OhsR acts as an organic peroxide-sensing transcriptional activator using an S-mycothiolation mechanism in Corynebacterium glutamicum

@article{Si2018OhsRAA,
  title={OhsR acts as an organic peroxide-sensing transcriptional activator using an S-mycothiolation mechanism in Corynebacterium glutamicum},
  author={Meiru Si and Tao Su and Can Chen and Jinfeng Liu and Zhijin Gong and Chengchuan Che and Guizhi Li and Ge Yang},
  journal={Microbial Cell Factories},
  year={2018},
  volume={17}
}
BackgroundCorynebacterium glutamicum is a well-known producer of various l-amino acids in industry. During the fermenting process, C. glutamicum unavoidably encounters oxidative stress due to a specific reactive oxygen species (ROS) produced by consistent adverse conditions. To combat the ROS, C. glutamicum has developed many common disulfide bond-based regulatory devices to control a specific set of antioxidant genes. However, nothing is known about the mixed disulfide between the protein… 
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TLDR
Results revealed that OasR was a key MarR-type redox stress-responsive transcriptional repressor, and sensed oxidative stress generated through hydroxyl radical formation to mediate antibiotic resistance in C. glutamicum.
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This report is the first to demonstrate the critical role of MsrR-3-MST-MFS in bacterial stress resistance, a novel redox-sensitive member of the XER family, in Corynebacterium glutamicum.
OsmC in Corynebacterium glutamicum was a thiol-dependent organic hydroperoxide reductase.
TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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Thioredoxin and protein-disulfide isomerase selectivity for redox regulation of Proteins in Corynebacterium glutamicum.
  • C. Che, Tao Su, +4 authors Ge Yang
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TLDR
Analysis of the Trx- and PDI-dependent redox shifts of ribonucleotide reductase (RNR), insulin, 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), and several thiol-dependent peroxidases by measuring enzyme activity and thiol status in vitro highlighted the complexity and plasticity of the intracellular redox network.
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Ohr Protects Corynebacterium glutamicum against Organic Hydroperoxide Induced Oxidative Stress
TLDR
It is shown that the Cys-based thiol-dependent Ohr of Corynebacterium glutamicum decomposes organic hydroperoxides more efficiently than hydrogen peroxide.
Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress
TLDR
Analysis of the free thiol groups in wild-type and mutant OhrRs under reducing and oxidizing conditions indicates that C22 is the organic hydroperoxide-sensing residue, and high-performance liquid chromatography-mass spectrometry analysis of tryptic fragments of alkylated, oxidized OhrR and nonreducing polyacrylamide gel electrophoresis analyses confirmed the formation of reversible intersubunit disulfide bonds.
Graded Response of the Multifunctional 2-Cysteine Peroxiredoxin, CgPrx, to Increasing Levels of Hydrogen Peroxide in Corynebacterium glutamicum.
TLDR
It is demonstrated for the first time that atypical 2-Cys CgPrx acts as both a Trx-dependent peroxidase and a molecular chaperone and plays a regulatory role in modulating the peroxide-mediated signaling cascades.
A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress
TLDR
The result that C. glutamicum PrxQ can prevent the damaging effects of adverse stresses by acting as thioredoxin-dependent monomeric peroxidase could be further applied to improve the survival ability and robustness of the important bacterium during fermentation process.
Overexpression of Mycothiol Disulfide Reductase Enhances Corynebacterium glutamicum Robustness by Modulating Cellular Redox Homeostasis and Antioxidant Proteins under Oxidative Stress
TLDR
Results indicate that the Mtr protein functions in C. glutamicum by protecting cells against oxidative stress, thus maintaining intracellular redox homeostasis.
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TLDR
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TLDR
A deletion mutant lacking the putative polyisoprenoid-binding protein showed an increased sensitivity to H2O2, supporting the role of RosR in the oxidative stress response of C. glutamicum.
Functional characterization of a mycothiol peroxidase in Corynebacterium glutamicum that uses both mycoredoxin and thioredoxin reducing systems in the response to oxidative stress.
TLDR
The MPx function is investigated by examining its potential peroxidase activity using different proton donors and it is proposed that the C. glutamicum MPx represents a new type of GPx that uses both mycoredoxin and Trx systems for oxidative stress response.
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TLDR
It is concluded that the redox-sensing transcriptional regulator QorR is involved in disulfide stress response of C. glutamicum by regulating qor2 expression.
Physiological roles of mycothiol in detoxification and tolerance to multiple poisonous chemicals in Corynebacterium glutamicum
TLDR
It is found that intracellular MSH contributes significantly to resistance to alkylating agents, glyphosate, ethanol, antibiotics, heavy metals and aromatic compounds, and is beneficial for withstanding oxidative stress induced by various oxidants in C. glutamicum.
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