Journal of Microbiology

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Lactobacillus rhamnosus KBL2290 Ameliorates Gut Inflammation in a Mouse Model of Dextran Sulfate Sodium‑Induced Colitis: Woon-ki Kim , Sung-gyu Min , Heeun Kwon , SungJun Park , Min Jung Jo , GwangPyo Ko; J. Microbiol. 2023;61(7):673-682. Published online June 14, 2023; DOI: https://doi.org/10.1007/s12275-023-00061-5

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Ulcerative colitis, a major form of inflammatory bowel disease (IBD) associated with chronic colonic inflammation, may be induced via overreactive innate and adaptive immune responses. Restoration of gut microbiota abundance and diversity is important to control the pathogenesis. Lactobacillus spp., well-known probiotics, ameliorate IBD symptoms via various mechanisms, including modulation of cytokine production, restoration of gut tight junction activity and normal mucosal thickness, and alterations in the gut microbiota. Here, we studied the effects of oral administration of Lactobacillus rhamnosus (L. rhamnosus) KBL2290 from the feces of a healthy Korean individual to mice with DSS-induced colitis. Compared to the dextran sulfate sodium (DSS) + phosphate-buffered saline control group, the DSS + L. rhamnosus KBL2290 group evidenced significant improvements in colitis symptoms, including restoration of body weight and colon length, and decreases in the disease activity and histological scores, particularly reduced levels of pro-inflammatory cytokines and an elevated level of anti-inflammatory interleukin-10. Lactobacillus rhamnosus KBL2290 modulated the levels of mRNAs encoding chemokines and markers of inflammation; increased regulatory T cell numbers; and restored tight junction activity in the mouse colon. The relative abundances of genera Akkermansia, Lactococcus, Bilophila, and Prevotella increased significantly, as did the levels of butyrate and propionate (the major short-chain fatty acids). Therefore, oral L. rhamnosus KBL2290 may be a useful novel probiotic.

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Research Support, Non-U.S. Gov'ts

Dimethyl sulfoxide reduction by a hyperhermophilic archaeon Thermococcus onnurineus NA1 via a cysteine-cystine redox shuttle: Ae Ran Choi , Min-Sik Kim , Sung Gyun Kang , Hyun Sook Lee; J. Microbiol. 2016;54(1):31-38. Published online January 5, 2016; DOI: https://doi.org/10.1007/s12275-016-5574-1

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Abstract

A variety of microbes grow by respiration with dimethyl sulfoxide (DMSO) as an electron acceptor, and several distinct DMSO respiratory systems, consisting of electron carriers and a terminal DMSO reductase, have been characterized. The heterotrophic growth of a hyperthermophilic archaeon Thermococcus onnurineus NA1 was enhanced by the addition of DMSO, but the archaeon was not capable of reducing DMSO to DMS directly using a DMSO reductase. Instead, the archaeon reduced DMSO via a cysteine-cystine redox shuttle through a mechanism whereby cystine is microbially reduced to cysteine, which is then reoxidized by DMSO reduction. A thioredoxin reductase-protein disulfide oxidoreductase redox couple was identified to have intracellular cystine-reducing activity, permitting recycle of cysteine. This study presents the first example of DMSO reduction via an electron shuttle. Several Thermococcales species also exhibited enhanced growth coupled with DMSO reduction, probably by disposing of excess reducing power rather than conserving energy.

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Jialin Chi, Shiyin Wu, Liping Fang, Kai Liu, Shaochen Huang, Wenjun Zhang, Fangbai Li
ACS Sustainable Chemistry & Engineering.2024; 12(44): 16444. CrossRef
Phenotypic and genomic characterization of Bathyarchaeum tardum gen. nov., sp. nov., a cultivated representative of the archaeal class Bathyarchaeia
Maria A. Khomyakova, Alexander Y. Merkel, Dana D. Mamiy, Alexandra A. Klyukina, Alexander I. Slobodkin
Frontiers in Microbiology.2023;[Epub] CrossRef
Direct Electron Transfer between the frhAGB -Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1
Hae-Chang Jung, Jae Kyu Lim, Tae-Jun Yang, Sung Gyun Kang, Hyun Sook Lee, Haruyuki Atomi
Applied and Environmental Microbiology.2020;[Epub] CrossRef
A peroxiredoxin of Thermus thermophilus HB27: Biochemical characterization of a new player in the antioxidant defence
Gabriella Fiorentino, Patrizia Contursi, Giovanni Gallo, Simonetta Bartolucci, Danila Limauro
International Journal of Biological Macromolecules.2020; 153: 608. CrossRef
A Reexamination of Thioredoxin Reductase from Thermoplasma acidophilum, a Thermoacidophilic Euryarchaeon, Identifies It as an NADH-Dependent Enzyme
Dwi Susanti, Usha Loganathan, Austin Compton, Biswarup Mukhopadhyay
ACS Omega.2017; 2(8): 4180. CrossRef
Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
Jae Kyu Lim, Hae-Chang Jung, Sung Gyun Kang, Hyun Sook Lee
Extremophiles.2017; 21(3): 491. CrossRef
Exploring membrane respiratory chains
Bruno C. Marreiros, Filipa Calisto, Paulo J. Castro, Afonso M. Duarte, Filipa V. Sena, Andreia F. Silva, Filipe M. Sousa, Miguel Teixeira, Patrícia N. Refojo, Manuela M. Pereira
Biochimica et Biophysica Acta (BBA) - Bioenergetics.2016; 1857(8): 1039. CrossRef

