Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris (Retracted Article)
Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris (Retracted Article)
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DOI：
10.1111/mmi.12000
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发表时间：
2012-11-01
影响因子：
3.6
通讯作者：
Dow, J. Maxwell
中科院分区：
文献类型：
--
作者：
Ryan, Robert P.;McCarthy, Yvonne;Dow, J. Maxwell
RpfG是一类广泛分布的细菌双组分调节剂的成员，具有HD-GYP环状二GMP磷酸二酯酶结构域。在植物病原体野油菜黄单胞菌（Xanthomonascampestris）中，RpfG与传感器激酶RpfC一起调节多种因子作为对细胞间扩散信号因子（DSF）的响应。RpfG与两个二鸟苷酸环化酶（GGDEF）结构域蛋白的动态物理相互作用控制运动性。在这里，我们表明，与预期相反，调节运动的GGDEF结构域蛋白不依赖于其环二GMP合成活性。此外，我们表明，RpfG和GGDEF结构域蛋白的复合物招募一个特定的PilZ结构域衔接蛋白，然后这个复合物与菌毛马达蛋白皮鲁和PiIT相互作用。结果支持一个模型，其中DSF信号通过影响菌毛作用的蛋白质的高度调节的动态相互作用来影响运动性。我们确定HD-GYP结构域相互作用所需的特定基序在许多GGDEF结构域蛋白中是保守的，这表明通过结构域间相互作用进行调节具有广泛的相关性。
RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris, RpfG together with the sensor kinase RpfC regulates multiple factors as a response to the cell-to-cell Diffusible Signalling Factor (DSF). A dynamic physical interaction of RpfG with two diguanylate cyclase (GGDEF) domain proteins controls motility. Here we show that, contrary to expectation, regulation of motility by the GGDEF domain proteins does not depend upon their cyclic di-GMP synthetic activity. Furthermore we show that the complex of RpfG and GGDEF domain proteins recruits a specific PilZ domain adaptor protein, and this complex then interacts with the pilus motor proteins PilU and PiIT. The results support a model in which DSF signalling influences motility through the highly regulated dynamic interaction of proteins that affect pilus action. A specific motif that we identify to be required for HD-GYP domain interaction is conserved in a number of GGDEF domain proteins, suggesting that regulation via interdomain interactions is of broad relevance.