Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in &lt;i&gt;Corynebacterium glutamicum&lt;/i&gt;

Su, Tao; Si, Meiru; Zhao, Yaofeng; Shen, Yao; Che, Chengchuan; Liu, Yan; Chen, Can

doi:10.2323/jgam.2018.05.005

Cited by 15 publications

(19 citation statements)

References 33 publications

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“…2A). Moreover, RcsA shares 31.1%, 24.2%, 29.8%, and 22.2% sequence homology with AhpD from P. aeruginosa (33), Mycobacterium tuberculosis (34), Thermus thermophilus TTHA0727 (35), and Corynebacterium glutamicum ATCC 13032 (36), respectively.…”

Section: Resultsmentioning

confidence: 99%

Roles of RcsA, an AhpD Family Protein, in Reactive Chlorine Stress Resistance and Virulence in Pseudomonas aeruginosa

Nontaleerak

Duang-nkern

Wongsaroj

et al. 2020

Appl Environ Microbiol

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Reactive chlorine species (RCS), particularly hypochlorous acid (HOCl), are powerful antimicrobial oxidants generated by biological pathways and chemical syntheses. Pseudomonas aeruginosa is an important opportunistic pathogen that has adapted mechanisms for protection and survival in harsh environments, including RCS exposure. Based on previous transcriptomic studies of HOCl exposure in P. aeruginosa, we found that the expression of PA0565, or rcsA, which encodes an alkyl hydroperoxidase D-like protein, exhibited the highest induction among the RCS-induced genes. In this study, the rcsA expression was dominant under HOCl stress and highly increased under HOCl-related stress conditions. Functional analysis of RcsA showed that the distinguishing core amino acid resides Cys60, Cys63, and His67 were required for the degradation of sodium hypochlorite (NaOCl), suggesting an extended motif in the AhpD family. After producing allelic exchange mutagenesis in the P. aeruginosa rcsA, the P. aeruginosa rcsA-deletion mutant showed a significantly decreased HOCl resistance. Ectopic expression of P. aeruginosa rcsA led to significantly increased NaOCl resistance in Escherichia coli. Moreover, the pathogenicity of the rcsA mutant decreased dramatically in both Caenorhabditis elegans and Drosophila melanogaster host-model systems compared to the wild type. Finally, the Cys60, Cys63, and His67 variants of RcsA were unsuccessful to complement to phenotypes of the rcsA mutant. Overall, our data indicate the importance of P. aeruginosa RcsA in defense against HOCl stress under disinfections and during infections of hosts, which involve the catalytic Cys60, Cys63, and His67 residues. Importance Pseudomonas aeruginosa is a common pathogen that is a major cause of serious infections in many hosts. Hypochlorous acid (HOCl) is a potent antimicrobial agent found in household bleach and is a widely used disinfectant. P. aeruginosa has evolved adaptive mechanisms for protection and survival during HOCl exposure. We identified P. aeruginosa rcsA as a HOCl-responsive gene encoding an antioxidant protein that may be involved in HOCl degradation. RcsA has a distinguishing core motif containing functional Cys60, Cys63 and His67 residues. P. aeruginosa rcsA plays an important role in bleach tolerance with expression of P. aeruginosa rcsA in Escherichia coli also conferring HOCl resistance. Interestingly, RcsA is required for full virulence in worm and fruit fly infection models indicating a correlation between mechanisms of bleach toxicity and host immunity during infection. This provides new insights into the mechanisms used by P. aeruginosa to persist in harsh environments such as hospitals.

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Section: Resultsmentioning

confidence: 99%

Roles of RcsA, an AhpD Family Protein, in Reactive Chlorine Stress Resistance and Virulence in Pseudomonas aeruginosa

Nontaleerak

Duang-nkern

Wongsaroj

et al. 2020

Appl Environ Microbiol

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“…The upregulation of proteins accompanied the removal of Cr(VI) or phenanthrene Chromium (VI) produces reactive oxygen species through the Fenton reaction. Frequently, enzymes such as SOD, alkylhydroperoxidase and alkyl hydroperoxide contribute to the maintenance of the redox balance (Su et al 2019). Indeed, these enzymes were predicted to be upregulated in Streptomyces sp.…”

