DrTrx2 structure, the orientation of the zinc-finger domain of DrTrx2 and its interdomain interaction, between the Trx-fold domain and the zinc-finger domain, is clearly distinguished from those of the other Trx2 structures. Full article
(This article belongs to the Special Issue Redox-Based Regulation in Prokaryotes)
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11 pages, 2712 KiB  
Article
Sulfane Sulfur Is a Strong Inducer of the Multiple Antibiotic Resistance Regulator MarR in Escherichia coli
by Huangwei Xu, Guanhua Xuan, Huaiwei Liu, Yongzhen Xia and Luying Xun
Antioxidants 2021, 10(11), 1778; https://doi.org/10.3390/antiox10111778 - 6 Nov 2021
Cited by 12 | Viewed by 2818
Abstract
Sulfane sulfur, including persulfide and polysulfide, is produced from the metabolism of sulfur-containing organic compounds or from sulfide oxidation. It is a normal cellular component, participating in signaling. In bacteria, it modifies gene regulators to activate the expression of genes involved in sulfur [...] Read more.
Sulfane sulfur, including persulfide and polysulfide, is produced from the metabolism of sulfur-containing organic compounds or from sulfide oxidation. It is a normal cellular component, participating in signaling. In bacteria, it modifies gene regulators to activate the expression of genes involved in sulfur metabolism. However, to determine whether sulfane sulfur is a common signal in bacteria, additional evidence is required. The ubiquitous multiple antibiotic resistance regulator (MarR) family of regulators controls the expression of numerous genes, but the intrinsic inducers are often elusive. Recently, two MarR family members, Pseudomonas aeruginosa MexR and Staphylococcus aureus MgrA, have been reported to sense sulfane sulfur. Here, we report that Escherichia coli MarR, the prototypical member of the family, also senses sulfane sulfur to form one or two disulfide or trisulfide bonds between two dimers. Although the tetramer with two disulfide bonds does not bind to its target DNA, our results suggest that the tetramer with one disulfide bond does bind to its target DNA, with reduced affinity. An MarR-repressed mKate reporter is strongly induced by polysulfide in E. coli. Further investigation is needed to determine whether sulfane sulfur is a common signal of the family members, but three members sense cellular sulfane sulfur to turn on antibiotic resistance genes. The findings offer additional support for a general signaling role of sulfane sulfur in bacteria. Full article
(This article belongs to the Special Issue Redox-Based Regulation in Prokaryotes)
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Review

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15 pages, 1438 KiB  
Review
Active Transposition of Insertion Sequences in Prokaryotes: Insights from the Response of Deinococcus geothermalis to Oxidative Stress
by Eunjung Shin, Qianying Ye and Sung-Jae Lee
Antioxidants 2022, 11(3), 481; https://doi.org/10.3390/antiox11030481 - 28 Feb 2022
Cited by 3 | Viewed by 4064
Abstract
Bacterial genomes contain numerous insertion sequences (ISs) as transposable elements involved in actions such as the sequestration, transmission, mutation and activation of genes that can influence the responsive capacity of the organism to environmental challenges. To date, at least 30 IS families have [...] Read more.
Bacterial genomes contain numerous insertion sequences (ISs) as transposable elements involved in actions such as the sequestration, transmission, mutation and activation of genes that can influence the responsive capacity of the organism to environmental challenges. To date, at least 30 IS families have been identified. In this review, we describe how certain ISs are transposed to carotenoid biosynthesis genes, such as phytoene synthase and phytoene desaturase, when radiation-resistant Deinococcus geothermalis with a redox imbalance and a targeted gene disruption mutation is exposed to oxidative stressors, such as gamma-irradiation, dielectric bilayer discharge plasma and hydrogen peroxide. We also explain the genetic features of IS elements, spontaneous mutation and various stress responses, including nutrient limitation, and physicochemical and oxidative stress, associated with the active transposition of bacterial ISs. Based on the current knowledge, we posit that the redox signalling mechanism inducing IS transposition involves redox sensing and redox switching for the activation of transposase expression and its activity. Full article
(This article belongs to the Special Issue Redox-Based Regulation in Prokaryotes)
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