The Degenerate EAL-GGDEF Domain Protein Flip Functions as a Cyclic di-GMP Receptor and Specifically Interacts with the PilZ-Domain Protein PXO_02715 to Regulate Virulence in Xanthomonas oryzae pv. oryzae

文献类型： 外文期刊

第一作者： Tian, Fang

作者： Tian, Fang;Li, Xiaotong;Fan, Susu;Chen, Huamin;Wu, Maosen;He, Chenyang;Yang, Ching-Hong

作者机构：

期刊名称：MOLECULAR PLANT-MICROBE INTERACTIONS （ 影响因子：4.171； 五年影响因子：4.836 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Degenerate GGDEF and EAL domain proteins represent major types of cyclic diguanylic acid (c-di-GMP) receptors in pathogenic bacteria. Here, we characterized a FimX-like protein (Filp) which possesses both GGDEF and EAL domains in Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight of rice. Both in silico analysis and enzyme assays indicated that the GGDEF and EAL domains of Filp were degenerate and enzymatically inactive. However, Filp bound to c-di-GMP efficiently within the EAL domain, where Q(477), E-653, and F-654 residues were crucial for the binding. Deletion of the flip gene in X. oryzae pv. oryzae resulted in attenuated virulence in rice and reduced type III secretion system (T3SS) gene expression. Complementation analysis with different truncated proteins indicated that REC, PAS, and EAL domains but not the GGDEF domain were required for the full activity of Filp in vivo. In addition, a PilZ-domain protein (PXO_02715) was identified as a Filp interactor by yeast two-hybrid and glutathione-S-transferase pull-down assays. Deletion of the PXO_02715 gene demonstrated changes in bacterial virulence and T3SS gene expression similar to Delta filp. Moreover, both mutants were impaired in their ability to induce hypersensitive response in nonhost plants. Thus, we concluded that Filp was a novel c-di-GMP receptor of X. oryzae pv. oryzae, and its function to regulate bacterial virulence expression might be via the interaction with PXO_02715.

分类号： Q94

  • 相关文献
作者其他论文 更多>>

微信小程序