Diguanylate Cyclase GdpX6 with c-di-GMP Binding Activity Involved in the Regulation of Virulence Expression in Xanthomonas oryzae pv. oryzae
文献类型: 外文期刊
第一作者: Yan, Weiwei
作者: Yan, Weiwei;Wei, Yiming;Yu, Chao;Tian, Fang;Yang, Fenghuan;Chen, Huamin;Yan, Weiwei;Wang, Qi;Fan, Susu
作者机构:
关键词: Xanthomonas oryzae pv; oryzae 1; virulence 2; c-di-GMP 3; diguanylate cyclase 4; GGDEF domain 5
期刊名称:MICROORGANISMS ( 影响因子:4.152; )
ISSN:
年卷期: 2021 年 9 卷 3 期
页码:
收录情况: SCI
摘要: Cyclic diguanylate monophosphate (c-di-GMP) is a secondary messenger present in bacteria. The GGDEF-domain proteins can participate in the synthesis of c-di-GMP as diguanylate cyclase (DGC) or bind with c-di-GMP to function as a c-di-GMP receptor. In the genome of Xanthomonas oryzae pv. oryzae (Xoo), the causal agent of bacterial blight of rice, there are 11 genes that encode single GGDEF domain proteins. The GGDEF domain protein, PXO_02019 (here GdpX6 [GGDEF-domain protein of Xoo 6]) was characterized in the present study. Firstly, the DGC and c-di-GMP binding activity of GdpX6 was confirmed in vitro. Mutation of the crucial residues D-403 residue of the I site in GGDEF motif and E-411 residue of A site in GGDEF motif of GdpX6 abolished c-di-GMP binding activity and DGC activity of GdpX6, respectively. Additionally, deletion of gdpX6 significantly increased the virulence, swimming motility, and decreased sliding motility and biofilm formation. In contrast, overexpression of GdpX6 in wild-type PXO99(A) strain decreased the virulence and swimming motility, and increased sliding motility and biofilm formation. Mutation of the E-411 residue but not D-403 residue of the GGDEF domain in GdpX6 abolished its biological functions, indicating the DGC activity to be imperative for its biological functions. Furthermore, GdpX6 exhibited multiple subcellular localization in bacterial cells, and D-403 or E-411 did not contribute to the localization of GdpX6. Thus, we concluded that GdpX6 exhibits DGC activity to control the virulence, swimming and sliding motility, and biofilm formation in Xoo.
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