Characterization of Deinococcus radiophilus Thioredoxin Reductase Active with Both NADH and NADPH: Hee-Jeong Seo , Young Nam Lee; J. Microbiol. 2010;48(5):637-643. Published online November 3, 2010; DOI: https://doi.org/10.1007/s12275-010-0283-7

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Abstract: Thioredoxin reductase (TrxR, EC 1.6.4.5) of Deinococcus radiophilus was purified by steps of sonication, ammonium sulfate fractionation, 2'5' ADP Sepharose 4B affinity chromatography, and Sephadex G-100 gel filtration. The purified TrxR, which was active with both NADPH and NADH, gave a 368 U/mg protein of specific activity with 478-fold purification and 18% recovery from the cell-free extract. An isoelectric point of the purified enzymes was ca. 4.5. The molecular weights of the purified TrxR estimated by PAGE and gel filtration were about 63.1 and 72.2 kDa, respectively. The molecular mass of a TrxR subunit is 37 kDa. This suggests that TrxR definitely belongs to low molecular weight TrxR (L-TrxR). The Km and Vmax of TrxR for NADPH are 12.5 μM and 25 μM/min, whereas those for NADH are 30.2 μM and 192 μ M/min. The Km and Vmax for 5, 5'-dithio-bis-2-nitrobenzoic acid (DTNB, a substituted substrate for thioredoxin) are 463 μM and 756 μM/min, respectively. The presence of FAD in TrxR was confirmed with the absorbance peaks at 385 and 460 nm. The purified TrxR was quite stable from pH 3 to 9, and was thermo-stable up to 70°C. TrxR activity was drastically reduced (ca. 70%) by Cu2+, Zn2+, Hg2+, and Cd2+, but moderately reduced (ca. 50%) by Ag+. A significant inhibition of TrxR by N ethylmaleimide suggests an occurrence of cysteine at its active sites. Amino acid sequences at the N-terminus of purified TrxR are H2N-Ser-Glu-Gln-Ala-Gln-Met-Tyr-Asp-Val-Ile-Ile-Val-Gly-Gly-Gly-Pro-Ala-Gly-Leu-Thr-Ala-COOH. These sequences show high similarity with TrxRs reported in Archaea, such as Methanosarcina mazei, Archaeoglobus fulgidus etc.

The Role and Regulation of Trx1, a Cytosolic Thioredoxin in Schizosaccharomyces pombe: Ji-Yoon Song , Jung-Hye Roe; J. Microbiol. 2008;46(4):408-414. Published online August 31, 2008; DOI: https://doi.org/10.1007/s12275-008-0076-4

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Abstract

The genome of fission yeast Schizosaccharomyces pombe harbors two genes for thioredoxins, trx1+ and trx2+, which encode cytosolic and mitochondrial thioredoxins, respectively. The Δtrx1 mutant was found sensitive to diverse external stressors such as various oxidants, heat, and salt, whereas Δtrx2 mutant was not sensitive except to paraquat, a superoxide generator. Both Δtrx1 and Δtrx2 mutants were more resistant to diamide, a thiol-specific oxidant, than the wild type. The trx1+ gene expression was induced by H2O2 and menadione, being mediated through a stress-responsive transcription factor Pap1. In Δtrx1 cells, the basal expression of Pap1-regulated genes were elevated, suggesting a role for Trx1 as a reducer for oxidized (activated) Pap1. The Δtrx1 mutant exhibited cysteine auxotrophy, which can be overcome by adding sulfite. This suggests that Trx1 serves as a primary electron donor for 3’-phosphoadenosine-5’-phosphosulfate (PAPS) reductase and thus is an essential protein for sulfur assimilation in S. pombe. These results suggest that, in contrast to Trx2 whose role is more confined to mitochondrial functions, Trx1 plays a major role in protecting S. pombe against various stressful conditions and enables proper sulfur metabolism.

