Journal Articles
- Lactobacillus rhamnosus KBL2290 Ameliorates Gut Inflammation in a Mouse Model of Dextran Sulfate Sodium‑Induced Colitis
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Woon-ki Kim , Sung-gyu Min , Heeun Kwon , SungJun Park , Min Jung Jo , GwangPyo Ko
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J. Microbiol. 2023;61(7):673-682. Published online June 14, 2023
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DOI: https://doi.org/10.1007/s12275-023-00061-5
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56
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5
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Abstract
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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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- Dietary supplementation with proanthocyanidins and rutin alleviates the symptoms of type 2 diabetes mice and regulates gut microbiota
Yue Gao, Binbin Huang, Yunyi Qin, Bing Qiao, Mengfei Ren, Liqing Cao, Yan Zhang, Maozhen Han
Frontiers in Microbiology.2025;[Epub] CrossRef - Probiotics: Shaping the gut immunological responses
Eirini Filidou, Leonidas Kandilogiannakis, Anne Shrewsbury, George Kolios, Katerina Kotzampassi
World Journal of Gastroenterology.2024; 30(15): 2096. CrossRef - Synergistic effects of probiotics with soy protein alleviate ulcerative colitis by repairing the intestinal barrier and regulating intestinal flora
Rentang Zhao, Bingqing Shang, Luyan Sun, Suyuan Lv, Guolong Liu, Qiu Wu, Yue Geng
Journal of Functional Foods.2024; 122: 106514. CrossRef - Lactobacillus gasseri BNR17 and Limosilactobacillus fermentum ABF21069 Ameliorate High Sucrose-Induced Obesity and Fatty Liver via Exopolysaccharide Production and β-oxidation
Yu Mi Jo, Yoon Ji Son, Seul-Ah Kim, Gyu Min Lee, Chang Won Ahn, Han-Oh Park, Ji-Hyun Yun
Journal of Microbiology.2024; 62(10): 907. CrossRef - Immune-Stimulating Potential of Lacticaseibacillus rhamnosus LM1019 in RAW 264.7 Cells and Immunosuppressed Mice Induced by Cyclophosphamide
Yeji You, Sung-Hwan Kim, Chul-Hong Kim, In-Hwan Kim, YoungSup Shin, Tae-Rahk Kim, Minn Sohn, Jeseong Park
Microorganisms.2023; 11(9): 2312. CrossRef
- Potent antibacterial and antibiofilm activities of TICbf-14, a peptide with increased stability against trypsin
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Liping Wang , Xiaoyun Liu , Xinyue Ye , Chenyu Zhou , Wenxuan Zhao , Changlin Zhou , Lingman Ma
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J. Microbiol. 2022;60(1):89-99. Published online December 29, 2021
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DOI: https://doi.org/10.1007/s12275-022-1368-9
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67
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Abstract
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The poor stability of peptides against trypsin largely limits
their development as potential antibacterial agents. Here, to
obtain a peptide with increased trypsin stability and potent
antibacterial activity, TICbf-14 derived from the cationic peptide
Cbf-14 was designed by the addition of disulfide-bridged
hendecapeptide (CWTKSIPPKPC) loop. Subsequently, the
trypsin stability and antimicrobial and antibiofilm activities
of this peptide were evaluated. The possible mechanisms underlying
its mode of action were also clarified. The results
showed that TICbf-14 exhibited elevated trypsin inhibitory
activity and effectively mitigated lung histopathological damage
in bacteria-infected mice by reducing the bacterial counts,
further inhibiting the systemic dissemination of bacteria and
host inflammation. Additionally, TICbf-14 significantly repressed
bacterial swimming motility and notably inhibited
biofilm formation. Considering the mode of action, we observed
that TICbf-14 exhibited a potent membrane-disruptive
mechanism, which was attributable to its destructive effect
on ionic bridges between divalent cations and LPS of the bacterial
membrane. Overall, TICbf-14, a bifunctional peptide
with both antimicrobial and trypsin inhibitory activity, is
highly likely to become an ideal candidate for drug development
against bacteria.
