Nitrosative stress: Activation of the transcription factor OxyR
Nitrosative stress: Activation of the transcription factor OxyR
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DOI：
10.1016/s0092-8674(00)80147-6
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发表时间：
1996-09-06
期刊：
影响因子：
64.5
通讯作者：
Stamler, JS
中科院分区：
文献类型：
--
作者：
Hausladen, A;Privalle, CT;Stamler, JS
过氧化氢（H2 O2）对大肠杆菌产生氧化应激，表现为谷胱甘肽和相关氧化还原敏感靶点的氧化。OxyR是一种含巯基的转录激活剂，其氧化控制参与H2 O2解毒的基因的表达。在这里，我们报告说，某些S-亚硝基硫醇（RSNOs）强加了我们所说的“亚硝化应激”，以E。大肠杆菌中，证明细胞内巯基和转录激活OxyR的S-亚硝基化降低。这种细胞和遗传反应决定了RSNO的代谢命运，从而有助于细菌从停滞中拯救出来。我们的研究表明，S-亚硝基化信号可以延伸到转录水平，并描述了一个代谢途径，构成了一个适应亚硝化应激。
Hydrogen peroxide (H2O2) imposes an oxidative stress to Escherichia coli that is manifested by oxidation of glutathione and related redox-sensitive targets. OxyR is a thiol-containing transcriptional activator whose oxidation controls the expression of genes involved in H2O2 detoxification. Here we report that certain S-nitrosothiols (RSNOs) impose what we term a ''nitrosative stress'' to E. coli, evidenced by lowering of intracellular thiol and the transcriptional activation of OxyR by S-nitrosylation. This cellular and genetic response determines the metabolic fate of RSNOs and thereby contributes to bacterial rescue from stasis. Our studies reveal that signaling by S-nitrosylation can extend to the level of transcription and describe a metabolic pathway that constitutes an adaptation to nitrosative stress.