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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases
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A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases

机译：沙门氏菌毒力因子家族起独特的一类自动调节的E3泛素连接酶作用

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摘要

Processes as diverse as receptor binding and signaling, cytoskeletal dynamics, and programmed cell death are manipulated by mimics of host proteins encoded by pathogenic bacteria. We show here that the Salmonella virulence factor SspH2 belongs to a growing class of bacterial effector proteins that harness and subvert the eukaryotic ubiquitination pathway. This virulence protein possesses ubiquitina-tion activity that depends on a conserved cysteine residue. A crystal structure of SspH2 reveals a canonical leucine-rich repeat (LRR) domain that interacts with a unique E3 ligase [which we have termed NEL for Novel E3 Ligase] C-terminal fold unrelated to previously observed HECT or RING-finger E3 ligases. Moreover, the LRR domain sequesters the catalytic cysteine residue contained in the NEL domain, and we suggest a mechanism for activation of the ligase requiring a substantial conformational change to release the catalytic domain for function. We also show that the N-terminal domain targets SspH2 to the apical plasma membrane of polarized epithelial cells and propose a model whereby binding of the LRR to proteins at the target site releases the ligase domain for site-specific function.
机译：受体结合和信号转导，细胞骨架动力学以及程序性细胞死亡等多种过程均由致病菌编码的宿主蛋白模拟物操纵。我们在这里显示沙门氏菌毒力因子SspH2属于一类生长的细菌效应蛋白，可以利用和破坏真核泛素化途径。该毒力蛋白具有泛素化活性，该活性取决于保守的半胱氨酸残基。 SspH2的晶体结构揭示了一个富含亮氨酸的重复序列（LRR）结构域，该结构域与一个独特的E3连接酶（我们将其称为新型E3连接酶的NEL）相互作用的C端折叠，与以前观察到的HECT或RING手指E3连接酶无关。此外，LRR域隔离了NEL域中包含的催化半胱氨酸残基，我们提出了一种激活连接酶的机制，需要实质性的构象变化才能释放催化域，以发挥功能。我们还显示，N末端结构域将SspH2靶向极化的上皮细胞的顶端质膜，并提出了一种模型，其中LRR与蛋白质在目标位点的结合释放了针对位点特异性功能的连接酶结构域。

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