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首页> 外文期刊>Nucleic Acids Research >The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence
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The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence

机译：细菌抗毒素HIPB与操作员DNA和磷酸化毒素HIPA建立三元复合物，以调节细菌持久性

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摘要

Nearly all bacteria exhibit a type of phenotypic growth described as persistence that is thought to underlie antibiotic tolerance and recalcitrant chronic infections. The chromosomally encoded high-persistence (Hip) toxin-antitoxin proteins HipA(SO) and HipB(SO) from Shewanella oneidensis, a proteobacterium with unusual respiratory capacities, constitute a type II toxin-antitoxin protein module. Here we show that phosphorylated HipA(SO) can engage in an unexpected ternary complex with HipB(SO) and double-stranded operator DNA that is distinct from the prototypical counterpart complex from Escherichia coli. The structure of HipB(SO) in complex with operator DNA reveals a flexible C-terminus that is sequestered by HipA(SO) in the ternary complex, indicative of its role in binding HipA(SO) to abolish its function in persistence. The structure of HipA(SO) in complex with a non-hydrolyzable ATP analogue shows that HipA(SO) autophosphorylation is coupled to an unusual conformational change of its phosphorylation loop. However, HipA(SO) is unable to phosphorylate the translation factor Elongation factor Tu, contrary to previous reports, but in agreement with more recent findings. Our studies suggest that the phosphorylation state of HipA is an important factor in persistence and that the structural and mechanistic diversity of HipAB modules as regulatory factors in bacterial persistence is broader than previously thought.
机译：几乎所有细菌都表现出一种表达一种表型生长，被称为持续存在的抗生素耐受性和顽抗慢性感染。染色体编码的高持久性（HIP）毒素 - 抗毒素蛋白HIPA（SO）和HIPB（SO）来自Shewanella Inidensis，具有不寻常的呼吸能力的促菌构成II型毒素 - 抗毒素蛋白模块。在这里，我们表明磷酸化的HIPA（SO）可以与HIPB（SO）和双链算子DNA的意外的三元络合物相互作用，其与来自大肠杆菌的原型对手复合物不同。与操作员DNA复合物的HIPB（SO）的结构揭示了在三元复合物中被HIPA（SO）隔离的柔性C-末端，其表明其在结合HIPA（SO）中的作用，以消除其持久性的功能。与非水解ATP类似物的复合物中HIPA（SO）的结构表明，HIPA（SO）自磷酸化与其磷酸化环的不寻常的构象变化偶联。然而，HIPA（SO）无法磷化平移因子伸长因子TU，与之前的报告相反，但与最近的发现一致。我们的研究表明，HIPA的磷酸化状态是持续存在的重要因素，并且HIPAB模块的结构和机械变化为细菌持久性的调节因素比以前认为更广泛。

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