scholarly journals Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in Corynebacterium glutamicum

2019 ◽  
Vol 65 (2) ◽  
pp. 72-79 ◽  
Author(s):  
Tao Su ◽  
Meiru Si ◽  
Yunfeng Zhao ◽  
Shumin Yao ◽  
Chengchuan Che ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Alkyl Hydroperoxidase

scholarly journals The role of Corynebacterium glutamicum spiA gene in whcA-mediated oxidative stress gene regulation

2012 ◽  
Vol 331 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Joon-Song Park ◽  
Joo-Young Lee ◽  
Hyung-Joon Kim ◽  
Eung-Soo Kim ◽  
Pil Kim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Gene Regulation ◽  
Corynebacterium Glutamicum ◽  
Stress Gene

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

2015 ◽  
Vol 469 (1) ◽  
pp. 45-57 ◽  
Author(s):  
Meiru Si ◽  
Yixiang Xu ◽  
Tietao Wang ◽  
Mingxiu Long ◽  
Wei Ding ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Stress Resistance ◽  
Functional Characterization ◽  
Gram Positive ◽  
Oxidative Stress Resistance ◽  
Proton Donors ◽  
New Type ◽  
And Oxidative Stress

Mycothiol peroxidase, a new type of GSH peroxidase distributed in GSH-lacking high-(G+C)-content Gram-positive actinobacteria, uses both mycoredoxin and thioredoxin systems as proton donors for regeneration and oxidative stress resistance.

scholarly journals Physiological response of Corynebacterium glutamicum to oxidative stress induced by deletion of the transcriptional repressor McbR

Microbiology ◽  
2008 ◽  
Vol 154 (12) ◽  
pp. 3917-3930 ◽  
Author(s):  
Jens O. Krömer ◽  
Christoph J. Bolten ◽  
Elmar Heinzle ◽  
Hartwig Schröder ◽  
Christoph Wittmann
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Physiological Response ◽  
Transcriptional Repressor

scholarly journals The Staphylococcal Ferritins Are Differentially Regulated in Response to Iron and Manganese and via PerR and Fur

2004 ◽  
Vol 72 (2) ◽  
pp. 972-979 ◽  
Author(s):  
Julie A. Morrissey ◽  
Alan Cockayne ◽  
Kirsty Brummell ◽  
Paul Williams
Keyword(s):  
Oxidative Stress ◽  
Staphylococcus Aureus ◽  
Staphylococcus Epidermidis ◽  
Oxidative Stress Response ◽  
Metal Availability ◽  
Wild Type ◽  
Additional Level ◽  
Alkyl Hydroperoxidase ◽  
Iron And Manganese

ABSTRACT Staphylococcus aureus and Staphylococcus epidermidis ferritin (FtnA and SefA, respectively) homologues are antigenic and highly conserved. A previous study showed that ftnA is a component of the S. aureus PerR regulon with its transcription induced by elevated iron and repressed by PerR, which functions as a manganese-dependent transcriptional repressor. We have further investigated the role of iron and Fur in the regulation of PerR regulon genes ftnA (ferritin), ahpC (alkyl-hydroperoxidase), and mrgA (Dps homologue) and shown that iron has a major role in the regulation of the PerR regulon and hence the oxidative stress response, since in the presence of both iron and manganese, transcription of PerR regulon genes is induced above the repressed levels observed with manganese alone. Furthermore the PerR regulon genes are differentially regulated by metal availability and Fur. First, there is an additional level of PerR-independent regulation of ftnA under low-iron conditions which is not observed with ahpC and mrgA. Second, there is a differential response of these genes to Fur as ftnA expression is constitutive in a fur mutant, while ahpC expression is constitutive under low-Fe/Mn conditions but some repression of ahpC still occurs in the presence of manganese, whereas mrgA expression is still repressed in the fur mutant as in wild-type S. aureus, although there is a decrease in the overall level of mrgA transcription. These studies have also shown that FtnA expression is regulated by growth phase, but maximal transcription of ftnA differs dependent on the growth medium. Moreover, there are significant regulatory differences between the S. aureus and S. epidermidis ferritins, as sefA expression in contrast to that of ftnA is derepressed under low-Fe/Mn ion conditions.

scholarly journals Artificial oxidative stress-tolerant Corynebacterium glutamicum

