...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>MicrobiologyOpen >Myo ‐inositol‐1‐phosphate synthase (Ino‐1) functions as a protection mechanism in Corynebacterium glutamicum under oxidative stress
【24h】

Myo ‐inositol‐1‐phosphate synthase (Ino‐1) functions as a protection mechanism in Corynebacterium glutamicum under oxidative stress

机译：Myo-inositol-1-磷酸合酶（Ino-1）在氧化应激下作为棒状谷氨酸棒杆菌的保护机制

获取原文
   

获取外文期刊封面封底 >>

       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Reactive oxygen species (ROS) generated in aerobic metabolism and oxidative stress lead to macromolecules damage, such as to proteins, lipids, and DNA, which can be eliminated by the redox buffer mycothiol (AcCys‐GlcN‐Ins, MSH). Myo ‐inositol‐phosphate synthase (Ino‐1) catalyzes the first committed step in the synthesis of MSH, thus playing a critical role in the growth of the organism. Although Ino‐1s have been systematically studied in eukaryotes, their physiological and biochemical functions remain largely unknown in bacteria. In this study, we report that Ino‐1 plays an important role in oxidative stress resistance in the gram‐positive Actinobacteria Corynebacterium glutamicum . Deletion of the ino‐1 gene resulted in a decrease in cell viability, an increase in ROS production, and the aggravation of protein carbonylation levels under various stress conditions. The physiological roles of Ino‐1 in the resistance to oxidative stresses were corroborated by the absence of MSH in the Δ ino‐1 mutant. In addition, we found that the homologous expression of Ino‐1 in C.?glutamicum yielded a functionally active protein, while when expressed in Escherichia coli BL21(DE3), it lacked measurable activity. An examination of the molecular mass (Mr) suggested that Ino‐1 expressed in E.?coli BL21(DE3) was not folded in a catalytically competent conformation. Together, the results unequivocally showed that Ino‐1 was important for the mediation of oxidative resistance by C.?glutamicum .
机译：在有氧代谢和氧化应激中产生的反应性氧物种（ROS）导致大分子损伤，例如蛋白质，脂质和DNA，其可以被氧化还原缓冲蛋白酶（Accys-Glcn-Ins，MSH）消除。 Myo-inositol-磷酸盐合酶（Ino-1）催化在合成MSH中的第一个承诺步骤，从而在生物体的生长中发挥着关键作用。虽然在真核生物中系统地研究了INO-1S，但它们的生理和生化功能在细菌中仍然很大程度上是未知的。在这项研究中，我们报告称Ino-1在革兰氏阳性肌动菌棒状杆菌中氧化应激抗性起着重​​要作用。 INO-1基因的缺失导致细胞活力降低，ROS生产的增加，以及在各种应激条件下的蛋白质羰基化水平的加剧。通过在ΔIno-1突变体中没有MSH，通过不存在MSH来证实INO-1在耐氧化应力的耐受性的生理作用。此外，我们发现在C.αGlutamicum中的InO-1的同源表达产生了功能效应的蛋白质，而当在大肠杆菌BL21（DE3）中表达时，它缺乏可测量的活性。对分子量（MR）的检查表明，在E.?COLI BL21（DE3）中表达的INO-1未折叠在催化竞争性兼容中。在一起，结果明确表明InO-1对于C.αGlutamicum的氧化耐药的调解非常重要。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号