Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
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DOI：
10.1073/pnas.1230660100
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发表时间：
2003-06-24
影响因子：
11.1
通讯作者：
Marco, Y
中科院分区：
文献类型：
--
作者：
Deslandes, L;Olivier, J;Marco, Y
RRS 1-R赋予对青枯病的致病因子青枯雷尔氏菌（Ralstonia solanacearum）的几个菌株的广谱抗性。虽然在遗传学上被定义为隐性，但该R基因编码的蛋白质的结构结合了在几种R蛋白中发现的TIR-NBS-LRR结构域和一些植物转录因子的WRKY基序特征，并且在转基因易感植物中表现为显性基因。在这里，我们表明，PopP 2，一个R。青枯菌III型效应子属于YopJ/AvrRxv蛋白家族，是RRS 1-R识别的无毒蛋白。此外，PopP 2之间的相互作用和RRS 1-R和RRS 1-S，存在于抗性的Nd-1和敏感的Col-5拟南芥生态型，分别通过使用酵母分裂泛素双杂交系统检测。这种需要全长R蛋白的相互作用在RRS 1蛋白和PopP 1之间没有观察到，PopP 1是存在于菌株GMI 1000中的YopJ/AvrRxv家族的另一个成员，并且赋予矮牵牛无毒力。我们进一步证明，Avr蛋白和RRS 1蛋白共定位在细胞核中，并且RRS 1蛋白的核定位依赖于PopP 2的存在。
RRS1-R confers broad-spectrum resistance to several strains of the causal agent of bacterial wilt, Ralstonia solanacearum. Although genetically defined as recessive, this R gene encodes a protein whose structure combines the TIR-NBS-LRR domains found in several R proteins and a WRKY motif characteristic of some plant transcriptional factors and behaves as a dominant gene in transgenic susceptible plants. Here we show that PopP2, a R. solanacearum type III effector, which belongs to the YopJ/AvrRxv protein family, is the avirulence protein recognized by RRS1-R. Furthermore, an interaction between PopP2 and both RRS1-R and RRS1-S, present in the resistant Nd-1 and susceptible Col-5 Arabidopsis thaliana ecotypes, respectively, was detected by using the yeast split-ubiquitin two-hybrid system. This interaction, which required the full-length R protein, was not observed between the RRS1 proteins and PopP1, another member of the YopJ/AvrRxv family present in strain GMI1000 and that confers avirulence in Petunia. We further demonstrate that both the Avr protein and the RRS1 proteins colocalize in the nucleus and that the nuclear localization of the RRS1 proteins are dependent on the presence of PopP2.