Functional characterization of a mycothiol peroxidase in Corynebacterium glutamicum that uses both mycoredoxin and thioredoxin reducing systems in the response to oxidative stress.

@article{Si2015FunctionalCO,
  title={Functional characterization of a mycothiol peroxidase in Corynebacterium glutamicum that uses both mycoredoxin and thioredoxin reducing systems in the response to oxidative stress.},
  author={Meiru Si and Yixiang Xu and Tietao Wang and Mingxiu Long and Wei Ding and Can Chen and Xinmeng Guan and Yingbao Liu and Yao Wang and Xihui Shen and Shuangjiang Liu},
  journal={The Biochemical journal},
  year={2015},
  volume={469 1},
  pages={
          45-57
        }
}
Previous studies have identified a putative mycothiol peroxidase (MPx) in Corynebacterium glutamicum that shared high sequence similarity to sulfur-containing Gpx (glutathione peroxidase; CysGPx). In the present study, we investigated the MPx function by examining its potential peroxidase activity using different proton donors. The MPx degrades hydrogen peroxide and alkyl hydroperoxides in the presence of either the thioredoxin/Trx reductase (Trx/TrxR) or the mycoredoxin 1/mycothione reductase… 
Molecular mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.
TLDR
It is presented the first evidence that the Mrx1 is able to protect against the damaging effects of various exogenous stresses by acting as a disulfide oxidoreductase, thereby giving a new insight in how C. glutamicum survives oxidative stressful conditions.
A novel mycothiol-dependent thiol–disulfide reductase in Corynebacterium glutamicum involving oxidative stress resistance
TLDR
This study presents the first evidence that NCgl2478 protects against various stresses by acting as an MSH-dependent thiol–disulfide reductase, belonging to a novel DsbA–Mrx1 cluster.
Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in Corynebacterium glutamicum.
TLDR
It is reported that C. glutamicum AhpDs were disulfide oxidoreductases behaving like thioredoxin (Trx) in regenerating thiol-dependent peroxidase for stress response, which provides the theoretical basis for an in-depth study of the reduction system in ahpC-lacking bacteria.
Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress
TLDR
Corynebacterium glutamicum MstX might be critically involved in response to oxidative conditions, thereby giving new insight in how C. glutamum survived oxidative stressful conditions.
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.
Chemistry and Redox Biology of Mycothiol.
TLDR
The description of MSH/Mrx-1-dependent activities of peroxidases helped to explain the higher susceptibility to oxidants observed in Actinomycetes lacking MSH, and the first mycothiol-S-transferase, member of the DinB superfamily of proteins, was described.
Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade
TLDR
Critical details of the Cd-MsrB catalytic mechanism are revealed, including a major structural rearrangement that primes the Cys-122–Cys-66 disulfide for thioredoxin reduction and a reversible protection against excessive oxidation of the catalytic cysteines in Cd, MsrB through intra- and intermolecular disulfides formation and S-mycothiolation.
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.
The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
TLDR
It is shown here that S-mycothiolation can function in redox-regulation and protection of the GapDH active site against overoxidation in C. diphtheriae which can be reversed by both, the Mrx1 and Trx pathways.
Thioredoxin and protein-disulfide isomerase selectivity for redox regulation of Proteins in Corynebacterium glutamicum.
  • C. Che, Tao Su, +4 authors Ge Yang
  • Medicine, Chemistry
    The Journal of general and applied microbiology
  • 2019
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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