The Yersinia pseudotuberculosis degradosome is required for oxidative stress, while its PNPase subunit plays a degradosome-independent role in cold growth.
The Yersinia pseudotuberculosis degradosome is required for oxidative stress, while its PNPase subunit plays a degradosome-independent role in cold growth.
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DOI：
10.1111/j.1574-6968.12000.x
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发表时间：
2012-11
影响因子：
2.1
通讯作者：
Rosenzweig JA
中科院分区：
文献类型：
--
作者：
Henry A;Shanks J;van Hoof A;Rosenzweig JA
耶尔森氏菌多核苷酸磷酸化酶（PNIPs）是一种3 '-5'核糖核酸外切酶，已被证明在几种胁迫反应期间影响生长。在大肠在大肠杆菌中，PND 3是被称为降解体的多蛋白复合物的亚基之一，但也具有不依赖于降解体的功能。E.大肠杆菌核糖核酸酶E（RNase E）用作支架，PNIPs、烯醇化酶（一种糖酵解酶）和RhlB解旋酶都已显示结合在其上。在耶尔森氏菌中，迄今为止，只有PNTR与RNase E发生物理相互作用。我们通过细菌双杂交和免疫共沉淀试验表明，RhlB和烯醇化酶也与RNase E相互作用。有趣的是，虽然PNTR是在低温下正常生长所必需的，但不需要耶尔森氏菌降解体的组装。然而，降解体组装需要在活性氧存在下生长。这些数据表明，虽然Y。假结核菌PNTR通过降解体依赖性机制在氧化应激反应中起作用，PNTR在冷应激期间的作用是不依赖于降解体的。
Yersinia polynucleotide phosphorylase (PNPase), a 3’–5’ exoribonuclease, has been shown to affect growth during several stress responses. In E. coli, PNPase is one of the subunits of a multi-protein complex known as the degradosome, but also has degradosome-independent functions. The carboxy–terminus of E. coli ribonuclease E (RNase E) serves as the scaffold upon which PNPase, enolase (a glycolytic enzyme), and RhlB helicase all have been shown to bind. In the yersiniae, only PNPase has thus far been shown to physically interact with RNase E. We show by bacterial two-hybrid and co-immunoprecipitation assays that RhlB and enolase also interact with RNase E. Interestingly, although PNPase is required for normal growth at cold temperatures, assembly of the yersiniae degradosome was not required. However, degradosome assembly was required for growth in the presence of reactive oxygen species. These data suggest that while the Y. pseudotuberculosis PNPase plays a role in the oxidative stress response through a degradosome-dependent mechanism, PNPase’s role during cold stress is degradosome-independent.
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影响因子：
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