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Functional Domains of the RhlR Transcriptional Regulator of Pseudomonas aeruginosa

机译:铜绿假单胞菌RhlR转录调节因子的功能域。

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摘要

The RhlR transcriptional regulator of Pseudomonas aeruginosa, along with its cognate autoinducer, N-butyryl homoserine lactone (C4-HSL), regulates gene expression in response to cell density. With an Escherichia coli LexA-based protein interaction system, we demonstrated that RhlR multimerized and that the degree of multimerization was dependent on the C4-HSL concentration. Studies with an E. coli lasB::lacZ lysogen demonstrated that RhlR multimerization was necessary for it to function as a transcriptional activator. Deletion analysis of RhlR indicated that the N-terminal domain of the protein is necessary for C4-HSL binding. Single amino acid substitutions in the C-terminal domain of RhlR generated mutant RhlR proteins that had the ability to bind C4-HSL and multimerize but were unable to activate lasB expression, demonstrating that the C-terminal domain is important for target gene activation. Single amino acid substitutions in both the N-terminal and C-terminal domains of RhlR demonstrated that both domains possess residues involved in multimerization. RhlR with a C-terminal deletion and an RhlR site-specific mutant form that possessed multimerization but not transcriptional activation capabilities were able to inhibit the ability of wild-type RhlR to activate rhlA expression in P. aeruginosa. We conclude that C4-HSL binding is necessary for RhlR multimerization and that RhlR functions as a multimer in P. aeruginosa.
机译:铜绿假单胞菌的RhlR转录调节子及其同源的自动诱导物N-丁酰高丝氨酸内酯(C4-HSL)响应细胞密度调节基因表达。使用基于大肠杆菌LexA的蛋白质相互作用系统,我们证明RhlR是多聚的,并且多聚的程度取决于C4-HSL浓度。用大肠杆菌lasB :: lacZ溶原原进行的研究表明,RhlR多聚化对于使其发挥转录激活剂的作用是必要的。 RhlR的缺失分析表明该蛋白的N-末端结构域对于C4-HSL结合是必需的。 RhlR C末端结构域中的单个氨基酸取代产生了具有结合C4-HSL和多聚体但不能激活lasB表达的能力的突变RhlR蛋白,表明C末端结构域对靶基因激活很重要。 RhlR的N端和C端结构域中的单个氨基酸取代表明,两个结构域均具有参与多聚化的残基。具有C端缺失的RhlR和具有多聚化但不具有转录激活功能的RhlR位点特异性突变体形式能够抑制野生型RhlR激活铜绿假单胞菌中rhlA表达的能力。我们得出结论,C4-HSL结合对于RhlR多聚化是必需的,并且RhlR在铜绿假单胞菌中起多聚体的作用。

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