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- Modified polymeric biomaterials with antimicrobial and immunomodulating properties
Katarzyna Szałapata, Mateusz Pięt, Martyna Kasela, Marcin Grąz, Justyna Kapral-Piotrowska, Aleksandra Mordzińska-Rak, Elżbieta Samorek, Paulina Pieniądz, Jolanta Polak, Monika Osińska-Jaroszuk, Roman Paduch, Bożena Pawlikowska-Pawlęga, Anna Malm, Anna Jar
Scientific Reports.2024;[Epub] CrossRef - Epinecidin-1, a marine antifungal peptide, inhibits Botrytis cinerea and delays gray mold in postharvest peaches
Li Fan, Yingying Wei, Yi Chen, Shu Jiang, Feng Xu, Chundan Zhang, Hongfei Wang, Xingfeng Shao
Food Chemistry.2023; 403: 134419. CrossRef
- Lentibacillus cibarius sp. nov., isolated from kimchi, a Korean fermented food
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Young Joon Oh , Joon Yong Kim , Hee Eun Jo , Hyo Kyeong Park , Seul Ki Lim , Min-Sung Kwon , Hak-Jong Choi
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J. Microbiol. 2020;58(5):387-394. Published online April 11, 2020
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DOI: https://doi.org/10.1007/s12275-020-9507-7
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54
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10
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11
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Abstract
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Two bacterial strains designated NKC220-2T and NKC851-2
were isolated from commercial kimchi from different areas
in Korea. The strains were Gram-positive, aerobic, oxidaseand
catalase-positive, rod-shaped, spore-forming, non-motile,
and halophilic bacteria. Both strains grew without NaCl,
unlike type species in the genus Lentibacillus. The optimal
pH for growth was 8.0, higher than that of the type species
in the genus Lentibacillus, although growth was observed at
pH 5.5–9.0. 16S rRNA gene sequence-based phylogenetic analysis
indicated that the two strains (99.3–99.9% similarity)
are grouped within the genus Lentibacillus and most closely
related to Lentibacillus juripiscarius IS40-3T (97.4–97.6% similarity)
isolated from fish sauce in Thailand. OrthoANI value
between two novel strains and Lentibacillus lipolyticus SSKP1-
9T (79.5–79.6% similarity) was far lower than the species demarcation
threshold. Comparative genomic analysis displayed
differences between the two strains as well as among other
strains belonging to Lentibacillus. Furthermore, each isolate
had strain-specific groups of orthologous genes based on pangenome
analysis. Genomic G + C contents of strains NKC-
220-2T and NKC851-2 were 41.9 and 42.2 mol%, respectively.
The strains contained meso-diaminopimelic acid in their
cell walls, and the major menaquinone was menaquinone-7.
Phosphatidylglycerol, diphosphatidylglycerol, and an unidentified
glycolipid, aminophospholipid, and phospholipid were
the major polar lipid components of both strains. The major
cellular fatty acids of the strains were anteiso-C15:0 and anteiso-
C17:0. Based on phenotypic, genomic, phylogenetic, and
chemotaxonomic features, strains NKC220-2T and NKC851-2
represent novel species of the genus Lentibacillus, for which
the name Lentibacillus cibarius sp. nov. is proposed. The type
strain is NKC220-2T (= KACC 21232T = JCM 33390T).
