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首页> 美国卫生研究院文献>Antioxidants Redox Signaling >Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite Stress
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Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite Stress

机译：次氯酸盐胁迫下谷氨酸棒杆菌中蛋白S-硫代巯基化作用作为氧化还原开关和硫醇保护机制。

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>Aims: Protein S-bacillithiolation was recently discovered as important thiol protection and redox-switch mechanism in response to hypochlorite stress in Firmicutes bacteria. Here we used transcriptomics to analyze the NaOCl stress response in the mycothiol (MSH)-producing Corynebacterium glutamicum. We further applied thiol-redox proteomics and mass spectrometry (MS) to identify protein S-mycothiolation. >Results: Transcriptomics revealed the strong upregulation of the disulfide stress σH regulon by NaOCl stress in C. glutamicum, including genes for the anti sigma factor (rshA), the thioredoxin and MSH pathways (trxB1, trxC, cg1375, trxB, mshC, mca, mtr) that maintain the redox balance. We identified 25 S-mycothiolated proteins in NaOCl-treated cells by liquid chromatography–tandem mass spectrometry (LC-MS/MS), including 16 proteins that are reversibly oxidized by NaOCl in the thiol-redox proteome. The S-mycothiolome includes the methionine synthase (MetE), the maltodextrin phosphorylase (MalP), the myoinositol-1-phosphate synthase (Ino1), enzymes for the biosynthesis of nucleotides (GuaB1, GuaB2, PurL, NadC), and thiamine (ThiD), translation proteins (TufA, PheT, RpsF, RplM, RpsM, RpsC), and antioxidant enzymes (Tpx, Gpx, MsrA). We further show that S-mycothiolation of the thiol peroxidase (Tpx) affects its peroxiredoxin activity in vitro that can be restored by mycoredoxin1. LC-MS/MS analysis further identified 8 proteins with S-cysteinylations in the mshC mutant suggesting that cysteine can be used for S-thiolations in the absence of MSH. >Innovation and Conclusion: We identified widespread protein S-mycothiolations in the MSH-producing C. glutamicum and demonstrate that S-mycothiolation reversibly affects the peroxidase activity of Tpx. Interestingly, many targets are conserved S-thiolated across bacillithiol- and MSH-producing bacteria, which could become future drug targets in related pathogenic Gram-positives. Antioxid. Redox Signal. 20, 589–605.
机译：>目的：最近发现，S-bacillithiolation蛋白是对Firmicutes细菌中次氯酸盐胁迫的重要硫醇保护和氧化还原转换机制。在这里，我们使用转录组学技术分析了生产霉菌硫醇（MSH）的谷氨酸棒杆菌中的NaOCl应激反应。我们进一步应用了巯基-氧化还原蛋白质组学和质谱（MS）来识别蛋白质S-mycothiolation。 >结果：转录组学揭示了NaOCl胁迫对谷氨酸棒杆菌对二硫键σ H regulon的强烈上调，包括抗sigma因子（rshA），硫氧还蛋白和维持氧化还原平衡的MSH途径（trxB1，trxC，cg1375，trxB，mshC，mca，mtr）。通过液相色谱-串联质谱法（LC-MS / MS），我们在NaOCl处理的细胞中鉴定出25种S-硫代巯基化蛋白质，包括16种在NaCl中可逆氧化的蛋白质。 S-霉菌硫菌素包括蛋氨酸合酶（MetE），麦芽糖糊精磷酸化酶（MalP），肌醇-1-磷酸合酶（Ino1），用于核苷酸生物合成的酶（GuaB1，GuaB2，PurL，NadC）和硫胺素（ThiD） ），翻译蛋白（TufA，PheT，RpsF，RplM，RpsM，RpsC）和抗氧化酶（Tpx，Gpx，MsrA）。我们进一步表明，巯基过氧化物酶（Tpx）的S-霉菌硫代化会影响其过氧化物酶活性，可以通过mycoredoxin1恢复。 LC-MS / MS分析进一步鉴定了 mshC 突变体中具有S-半胱氨酸化的8种蛋白质，这表明半胱氨酸可在没有MSH的情况下用于 S-硫醇化。 > 创新和结论： ：我们在产生MSH的 C中鉴定了广泛的蛋白 S-硫代巯基化。谷氨酸，并证明 S-霉菌硫醇化可逆地影响Tpx的过氧化物酶活性。有趣的是，许多靶标在产芽孢硫醇和MSH的细菌中被保守地 S-硫醇化，这些细菌可能成为相关致病性革兰氏阳性菌的未来药物靶标。 抗氧化剂。氧化还原信号。 20，589–605。

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