AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species Pseudomonas aeruginosa and subsequently abundant P. aeruginosa clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of P. aeruginosa primarily in stationary phase and boosts heat resistance 100-fold when expressed in Escherichia coli. This qualifies ClpG as a potential persistence and virulence factor in P. aeruginosa.

中文翻译：

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独立的ClpG歧化酶赋予细菌优异的耐热性

AAA +分解油脂可溶解聚集的蛋白质，并赋予细胞耐热性。它们的分解活性关键取决于伴侣蛋白，该伴侣蛋白将AAA +分解蛋白靶向蛋白聚集体，同时刺激其ATPase活性。在这里，我们报告通过铜绿假单胞菌和随后丰富的铜绿假单胞菌物种通过水平基因转移获得的两个有效的ClpG disaggregase同源物。克隆C. ClpG在不涉及任何合作伙伴的情况下，具有很高的独立分解潜力。ClpG与其他AAA +分解油脂具有特定的分子特征，包括高的基础ATPase活性，独特的聚集结合结构域以及在固定相中几乎排他的表达。因此，ClpG主要在固定相中极大地有助于铜绿假单胞菌的耐热性，并且在大肠杆菌中表达时耐热性提高100倍。这使ClpG成为铜绿假单胞菌中潜在的持久性和毒力因子。