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- Detection of the Microbial Composition of Some Commercial Fermented Liquid Products via Metagenomic Analysis
Cansu Çelik Doğan, Hafize Tuğba Yüksel Dolgun, Serkan İkiz, Şükrü Kırkan, Uğur Parın
Foods.2023; 12(19): 3538. CrossRef -
Lentibacillus daqui sp. nov., isolated from high-temperature Daqu, a starter for production of Chinese Jiang-flavour Baijiu
Yuan Liang, Zhen-Ming Lu, Wei Shi, Lin-Huan Wu, Li-Juan Chai, Xiao-Juan Zhang, Su-Yi Zhang, Song-Tao Wang, Cai-Hong Shen, Zheng-Hong Xu
International Journal of Systematic and Evolutionary Microbiology
.2023;[Epub] CrossRef - Occurrence of biogenic amines and their correlation with bacterial communities in the Ivorian traditional fermented fish adjuevan during the storage
Marina Ghislaine Abré, Clémentine Amenan Kouakou-Kouamé, Florent Kouadio N’guessan, Corinne Teyssier, Didier Montet
Folia Microbiologica.2023; 68(2): 257. CrossRef - Description of Corynebacterium poyangense sp. nov., isolated from the feces of the greater white-fronted geese (Anser albifrons)
Qian Liu, Guoying Fan, Kui Wu, Xiangning Bai, Xi Yang, Wentao Song, Shengen Chen, Yanwen Xiong, Haiying Chen
Journal of Microbiology.2022; 60(7): 668. CrossRef -
Parasphingorhabdus cellanae sp. nov., isolated from the gut of a Korean limpet, Cellana toreuma
Ji-Ho Yoo, Jeong Eun Han, June-Young Lee, Su-Won Jeong, Yun-Seok Jeong, Jae-Yun Lee, So-Yeon Lee, Hojun Sung, Euon Jung Tak, Hyun Sik Kim, Pil Soo Kim, Jee-Won Choi, Do-Yeon Kim, In Chul Jeong, Do-Hun Gim, Seo Min Kang, Jin-Woo Bae
International Journal of Systematic and Evolutionary Microbiology
.2022;[Epub] CrossRef - Isolation and characterization of tick-borne Roseomonas haemaphysalidis sp. nov. and rodent-borne Roseomonas marmotae sp. nov.
Wentao Zhu, Juan Zhou, Shan Lu, Jing Yang, Xin-He Lai, Dong Jin, Ji Pu, Yuyuan Huang, Liyun Liu, Zhenjun Li, Jianguo Xu
Journal of Microbiology.2022; 60(2): 137. CrossRef - The Methods of Digging for “Gold” within the Salt: Characterization of Halophilic Prokaryotes and Identification of Their Valuable Biological Products Using Sequencing and Genome Mining Tools
Jakub Lach, Paulina Jęcz, Dominik Strapagiel, Agnieszka Matera-Witkiewicz, Paweł Stączek
Genes.2021; 12(11): 1756. CrossRef - Lentibacillus saliphilus. sp. nov., a moderately halophilic bacterium isolated from a saltern in Korea
Yun Wang, Gang-Qiang Jiang, Hong-Ping Lin, Peng Sun, Hong-Yan Zhang, Dong-Mei Lu, Li-Yun Wang, Chang-Jin Kim, Shu-Kun Tang
Archives of Microbiology.2021; 203(2): 621. CrossRef - Salicibibacter cibarius sp. nov. and Salicibibacter cibi sp. nov., two novel species of the family Bacillaceae isolated from kimchi
Young Joon Oh, Joon Yong Kim, Seul Ki Lim, Min-Sung Kwon, Hak-Jong Choi
Journal of Microbiology.2021; 59(5): 460. CrossRef - Flaviflexus ciconiae sp. nov., isolated from the faeces of the oriental stork, Ciconia boyciana
Jae-Yun Lee, Woorim Kang, Pil Soo Kim, So-Yeon Lee, Na-Ri Shin, Hojun Sung, June-Young Lee, Ji-Hyun Yun, Yun-Seok Jeong, Jeong Eun Han, Mi-Ja Jung, Dong-Wook Hyun, Hyun Sik Kim, Euon Jung Tak, Jin-Woo Bae
International Journal of Systematic and Evolutionary Microbiology.2020; 70(10): 5439. CrossRef - List of new names and new combinations that have appeared in effective publications outside of the IJSEM and are submitted for valid publication
Aharon Oren, George M. Garrity
International Journal of Systematic and Evolutionary Microbiology
.2019;[Epub] CrossRef
Reviews
- REVIEW] Antibacterial strategies inspired by the oxidative stress and response networks
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So Youn Kim , Chanseop Park , Hye-Jeong Jang , Bi-o Kim , Hee-Won Bae , In-Young Chung , Eun Sook Kim , You-Hee Cho
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J. Microbiol. 2019;57(3):203-212. Published online February 26, 2019
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DOI: https://doi.org/10.1007/s12275-019-8711-9
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109
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Abstract
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Oxidative stress arises from an imbalance between the excessive
accumulation of reactive oxygen species (ROS) and
a cell’s capability to readily detoxify them. Although ROS are
spontaneously generated during the normal oxygen respiration
and metabolism, the ROS generation is usually augmented
by redox-cycling agents, membrane disrupters, and
bactericidal antibiotics, which contributes their antimicrobial
bioactivity. It is noted that all the bacteria deploy an arsenal
of inducible antioxidant defense systems to cope with the
devastating effect exerted by the oxidative stress: these systems
include the antioxidant effectors such as catalases and
the master regulators such as OxyR. The oxidative stress response
is not essential for normal growth, but critical to survive
the oxidative stress conditions that the bacterial pathogens
may encounter due to the host immune response and/or
the antibiotic treatment. Based on these, we here define the
ROS-inspired antibacterial strategies to enhance the oxidative
stress of ROS generation and/or to compromise the bacterial
response of ROS detoxification, by delineating the ROSgenerating
antimicrobials and the core concept of the bacterial
response against the oxidative stress.
