Cell-cell signal dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris
Cell-cell signal dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris
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DOI：
10.4161/viru.1.5.12704
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发表时间：
2010-09-01
期刊：
影响因子：
5.2
通讯作者：
Dow, J. Maxwell
中科院分区：
文献类型：
--
作者：
Ryan, Robert P.;Dow, J. Maxwell
野油菜黄单胞菌致病变种（Xanthomonascampestrispv.）campestris（Xcc）是一种包含RpfG和复合传感器激酶RpfC的双组分系统，涉及对细胞-细胞信号传导分子DSF的传感和响应，以正向调节毒力因子如胞外酶、生物膜结构和运动性的合成。RpfG是一种双组分调节剂，具有连接到HD-GYP环状二GMP磷酸二酯酶结构域的Chey样接收器结构域。在最近的一篇论文中，我们表明RpfG与两种具有二鸟苷酸环化酶（GGDEF）结构域的蛋白质的物理相互作用，起到控制RpfG调节的毒力功能的子集的作用。这些蛋白质-蛋白质相互作用需要RpfG的HD-GYP结构域中的保守GYP基序，并且依赖于DSF信号传导。在这里，我们讨论了这些发现，特别是考虑不同的情况下，RPfG的作用，在多个信号通路，涉及环二GMP的影响毒力。
In the plant pathogen Xanthomonas campestris pv. campestris (Xcc) a two component system comprising RpfG and the complex sensor kinase RpfC is implicated in sensing and responding to the cell-cell signaling molecule DSF to positively regulate the synthesis of virulence factors such as extracellular enzymes, biofilm structure and motility. RpfG is a two-component regulator with a CheY-like receiver domain attached to an HD-GYP cyclic di-GMP phosphodiesterase domain. In a recent paper we showed that that the physical interaction of RpfG with two proteins with a diguanylate cyclase (GGDEF) domain, acts to control a sub-set of RpfG-regulated virulence functions. These protein-protein interactions required the conserved GYP motif in the HD-GYP domain of RpfG and were dependent on DSF signaling. Here we discuss these findings, considering in particular different scenarios for the role of RpfG in multiple signaling pathways involving cyclic di-GMP that impinge on virulence.