Modulation of Yersinia type three secretion system by the S1 domain of polynucleotide phosphorylase.
Modulation of Yersinia type three secretion system by the S1 domain of polynucleotide phosphorylase.
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DOI：
10.1074/jbc.m405662200
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发表时间：
2005-01-07
影响因子：
4.8
通讯作者：
Schesser, K
中科院分区：
文献类型：
--
作者：
Rosenzweig, JA;Weltman, G;Schesser, K
低温和与宿主吞噬细胞的接触都是在许多细菌物种中进行了相对较好的研究的两个压力。以前的工作表明，胞外核糖核酸酶多核苷酸磷酸化酶(PNPase)是耶尔森氏菌在低温下生长所必需的。在这里，我们发现PNPase还可以增强假结核耶尔森菌和鼠疫耶尔森菌抵抗小鼠巨噬细胞杀伤活性的能力。PNPase是耶尔森氏菌三型分泌系统(TTSS)的最佳功能所必需的，TTSS是一种将效应蛋白直接注入宿主细胞的细胞器。出乎意料的是，PNPase对TTSS的影响不依赖于它的核糖核酸酶活性，而是需要它的S1RNA结合域。相反，催化失活的酶并不能增强PNPase的低温生长效应。令人惊讶的是，通过表达来自PNPase、RNaseR、RNaseII或RpsA的70个氨基酸S1结构域，PNP突变株恢复了野生型TTSS的功能。我们的发现表明，PNPase在提高耶尔森氏菌在应对压力条件下的存活率方面发挥着多方面的作用。
Both low temperatures and encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. Previous work has shown that the exoribonuclease polynucleotide phosphorylase (PNPase) is required for Yersiniae to grow at low temperatures. Here, we show that PNPase also enhances the ability of Yersinia pseudotuberculosis and Yersinia pestis to withstand the killing activities of murine macrophages. PNPase is required for the optimal functioning of the Yersinia type three secretion system (TTSS), an organelle that injects effector proteins directly into host cells. Unexpectedly, the effect of PNPase on the TTSS is independent of its ribonuclease activity and instead requires its S1 RNA binding domain. In contrast, catalytically inactive enzyme does not enhance the low temperature growth effect of PNPase. Surprisingly, wild-type-like TTSS functioning was restored to the pnp mutant strain by expressing just the similar to70 amino acid S1 domains from either PNPase, RNase R, RNase II, or RpsA. Our findings suggest that PNPase plays multifaceted roles in enhancing Yersinia survival in response to stressful conditions.