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- [MINIREVIEW] Alanine dehydrogenases in mycobacteria
-
Ji-A Jeong , Jeong-Il Oh
-
J. Microbiol. 2019;57(2):81-92. Published online January 31, 2019
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DOI: https://doi.org/10.1007/s12275-019-8543-7
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48
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11
Web of Science
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11
Crossref
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Abstract
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Since NAD(H)-dependent L-alanine dehydrogenase (EC
1.1.4.1; Ald) was identified as one of the major antigens present
in culture filtrates of Mycobacterium tuberculosis, many
studies on the enzyme have been conducted. Ald catalyzes
the reversible conversion of pyruvate to alanine with concomitant
oxidation of NADH to NAD+ and has a homohexameric
quaternary structure. Expression of the ald genes was
observed to be strongly upregulated in M. tuberculosis and
Mycobacterium smegmatis grown in the presence of alanine.
Furthermore, expression of the ald genes in some mycobacteria
was observed to increase under respiration-inhibitory
conditions such as oxygen-limiting and nutrient-starvation
conditions. Upregulation of ald expression by alanine or under
respiration-inhibitory conditions is mediated by AldR, a
member of the Lrp/AsnC family of transcriptional regulators.
Mycobacterial Alds were demonstrated to be the enzymes required
for utilization of alanine as a nitrogen source and to
help mycobacteria survive under respiration-inhibitory conditions
by maintaining cellular NADH/NAD+ homeostasis.
Several inhibitors of Ald have been developed, and their application
in combination with respiration-inhibitory antitubercular
drugs such as Q203 and bedaquiline was recently suggested.
-
Citations
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- Amino Acid Biosynthesis Inhibitors in Tuberculosis Drug Discovery
Michela Guida, Chiara Tammaro, Miriana Quaranta, Benedetta Salvucci, Mariangela Biava, Giovanna Poce, Sara Consalvi
Pharmaceutics.2024; 16(6): 725. CrossRef - Alanine dehydrogenases from four different microorganisms: characterization and their application in L-alanine production
Pengfei Gu, Qianqian Ma, Shuo Zhao, Qiang Li, Juan Gao
Biotechnology for Biofuels and Bioproducts.2023;[Epub] CrossRef - Application of reductive amination by heterologously expressed Thermomicrobium roseum L-alanine dehydrogenase to synthesize L-alanine derivatives
Huri Dedeakayoğulları, Jarkko Valjakka, Ossi Turunen, Berin Yilmazer, Ğarip Demir, Janne Jänis, Barış Binay
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Pragya Anand, Yusuf Akhter
International Journal of Biological Macromolecules.2022; 212: 474. CrossRef -
Alanine synthesized by alanine dehydrogenase enables ammonium-tolerant nitrogen fixation in
Paenibacillus sabinae
T27
Qin Li, Haowei Zhang, Yi Song, Minyang Wang, Chongchong Hua, Yashi Li, Sanfeng Chen, Ray Dixon, Jilun Li
Proceedings of the National Academy of Sciences.2022;[Epub] CrossRef - Antibacterial Activity of Squaric Amide Derivative SA2 against Methicillin-Resistant Staphylococcus aureus
Moxi Yu, Yachen Hou, Meiling Cheng, Yongshen Liu, Caise Ling, Dongshen Zhai, Hui Zhao, Yaoyao Li, Yamiao Chen, Xiaoyan Xue, Xue Ma, Min Jia, Bin Wang, Pingan Wang, Mingkai Li
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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
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DOI: https://doi.org/10.1007/s12275-016-5574-1
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51
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0
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7
Crossref
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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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Citations
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- Heavy Metal-Resistant Biohybrid System Boosts Dissimilatory Nitrate Reduction to Ammonium for Agronomic Sustainability
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
