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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural basis for antiactivation in bacterial quorum sensing
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Structural basis for antiactivation in bacterial quorum sensing

机译：细菌群体感应中抗激活的结构基础

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Bacteria can communicate via diffusible signal molecules they generate and release to coordinate their behavior in response to the environment. Signal molecule concentration is often proportional to bacterial population density, and when this reaches a critical concentration, reflecting a bacterial quorum, specific behaviors including virulence, symbiosis, and horizontal gene transfer are activated. Quorum-sensing regulation in many Gram-negative bacteria involves acylated homoserine lactone signals that are perceived through binding to LuxR-type, acylated-homo-serine-lactone-responsive transcription factors. Bacteria of the rhi-zobial group employ the LuxR-type transcriptional activator TraR in quorum sensing, and its activity is further regulated through interactions with the TraM antiactivator. In this study, we have crystallographically determined the 3D structure of the TraR-TraM antiactivation complex from Rhizobium sp. strain NGR234. Unexpectedly, the antiactivator TraM binds to TraR at a site distinct from its DNA-binding motif and induces an allosteric conformational change in the protein, thereby preventing DNA binding. Structural analysis reveals a highly conserved TraR-TraM interface and suggests a mechanism for antiactivation complex formation. This structure may inform alternative strategies to control quorum-sensing-regulated microbial activity including amelioration of infectious disease and antibiotic resistance. In addition, the structural basis of antiactivation presents a regulatory interaction that provides general insights relevant to the field of transcription regulation and signal transduction.
机译：细菌可以通过它们产生和释放的可扩散信号分子进行通信，以协调其响应环境的行为。信号分子浓度通常与细菌种群密度成正比，当达到临界浓度时，反映细菌群体，就会激活包括毒力，共生和水平基因转移在内的特定行为。在许多革兰氏阴性细菌中，群体感应调节涉及酰化的高丝氨酸内酯信号，该信号通过与LuxR型酰化的高丝氨酸-内酯-内酯响应转录因子结合而被感知。根瘤菌群的细菌在群体感应中采用LuxR型转录激活因子TraR，其活性通过与TraM抗激活因子的相互作用得到进一步调节。在这项研究中，我们从晶体学上确定了根瘤菌（Rhizobium sp）的TraR-TraM抗活化复合物的3D结构。 NGR234株。出乎意料的是，抗活化剂TraM在与其DNA结合基序不同的位点与TraR结合，并诱导蛋白质的变构构象变化，从而阻止了DNA结合。结构分析揭示了高度保守的TraR-TraM界面，并提出了抗活化复合物形成的机制。这种结构可能会为控制群体感应调节的微生物活性提供替代策略，包括改善传染病和抗生素耐药性。另外，抗激活的结构基础提供了调节相互作用，该相互作用提供了与转录调节和信号转导领域有关的一般见解。

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