Section: Discussionmentioning

confidence: 99%

“…Frequently, enzymes such as SOD, alkylhydroperoxidase and alkyl hydroperoxide contribute to the maintenance of the redox balance (Su et al . 2019). Indeed, these enzymes were predicted to be upregulated in Streptomyces sp.…”

Section: Discussionmentioning

confidence: 99%

Genomic analysis and proteomic response of the chromium‐resistant and phenanthrene‐degrading strain Streptomyces sp. MC1

et al. 2021

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Aim: Chemically disparate toxic organic and/or inorganic molecules produced by anthropogenic activities often hinder the bioremediation process. This research was conducted to understand the capacity of Streptomyces sp. MC1 to remove chemically disparate toxics such as Cr(VI) or phenanthrene. Methods and Results: Genomic, metabolic modeling and proteomic approaches were used in this study. Our results demonstrated that Streptomyces sp. MC1 has the genetic determinants to remove Cr(VI) or degrade phenanthrene. Proteomics showed that these genetic determinants were expressed. Metabolic versatility of the strain was confirmed by two metabolic models in complex and minimal media. Interestingly, our results also suggested a connection between the degradation of phenanthrene and synthesis of specialized metabolites. Conclusions: Streptomyces sp. MC1 has the genetic and physiological potential to remove Cr(VI) or degrade phenanthrene Significance and Impact of Study: The probability of a microorganism to survive in the presence of different contaminants depends on its genetic potential and the ability to express it. The genetic and proteomic profiles obtained for Streptomyces sp. MC1 can be recommended as model and predict if other Streptomyces strains can be used in bioremediation processes. Our work also hypothesized that intermediates of the phenanthrene degradation serve as precursors for the specialized metabolism.

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“…Peroxidase activity assays were performed by monitoring the decrease in absorbance at 340 nm arising from NADPH oxidation [40]. The catalytic properties of MstX were determined using a reduced system (Mtr and 500 μM MSH) as the possible electron donors.…”

Section: Methodsmentioning

confidence: 99%

Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress

Che

et al. 2019

Microb Cell Fact

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BackgroundOxidative stress caused by inevitable hostile conditions during fermentative process was the most serious threat to the survival of the well-known industrial microorganism Corynebacterium glutamicum. To survive, C. glutamicum developed several antioxidant defenses including millimolar concentrations of mycothiol (MSH) and protective enzymes. Glutathione (GSH) S-transferases (GSTs) with essentially defensive role in oxidative stress have been well defined in numerous microorganisms, while their physiological and biochemical functions remained elusive in C. glutamicum thus far.ResultsIn the present study, we described protein NCgl1216 belonging to a novel MSH S-transferase Xi class (MstX), considered as the equivalent of GST Xi class (GSTX). MstX had a characteristic conserved catalytic motif (Cys-Pro-Trp-Ala, C-P-W-A). MstX was active as thiol transferase, dehydroascorbate reductase, mycothiolyl-hydroquinone reductase and MSH peroxidase, while it showed null activity toward canonical GSTs substrate as 1-chloro-2,4-dinitrobenzene (CDNB) and GST Omega’s specific substance glutathionyl-acetophenones, indicating MstX had some biochemical characteristics related with mycoredoxin (Mrx). Site-directed mutagenesis showed that, among the two cysteine residues of the molecule, only the residue at position 67 was required for the activity. Moreover, the residues adjacent to the active Cys67 were also important for activity. These results indicated that the thiol transferase of MstX operated through a monothiol mechanism. In addition, we found MstX played important role in various stress resistance. The lack of C. glutamicum mstX gene resulted in significant growth inhibition and increased sensitivity under adverse stress condition. The mstX expression was induced by stress.ConclusionCorynebacterium glutamicum MstX might be critically involved in response to oxidative conditions, thereby giving new insight in how C. glutamicum survived oxidative stressful conditions.

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Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in <i>Corynebacterium glutamicum</i>

Cited by 15 publications

References 33 publications

Roles of RcsA, an AhpD Family Protein, in Reactive Chlorine Stress Resistance and Virulence in Pseudomonas aeruginosa

Roles of RcsA, an AhpD Family Protein, in Reactive Chlorine Stress Resistance and Virulence in Pseudomonas aeruginosa

Genomic analysis and proteomic response of the chromium‐resistant and phenanthrene‐degrading strain Streptomyces sp. MC1

Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress

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