- A Quantitative and Direct PCR Assay for the Subspecies-Specific Detection of Clavibacter michiganensis subsp. michiganensis Based on a Ferredoxin Reductase Gene
-
Min Seok Cho , Jang Ha Lee , Nam Han Her , ChangKug Kim , Young-Joo Seol , Jang Ho Hahn , Ji Hyoun Baeg , Hong Gi Kim , Dong Suk Park
-
J. Microbiol. 2012;50(3):496-501. Published online June 30, 2012
-
DOI: https://doi.org/10.1007/s12275-012-1611-x
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29
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3
Scopus
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Abstract
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The Gram-positive bacterium Clavibacter michiganensis subsp. michiganensis is the causal agent of canker disease in tomato. Because it is very important to control newly introduced inoculum sources from commercial materials, the specific detection of this pathogen in seeds and seedlings is essential for effective disease control. In this study, a novel and efficient assay for the detection and quantitation of C. michiganensis subsp. michiganensis in symptomless tomato and red pepper seeds was developed. A pair of polymerase chain reaction (PCR) primers (Cmm141F/R) was designed to amplify a specific 141 bp fragment on the basis of a ferredoxin reductase gene of C. michiganensis subsp. michiganensis NCPPB 382. The specificity of the primer set was evaluated using purified DNA from 16 isolates of five C. michiganensis subspecies, one other Clavibacter species, and 17 other reference bacteria. The primer set amplified a single band of expected size from the genomic DNA obtained from the C. michiganensis subsp. michiganensis strains but not from the other C. michiganensis subspecies or from other Clavibacter species. The detection limit was a single cloned copy of the ferredoxin reductase gene of C. michiganensis subsp. michiganensis. In conclusion, this quantitative direct PCR assay can be applied as a practical diagnostic method for epidemiological research and the sanitary management of seeds and seedlings with a low level or latent infection of C. michiganensis subsp. michiganensis.
- 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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37
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4
Scopus
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Abstract
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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 Involvement of the nif-Associated Ferredoxin-Like Genes fdxA and fdxN of Herbaspirillum seropedicae in Nitrogen Fixation
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André L.F. Souza , Adriana L. Invitti , Fabiane G.M. Rego , Rose A. Monteiro , Giseli Klassen , Emanuel M. Souza , Leda S. Chubatsu , Fábio O. Pedrosa , Liu U. Rigo
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J. Microbiol. 2010;48(1):77-83. Published online March 11, 2010
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DOI: https://doi.org/10.1007/s12275-009-0077-y
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Abstract
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The pathway of electron transport to nitrogenase in the endophytic β-Proteobacterium Herbaspirillum seropedicae has not been characterized. We have generated mutants in two nif-associated genes encoding putative ferredoxins, fdxA and fdxN. The fdxA gene is part of the operon nifHDKENXorf1orf2fdxAnifQmodABC
and is transcribed from the nifH promoter, as revealed by lacZ gene fusion. The fdxN gene is probably cotranscribed with the nifB gene. Mutational analysis suggests that the FdxA protein is essential for maximum nitrogenase activity, since the nitrogenase activity of the fdxA mutant strain was reduced to about 30% of that
of the wild-type strain. In addition, the fdxA mutation had no effect on the nitrogenase switch-off in response to ammonium. Nitrogenase activity of a mutant strain lacking the fdxN gene was completely abolished. This phenotype was reverted by complementation with fdxN expressed under lacZ promoter control. The results suggest that the products of both the fdxA and fdxN genes are probably involved in electron transfer during nitrogen fixation.
