The Periplasmic PDZ Domain-Containing Protein Prc Modulates Full Virulence, Envelops Stress Responses, and Directly Interacts with Dipeptidyl Peptidase of Xanthomonas oryzae pv. oryzae
The Periplasmic PDZ Domain-Containing Protein Prc Modulates Full Virulence, Envelops Stress Responses, and Directly Interacts with Dipeptidyl Peptidase of Xanthomonas oryzae pv. oryzae
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含有周质 PDZ 结构域的蛋白 Prc 可调节完全毒力、包络应激反应，并直接与米黄单胞菌 pv. 的二肽基肽酶相互作用。
DOI：
10.1094/mpmi-08-13-0234-r
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发表时间：
2014-02-01
影响因子：
3.5
通讯作者：
Qian, Wei
中科院分区：
文献类型：
--
作者：
Deng, Chao-Ying;Deng, Ai-Hua;Qian, Wei
含有PDZ结构域的蛋白酶，也被称为HtrA家族蛋白酶，在细菌细胞中通过调节疾病发病机制和细胞包膜应激反应发挥重要作用。这些蛋白酶通过蛋白水解和非蛋白水解模式具有不同的功能。在这里，我们报告了水稻白叶枯病菌，米黄单胞菌pv的基因组。oryzae编码7种含PDZ结构域的蛋白。编码基因系统失活表明PXO_01122和PXO_04290 （prc）与毒力有关。prc编码一种推测存在于细菌外周质中的HtrA家族蛋白酶。prc突变还导致其对多种环境胁迫敏感，包括H2O2、十二烷基硫酸钠和渗透压胁迫。比较亚蛋白质组学分析显示，prc突变体中34种质周蛋白的含量低于野生型。这些蛋白质与蛋白质水解、大分子生物合成、碳水化合物或能量代谢、信号转导以及蛋白质易位或折叠有关。我们提供的体内和体外证据表明，Prc稳定并直接结合其中一种蛋白质，DppP，一种有助于完全毒力的二肽基肽酶。综上所述，我们的研究结果表明Prc通过作为细胞包膜应激反应的质周调节剂来促进细菌的毒力。
PDZ domain-containing proteases, also known as HtrA family proteases, play important roles in bacterial cells by modulating disease pathogenesis and cell-envelope stress responses. These proteases have diverse functions through proteolysis-and nonproteolysis-dependent modes. Here, we report that the genome of the causative agent of rice bacterial blight, Xanthomonas oryzae pv. oryzae, encodes seven PDZ domain-containing proteins. Systematic inactivation of their encoding genes revealed that PXO_01122 and PXO_04290 (prc) are involved in virulence. prc encodes a putative HtrA family protease that localizes in the bacterial periplasm. Mutation of prc also resulted in susceptibility to multiple environmental stresses, including H2O2, sodium dodecylsulfate, and osmolarity stresses. Comparative subproteomic analyses showed that the amounts of 34 periplasmic proteins were lower in the prc mutant than in wild-type. These proteins were associated with proteolysis, biosynthesis of macromolecules, carbohydrate or energy metabolism, signal transduction, and protein translocation or folding. We provide in vivo and in vitro evidence demonstrating that Prc stabilizes and directly binds to one of these proteins, DppP, a dipeptidyl peptidase contributing to full virulence. Taken together, our results suggest that Prc contributes to bacterial virulence by acting as a periplasmic modulator of cell-envelope stress responses.