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首页> 外文期刊>Infection and immunity >E3 Ubiquitin Ligase Activity and Targeting of BAT3 by Multiple Legionella pneumophila Translocated Substrates
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E3 Ubiquitin Ligase Activity and Targeting of BAT3 by Multiple Legionella pneumophila Translocated Substrates

机译：E3泛素连接酶活性和多个嗜肺军团菌易位底物对BAT3的靶向

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The intracellular bacterial pathogen Legionella pneumophila modulates a number of host processes during intracellular growth, including the eukaryotic ubiquitination machinery, which dictates the stability, activity, and/or localization of a large number of proteins. A number of L. pneumophila proteins contain eukaryotic-like motifs typically associated with ubiquitination. Central among these is a family of five F-box-domain-containing proteins of Legionella pneumophila. Each of these five proteins is translocated to the host cytosol by the Dot/Icm type IV protein translocation system during infection. We show that three of these proteins, LegU1, LegAU13, and LicA, interact with components of the host ubiquitination machinery in vivo. In addition, LegU1 and LegAU13 are integrated into functional Skp-Cullin-F-box (SCF) complexes that confer E3 ubiquitin ligase activity. LegU1 specifically interacts with and can direct the ubiquitination of the host chaperone protein BAT3. In a screen for additional L. pneumophila proteins that associate with LegU1 in mammalian cells, we identified the bacterial protein Lpg2160. We demonstrate that Lpg2160 also associates with BAT3 independently of LegU1. We show that Lpg2160 is a translocated substrate of the Dot/Icm system and contains a C-terminal translocation signal. We propose a model in which LegU1 and Lpg2160 may function redundantly or in concert to modulate BAT3 activity during the course of infection.
机译：细胞内细菌病原体嗜肺军团菌在细胞内生长过程中调节许多宿主过程，包括真核泛素化机制，这决定了大量蛋白质的稳定性，活性和/或定位。多个 L。肺炎蛋白含有通常与泛素化有关的真核样基序。其中一个核心是五个嗜肺军团菌（Legionella pneumophila）含5个F-box-domain的蛋白质家族。在感染过程中，这五种蛋白质中的每一种都通过Dot / Icm IV型蛋白质转运系统转运到宿主细胞质中。我们显示，其中三种蛋白质LegU1，LegAU13和LicA与宿主泛素化机制体内相互作用。此外，LegU1和LegAU13被整合到功能性Skp-Cullin-F-box（SCF）复合物中，从而赋予E3泛素连接酶活性。 LegU1与宿主伴侣蛋白BAT3特异性相互作用并可以指导其泛素化。在屏幕上显示其他 L。与哺乳动物细胞中LegU1相关的嗜肺细胞蛋白，我们鉴定出细菌蛋白Lpg2160。我们证明Lpg2160也独立于LegU1与BAT3关联。我们显示Lpg2160是Dot / Icm系统的易位基板，并包含C端易位信号。我们提出了一个模型，其中LegU1和Lpg2160可能在感染过程中冗余发挥作用或协同调节BAT3的活性。

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