Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris.

Journal article

RpfG is a paradigm for a class of widespread bacterial two-component regulators with a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. 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 diffusible signaling factor (DSF), which is essential for cell-cell signaling. RpfF ...

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Authors: Ryan, R; McCarthy, Y; Andrade, M; Farah, C; Armitage, J

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 107
• Issue: 13
• Pages: 5989-5994
• Publication date: 2010-03-01
• DOI: 10.1073/pnas.0912839107
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Amino Acid Substitution; Mutagenesis, Site-Directed; Xanthomonas campestris; Recombinant Proteins; Bacterial Proteins; Protein Structure, Tertiary; Plants; Two-Hybrid System Techniques; Signal Transduction; Fluorescence Resonance Energy Transfer; Protein Interaction Domains and Motifs; Virulence; Microbial Interactions