Graded Response of the Multifunctional 2-Cysteine Peroxiredoxin, CgPrx, to Increasing Levels of Hydrogen Peroxide in <i>Corynebacterium glutamicum</i>

Si, Meiru; Wang, Tietao; Pan, Junfeng; Lin, Jie; Chen, Can; Wei, Yahong; Lu, Zhiqiang; Shen, Xihui

doi:10.1089/ars.2016.6650

Cited by 26 publications

(37 citation statements)

References 51 publications

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“…However, no significant changes in the expression of these genes were observed in the H 2 O 2 subgroup. This effect may be attributed to H 2 O 2 treatment exceeding the working range for peroxiredoxins (Bang et al, 2016;Si et al, 2017). In addition, intracellular ROS tests showed that light reduced the intracellular ROS level in magnetic cells, suggesting that light can reduce the oxidative stress level in these cells.…”

Section: Discussionmentioning

confidence: 98%

Light irradiation helps magnetotactic bacteria eliminate intracellular reactive oxygen species

Wang

Chen

et al. 2017

Environmental Microbiology

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Magnetotactic bacteria (MTB) demonstrate photoresponse. However, little is known about the biological significance of this behaviour. Magnetosomes exhibit peroxidase-like activity and can scavenge reactive oxygen species (ROS). Magnetosomes extracted from the Magnetospirillum magneticum strain AMB-1 show enhanced peroxidase-like activity under illumination. The present study investigated the effects of light irradiation on nonmagnetic (without magnetosomes) and magnetic (with magnetosomes) AMB-1 cells. Results showed that light irradiation did not affect the growth of nonmagnetic and magnetic cells but significantly increased magnetosome synthesis and reduced intracellular ROS level in magnetic cells. Quantitative reverse transcription polymerase chain reaction (qRT-PCR) was performed to analyse the expression level of magnetosome formation-associated genes (mamA, mms6, mms13 and mmsF) and stress-related genes (recA, oxyR, SOD, amb0664 and amb2684). Results showed that light irradiation upregulated the expression of mms6, mms13 and mmsF. Furthermore, light irradiation upregulated the expression of stress-related genes in nonmagnetic cells but downregulated them in magnetic cells. Additionally, magnetic cells exhibited stronger phototactic behaviour than nonmagnetic ones. These results suggested that light irradiation could heighten the ability of MTB to eliminate intracellular ROS and help them adapt to lighted environments. This phenomenon may be related to the enhanced peroxidase-like activity of magnetosomes under light irradiation.

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Section: Discussionmentioning

confidence: 98%

Light irradiation helps magnetotactic bacteria eliminate intracellular reactive oxygen species

Wang

Chen

et al. 2017

Environmental Microbiology

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“…In C . glutamicum , the major targets for S -mycothiolation are the maltodextrin phosphorylase MalP and the thiol-peroxidase Tpx and it was shown that S -mycothiolation inhibited the activities of MalP and Tpx 10, 15 . Thus, it seems that abundant redox-sensitive metabolic enzymes are the main targets for inactivation by S -thiolations in different bacteria.…”

Section: Discussionmentioning

confidence: 99%

“…The redox-regulatory mechanisms of S -mycothiolated proteins have been studied thus far for several antioxidant enzymes, such as thiol peroxidases (Tpx, Mpx, AhpE) and methionine sulfoxide reductases (MsrA) 10, 12–15 . Moreover, Tpx has been shown to function as a peroxidase and as oligomeric chaperone in response to different levels of H 2 O 2 15 .…”

Section: Introductionmentioning

confidence: 99%

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The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress

Hillion

Imber

Pedre

et al. 2017

Sci Rep

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Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes and functions in post-translational thiol-modification by protein S-mycothiolation as emerging thiol-protection and redox-regulatory mechanism. Here, we have used shotgun-proteomics to identify 26 S-mycothiolated proteins in the pathogen Corynebacterium diphtheriae DSM43989 under hypochlorite stress that are involved in energy metabolism, amino acid and nucleotide biosynthesis, antioxidant functions and translation. The glyceraldehyde-3-phosphate dehydrogenase (GapDH) represents the most abundant S-mycothiolated protein that was modified at its active site Cys153 in vivo. Exposure of purified GapDH to H2O2 and NaOCl resulted in irreversible inactivation due to overoxidation of the active site in vitro. Treatment of GapDH with H2O2 or NaOCl in the presence of MSH resulted in S-mycothiolation and reversible GapDH inactivation in vitro which was faster compared to the overoxidation pathway. Reactivation of S-mycothiolated GapDH could be catalyzed by both, the Trx and the Mrx1 pathways in vitro, but demycothiolation by Mrx1 was faster compared to Trx. In summary, we show 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.

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“…al . reported that an atypical 2-Cys Prx in C. glutamicum mainly exists as a monomer and displays a Trx-dependent peroxidase activity at low peroxide concentrations; over oxidation induces Prx sulfonation irreversibly inactivates its peroxidase activity, and in turn, activates its oligomerization and chaperone activities [33]. Thus, the yin and yang relationship of the peroxidase and chaperone activities of Prx is crucial for maintaining protein homeostasis in cells.…”

Section: Discussionmentioning

confidence: 99%

Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry

Dai

Yang

et al. 2017

Free Radical Biology and Medicine

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Peroxiredoxin 1 (Prx1) is an essential peroxidase that reduces cellular peroxides. It holds 2 indispensable cysteines for its activity: a peroxidatic cysteine (CP) for peroxide reduction and a resolving cysteine (CR) for CP regeneration. CP can be readily sulfonated to CP–SO3H by protracted oxidative stress, which inactivates Prx1 as a peroxidase. By comparison, sulfonation of CR to CR–SO3H in mammalian cells has only been reported once. The rare report of CR sulfonation prompts the following questions: “can CR–SO3H be detected more readily with the current high sensitivity mass spectrometers (MS)?” and “do CP and CR have distinct propensities to sulfonation?” Answers to these questions could shed light on how differential sulfonation of CP and CR regulates Prx1 functions in cells. We used a sensitive Orbitrap MS to analyze both basal and H2O2-induced sulfonation of CR and CP in either recombinant human Prx1 (rPrx1) or HeLa cell Prx1 (cPrx1). In the Orbitrap MS, we optimized both collision-induced dissociation and high-energy collisional dissociation methods to improve the analytical sensitivity cysteine sulfonation. In the basal states without added H2O2, both CP and CR were partially sulfonated in either rPrx1 or cPrx1. Still, exogenous H2O2 heightened the sulfonation levels of both CP and CR by ~200–700%. While titration with H2O2 revealed that CP and CR possessed distinct propensities to sulfonation. This surprising discovery of prevalent Prx1 CR sulfonation affords a motivation for future investigation of its precise functions in cellular stress response.

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Graded Response of the Multifunctional 2-Cysteine Peroxiredoxin, CgPrx, to Increasing Levels of Hydrogen Peroxide in Corynebacterium glutamicum

Abstract: These results reveal that CgPrx functions as a multifunctional protein crucial for adapting appropriate responses to different levels of oxidative challenge in C. glutamicum. Antioxid. Redox Signal. 26, 1-14.

Cited by 26 publications

References 51 publications

Light irradiation helps magnetotactic bacteria eliminate intracellular reactive oxygen species

Light irradiation helps magnetotactic bacteria eliminate intracellular reactive oxygen species

The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress

Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry

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