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Updated: Jun 5, 2026

A Hydroponic Co-cultivation System for Simultaneous and Systematic Analysis of Plant/Microbe Molecular Interactions and Signaling
Published on: July 22, 2017
Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction in
1BIOMERIT Research Centre, Department of Microbiology, BioSciences Institute, University College Cork, Cork, Ireland. r.ryan@ucc.ie
Abstract:
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.
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