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首页> 美国卫生研究院文献>Scientific Reports >Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress
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Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress

机译：在次氯酸盐胁迫下监测耻垢分枝杆菌中的总蛋白硫醇氧化和蛋白S-霉硫醇化

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Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols.
机译：霉菌硫醇（MSH）是放线菌中主要的低分子量（LMW）硫醇。在这里，我们使用shot弹枪蛋白质组学，OxICAT和RNA-seq转录组学来分析蛋白质S-分枝硫代羟化，可逆的硫醇氧化及其对次氯酸盐胁迫下耻垢分枝杆菌基因表达的影响。在NaOCl胁迫下总共鉴定出58种S-霉菌硫醇化蛋白，它们参与能量代谢，脂肪酸和霉菌酸的生物合成，蛋白质翻译，氧化还原调节和排毒。蛋白S-硫代巯基化伴随着巯基代谢组中MSH的消耗。使用OxICAT对1098个Cys残基的氧化还原状态进行的定量分析显示，在NaOCl胁迫下，381个Cys残基（33.6％）显示出增加的氧化作用，与40个S-硫代巯基化Cys肽重叠。没有MSH导致338 Cys残基的较高基础氧化水平（41.1％）。 RseA和RshA抗sigma因子以及Zur和NrdR阻遏物被鉴定为NaOCl敏感蛋白，它们的氧化作用导致RNA-seq转录组中SigH，SigE，Zur和NrdR调控因子上调。总之，我们在这里显示NaOCl胁迫会导致广泛的硫醇氧化，包括蛋白S-霉菌硫醇化，从而导致耻垢分枝杆菌的抗氧化防御机制得到诱导。我们的结果进一步表明，MSH对于维持蛋白质硫醇的还原状态非常重要。

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