OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli
OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli
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OxyR 感知硫烷硫并激活基因以将其在大肠杆菌中去除
DOI：
10.1016/j.redox.2019.101293
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发表时间：
2019-09-01
期刊：
影响因子：
11.4
通讯作者：
Liu, Huaiwei
中科院分区：
文献类型：
--
作者：
Hou, Ningke;Yan, Zhenzhen;Liu, Huaiwei
硫烷硫物种包括硫化氢和有机过硫化物，它们是新发现的正常细胞成分，它们参与信号转导并保护细胞免受氧化应激的伤害。它们的产生得到了广泛的研究，但它们的去除还不是很有特色。在此，我们证明了在厌氧和好氧条件下，高浓度的硫磺对大肠杆菌都有毒性。OxyR是一种众所周知的过氧化氢调节因子，通过突变分析、构建基因电路和体外基因表达发现，它也能感应到硫磺。在Cys199处，多硫化物修饰OxyR形成过硫化物OxyR C199-SSH，修饰后的OxyR激活硫氧还蛋白2和谷氧还蛋白1的表达。这两种酶都能将硫烷硫还原为硫化氢。生物信息学分析表明，OxyR同系物广泛存在于细菌中，包括专性厌氧细菌。因此，硫磺的OxyR传感可能代表了细菌应对硫磺胁迫的一种保存机制。
Sulfane sulfur species including hydrogen polysulfide and organic persulfide are newly recognized normal cellular components, and they participate in signaling and protect cells from oxidative stress. Their production has been extensively studied, but their removal is less characterized. Herein, we showed that sulfane sulfur at high levels was toxic to Escherichia coli under both anaerobic and aerobic conditions. OxyR, a well-known regulator against H2O2, also sensed sulfane sulfur, as revealed via mutational analysis, constructed gene circuits, and in vitro gene expression. Hydrogen polysulfide modified OxyR at Cys199 to form a persulfide OxyR C199-SSH, and the modified OxyR activated the expression of thioredoxin 2 and glutaredoxin 1. The two enzymes are known to reduce sulfane sulfur to hydrogen sulfide. Bioinformatics analysis indicated that OxyR homologs are widely present in bacteria, including obligate anaerobic bacteria. Thus, the OxyR sensing of sulfane sulfur may represent a preserved mechanism for bacteria to deal with sulfane sulfur stress.