Mycothiol protects &lt;i&gt;Corynebacterium glutamicum&lt;/i&gt; against acid stress via maintaining intracellular pH homeostasis, scavenging ROS, and &lt;i&gt;S&lt;/i&gt;-mycothiolating MetE

Liu, Yingbao; Yang, Xiaobing; Yin, Yiming; Lin, Jie; Chen, Can; Pan, Junfeng; Si, Meiru; Shen, Xihui

doi:10.2323/jgam.2016.02.001

Cited by 33 publications

(19 citation statements)

References 44 publications

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“…Regeneration of peroxidase and methionine sulfoxide reductase activities requires both the mycoredoxin (Mrx1) and thioredoxin pathways in vitro 10, 12, 13, 16, 17 . Apart from its redox-regulatory role for antioxidant enzymes, MSH also functions in thiol-protection of the methionine synthase MetE by protein S- mycothiolation under acid stress conditions 18 .…”

Section: Introductionmentioning

confidence: 99%

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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Section: Introductionmentioning

confidence: 99%

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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“…Oxidative stress caused MetE inactivation by S-mycothiolation, which resulted in methionine synthesis impairment. Under these conditions, MetE protein levels were increased (Follmann et al, 2009;Liu et al, 2016). In E. coli, it is also reported that oxidative stress causes MetE inactivation by S-glutathionylation, which results in methionine limitation (Hondorp and Matthews, 2004).…”

Section: Fig 3 the Effect Of The Growth Phase On Mete Overproductiomentioning

confidence: 87%

RNase E/G-dependent degradation of <i>metE</i> mRNA, encoding methionine synthase, in <i>Corynebacterium glutamicum</i>

Endo

Maeda

Kawame

et al. 2019

J. Gen. Appl. Microbiol.

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Corynebacterium glutamicum is used for the industrial production of various metabolites, including L-glutamic acid and L-lysine. With the aim of understanding the post-transcriptional regulation of amino acid biosynthesis in this bacterium, we investigated the role of RNase E/G in the degradation of mRNAs encoding metabolic enzymes. In this study, we found that the cobalamin-independent methionine synthase MetE was overexpressed in ΔrneG mutant cells grown on various carbon sources. The level of metE mRNA was also approximately 6- to 10-fold higher in the ΔrneG mutant strain than in the wild-type strain. A rifampicin chase experiment showed that the half-life of metE mRNA was approximately 4.2 times longer in the ΔrneG mutant than in the wild-type strain. These results showed that RNase E/G is involved in the degradation of metE mRNA in C. glutamicum.

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“…In vivo ROS levels were measured using the fluorogenic probe 2¢,7¢dichlorofluorescein diacetate (DCFH-DA) (Sigma-Aldrich, St. Louis, MI, USA) as described by Liu et al (2016).…”

Section: Measurement Of Intracellular Ros Levelsmentioning

confidence: 99%

Mycothiol protects <i>Corynebacterium glutamicum</i> against acid stress via maintaining intracellular pH homeostasis, scavenging ROS, and <i>S</i>-mycothiolating MetE

Cited by 33 publications

References 44 publications

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

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

RNase E/G-dependent degradation of <i>metE</i> mRNA, encoding methionine synthase, in <i>Corynebacterium glutamicum</i>

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

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