AMB Express ◽  
2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Joo-Young Lee ◽  
Hyo Jung Lee ◽  
Jiyoon Seo ◽  
Eung-Soo Kim ◽  
Heung-Shick Lee ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum

scholarly journals OsnR is an autoregulatory negative transcription factor controlling redox-dependent stress responses in Corynebacterium glutamicum

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Haeri Jeong ◽  
Younhee Kim ◽  
Heung-Shick Lee
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Stress Responses ◽  
Promoter Region ◽  
Underlying Mechanism ◽  
In Vitro Assays ◽  
Expression Of Genes

Abstract Background Corynebacterium glutamicum is used in the industrial production of amino acids and nucleotides. During the course of fermentation, C. glutamicum cells face various stresses and employ multiple regulatory genes to cope with the oxidative stress. The osnR gene plays a negative regulatory role in redox-dependent oxidative-stress responses, but the underlying mechanism is not known yet. Results Overexpression of the osnR gene in C. glutamicum affected the expression of genes involved in the mycothiol metabolism. ChIP-seq analysis revealed that OsnR binds to the promoter region of multiple genes, including osnR and cg0026, which seems to function in the membrane-associated redox metabolism. Studies on the role of the osnR gene involving in vitro assays employing purified OsnR proteins and in vivo physiological analyses have identified that OsnR inhibits the transcription of its own gene. Further, oxidant diamide stimulates OsnR-binding to the promoter region of the osnR gene. The genes affected by the overexpression of osnR have been found to be under the control of σH. In the osnR-overexpressing strain, the transcription of sigH is significantly decreased and the stimulation of sigH transcription by external stress is lost, suggesting that osnR and sigH form an intimate regulatory network. Conclusions Our study suggests that OsnR not only functions as a transcriptional repressor of its own gene and of those involved in redox-dependent stress responses but also participates in the global transcriptional regulation by controlling the transcription of other master regulators, such as sigH.

scholarly journals NrdH Redoxin Enhances Resistance to Multiple Oxidative Stresses by Acting as a Peroxidase Cofactor in Corynebacterium glutamicum

2013 ◽  
Vol 80 (5) ◽  
pp. 1750-1762 ◽  
Author(s):  
Mei-Ru Si ◽  
Lei Zhang ◽  
Zhi-Fang Yang ◽  
Yi-Xiang Xu ◽  
Ying-Bao Liu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Sequence Similarity ◽  
Thioredoxin Reductase ◽  
Amino Acid Sequence Similarity ◽  
Content Type ◽  
Reduction Activity ◽  
Oxidative Stresses ◽  
High Amino Acid ◽  
Thiol Peroxidase

ABSTRACTNrdH redoxins are small protein disulfide oxidoreductases behaving like thioredoxins but sharing a high amino acid sequence similarity to glutaredoxins. Although NrdH redoxins are supposed to be another candidate in the antioxidant system, their physiological roles in oxidative stress remain unclear. In this study, we confirmed that theCorynebacterium glutamicumNrdH redoxin catalytically reduces the disulfides in the class Ib ribonucleotide reductases (RNR), insulin and 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB), by exclusively receiving electrons from thioredoxin reductase. Overexpression of NrdH increased the resistance ofC. glutamicumto multiple oxidative stresses by reducing ROS accumulation. Accordingly, elevated expression of thenrdHgene was observed when theC. glutamicumwild-type strain was exposed to oxidative stress conditions. It was discovered that the NrdH-mediated resistance to oxidative stresses was largely dependent on the presence of the thiol peroxidase Prx, as the increased resistance to oxidative stresses mediated by overexpression of NrdH was largely abrogated in theprxmutant. Furthermore, we showed that NrdH facilitated the hydroperoxide reduction activity of Prx by directly targeting and serving as its electron donor. Thus, we present evidence that the NrdH redoxin can protect against the damaging effects of reactive oxygen species (ROS) induced by various exogenous oxidative stresses by acting as a peroxidase cofactor.

Impaired oxidative stress and sulfur assimilation contribute to acid tolerance of Corynebacterium glutamicum

2019 ◽  
Vol 103 (4) ◽  
pp. 1877-1891 ◽  
Author(s):  
Ning Xu ◽  
Hongfang Lv ◽  
Liang Wei ◽  
Yuan Liang ◽  
Jiansong Ju ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Corynebacterium Glutamicum ◽  
Acid Tolerance ◽  
Sulfur Assimilation
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