- Overexpression of Bacterioferritin Comigratory Protein (Bcp) Enhances Viability and Reduced Glutathione Level in the Fission Yeast Under Stress
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Ga-Young Kang , Eun-Hee Park , Kyunghoon Kim , Chang-Jin Lim
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J. Microbiol. 2009;47(1):60-67. Published online February 20, 2009
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DOI: https://doi.org/10.1007/s12275-008-0077-3
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Abstract
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The structural gene encoding bacterioferritin comigratory protein (Bcp) was amplified using PCR from the genomic DNA of Schizosaccharomyces pombe, and transferred into the shuttle vector pRS316 to generate the recombinant plasmid pBCP10. The bcp+ mRNA level in the pBCP10-containing yeast cells was significantly higher than that in the control yeast cells, indicating that the cloned gene is functioning. The S. pombe cells harboring the plasmid pBCP10 exhibited higher survival on the solid minimal media with hydrogen peroxide, tert-BOOH or cadmium than the control yeast cells. They also exhibited enhanced cellular viability in the liquid media containing the stressful agents. The increased viabilities of the fission yeast cells harboring the plasmid pBCP10 were also obtained with 0.4% glucose or 0.4% sucrose as a sole carbon source, and nitrogen starvation, compared with those of the control yeast cells. The total glutathione (GSH) content and total GSH/GSSG ratio were significantly higher in the yeast cells harboring the plasmid pBCP10 than in the control yeast cells. In brief, the S. pombe Bcp plays a protective role in the defensive response to oxidative stress possibly via up-regulation of total and reduced glutathione levels.
- The Role and Regulation of Trx1, a Cytosolic Thioredoxin in Schizosaccharomyces pombe
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Ji-Yoon Song , Jung-Hye Roe
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J. Microbiol. 2008;46(4):408-414. Published online August 31, 2008
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DOI: https://doi.org/10.1007/s12275-008-0076-4
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47
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Crossref
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Abstract
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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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- Cloning and Characterization of a Thioredoxin Gene, CpTrx1, from the Chestnut Blight Fungus Cryphonectria parasitica
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Ji-Hye Kim Dae-Hyuk Kim
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J. Microbiol. 2006;44(5):556-561.
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DOI: https://doi.org/2441 [pii]
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Abstract
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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
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Hee Jeong Seo , Young Nam Lee
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J. Microbiol. 2006;44(4):461-465.
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DOI: https://doi.org/2404 [pii]
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Abstract
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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.
- Effect of Mutations of Five Conserved Histidine Residues in the Catalytic Subunit of the cbb3 Cytochrome c Oxidase on its Function
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Jeong-Il Oh
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J. Microbiol. 2006;44(3):284-292.
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DOI: https://doi.org/2384 [pii]
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Abstract
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The cbb3 cytochrome c oxidase has the dual function as a terminal oxidase and oxygen sensor in the photosynthetic bacterium, Rhodobacter sphaeroides. The cbb3 oxidase forms a signal transduction pathway together with the PrrBA two-component system that controls photosynthesis gene expression in response to changes in oxygen tension in the environment. Under aerobic conditions the cbb3 oxidase generates an inhibitory signal, which shifts the equilibrium of PrrB kinase/phosphatase activities towards the phosphatase mode. Photosynthesis genes are thereby turned off under aerobic conditions. The catalytic subunit (CcoN) of the R. sphaeroides cbb3 oxidase contains five histidine residues (H214, H233, H303, H320, and H444) that are conserved in all CcoN subunits of the cbb3 oxidase, but not in the catalytic subunits of other members of copper-heme superfamily oxidases. H214A mutation of CcoN affected neither catalytic activity nor sensory (signaling) function of the cbb3 oxidase, whereas H320A mutation led to almost complete loss of both catalytic activity and sensory function of the cbb3 oxidase. H233V and H444A mutations brought about the partial loss of catalytic activity and sensory function of the cbb3 oxidase. Interestingly, the H303A mutant form of the cbb3 oxidase retains the catalytic function as a cytochrome c oxidase as compared to the wild-type oxidase, while it is defective in signaling function as an oxygen sensor. H303 appears to be implicated in either signal sensing or generation of the inhibitory signal to the PrrBA two-component system.
- Transcriptional Analysis and Pap1-Dependence of the Unique Gene Encoding Thioredoxin Reductase from the Fission Yeast
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Hyun-Jung Kang , Sung-Min Hong , Byung-Chul Kim , Kyunghoon Kim , Eun-Hee Park , Chang-Jin Lim
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J. Microbiol. 2006;44(1):35-41.
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DOI: https://doi.org/2339 [pii]
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Abstract
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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.