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In fission yeast, 65 non-essential mitochondrial proteins related to respiration and stress become essential in low-glucose conditions
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Jie Yin, Wenkai Ren, Guan Yang, Jielin Duan, Xingguo Huang, Rejun Fang, Chongyong Li, Tiejun Li, Yulong Yin, Yongqing Hou, Sung Woo Kim, Guoyao Wu
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Diverse fission yeast genes required for responding to oxidative and metal stress: Comparative analysis of glutathione‐related and other defense gene deletions
Tomáš Pluskal, Kenichi Sajiki, Joanne Becker, Kojiro Takeda, Mitsuhiro Yanagida
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A. Manaa, E. Gharbi, H. Mimouni, S. Wasti, S. Aschi-Smiti, S. Lutts, H. Ben Ahmed
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The Oxidative Stress Responsive Transcription Factor Pap1 Confers DNA Damage Resistance on Checkpoint-Deficient Fission Yeast Cells
Carrie Belfield, Craig Queenan, Hui Rao, Kenji Kitamura, Nancy C. Walworth, Deanna M. Koepp
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The transcription factors Pap1 and Prr1 collaborate to activate antioxidant, but not drug tolerance, genes in response to H 2 O 2
Isabel A. Calvo, Patricia García, José Ayté, Elena Hidalgo
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Katrine M. Andersen, Camilla Jensen, Franziska Kriegenburg, Anne-Marie B. Lauridsen, Colin Gordon, Rasmus Hartmann-Petersen
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Salt-Stress Induced Physiological and Proteomic Changes in Tomato (Solanum lycopersicum) Seedlings
Arafet Manaa, Hela Ben Ahmed, Samira Smiti, Mireille Faurobert
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Cloning and Characterization of a Thioredoxin Gene, CpTrx1, from the Chestnut Blight Fungus Cryphonectria parasitica: Ji-Hye Kim Dae-Hyuk Kim; J. Microbiol. 2006;44(5):556-561.; DOI: https://doi.org/2441 [pii]

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Abstract: A differential display for the expression profiles of wild-type Cryphonectria parasitica and its virally-infected isogenic hypovirulent strain revealed several transcripts of interest, which evidenced significant matches with fungal genes of known function. Among which, we have further analyzed an amplified PCR product with significant sequence similarity to the known fungal stress-responsive thioredoxin gene from Neurospora crassa. The product of the cloned thioredoxin gene, CpTrx1, consists of 117 amino acids, with a predicted molecular mass of 13.0 kDa and a pI of 5.4. Sequence comparisons demonstrated that the deduced protein sequence of the CpTrx1 gene evidenced a high degree of homology to all known thioredoxins, with the highest degree of homology with trx1, a thioredoxin gene from Saccharomyces cerevisiae, and evidenced a preservation of the conserved hall markresidues (Trp-Cys-Gly-Pro-Cys) at the active site of thioredoxin. The E. coli-generated CpTRX1 manifested thioredoxin activity, according to the insulin reduction assay, which indicates that the cloned gene does indeed encode for the C. parasitica thioredoxin.

Occurrence of Thioredoxin Reductase in Deinococcus Species, the UV resistant Bacteria: Hee Jeong Seo , Young Nam Lee; J. Microbiol. 2006;44(4):461-465.; DOI: https://doi.org/2404 [pii]

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Abstract: The occurrence of thioredoxin reductase (NAD(P)H: oxidized-thioredoxin reductase, EC 1.6.4.5, TrxR) in five mesophilic species of Deinococcus was investigated by PAGE. Each species possessed a unique TrxR pattern, for example, a single TrxR characterized D. radiopugnans while multiple forms of TrxR occurred in other Deinococcal spp. Most of TrxRs occurring in Deinococcus showed dual cofactor specificity, active with either NADH or NADPH, although the NADPH specific-TrxR was observed in D. radiophilus and D.proteolyticus.

Transcriptional Analysis and Pap1-Dependence of the Unique Gene Encoding Thioredoxin Reductase from the Fission Yeast: Hyun-Jung Kang , Sung-Min Hong , Byung-Chul Kim , Kyunghoon Kim , Eun-Hee Park , Chang-Jin Lim; J. Microbiol. 2006;44(1):35-41.; DOI: https://doi.org/2339 [pii]

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Abstract: The unique gene encoding thioredoxin reductase (TrxR) was previously cloned and characterized from the fission yeast Schizosaccharomyces pombe, and its expression was induced by oxidative stress. To elucidate the regulatory mechanism of the S. pombe TrxR gene, three fusion plasmids were generated using polymerase chain reaction: pYUTR20, pYUTR30, and pYUTR40. Plasmid pYUTR20 has an upstream region of 891 base pairs, pYUTR30 has 499 in this region, and pYUTR40 has an 186 bp upstream region. Negatively acting sequence is located between ‒1,526 ~ ‒891 bp upstream of the gene. The upstream sequence, responsible for the induction of TrxR by menadione (MD), is situated on the ‒499 ~ ‒186 bp region, which is also required for TrxR induction by mercuric chloride. The same region also appeared to be required for Pap1-mediated transcriptional regulation of the TrxR gene, which contains the two plausible Pap1 binding sites, TTACGAAT and TTACGCGA. Consistently, basal and inducible expression of the TrxR gene was markedly lower in the Pap1-negative TP108-3C cells than in wild-type yeast cells. In summary, up-regulation of the S. pombe TrxR gene is mediated by Pap1 via the transcriptional motif( s) located on the ‒499 ~ ‒186 bp region.

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