| Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris. | |
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MedLine Citation:
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PMID: 20231439 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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 is involved in synthesizing DSF, and mutations of rpfF, rpfG, or rpfC lead to a coordinate reduction in the synthesis of virulence factors such as extracellular enzymes, biofilm structure, and motility. Using yeast two-hybrid analysis and fluorescence resonance energy transfer experiments in Xcc, we show that the physical interaction of RpfG with two proteins with diguanylate cyclase (GGDEF) domains controls a subset of RpfG-regulated virulence functions. RpfG interactions were abolished by alanine substitutions of the three residues of the conserved GYP motif in the HD-GYP domain. Changing the GYP motif or deletion of the two GGDEF-domain proteins reduced Xcc motility but not the synthesis of extracellular enzymes or biofilm formation. RpfG-GGDEF interactions are dynamic and depend on DSF signaling, being reduced in the rpfF mutant but restored by DSF addition. The results are consistent with a model in which DSF signal transduction controlling motility depends on a highly regulated, dynamic interaction of proteins that influence the localized expression of cyclic di-GMP. |
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Authors:
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Robert P Ryan; Yvonne McCarthy; Maxuel Andrade; Chuck S Farah; Judith P Armitage; J Maxwell Dow |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-03-15 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 107 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2010 Mar |
Date Detail:
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Created Date: 2010-04-01 Completed Date: 2010-04-28 Revised Date: 2010-10-01 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 5989-94 Citation Subset: IM |
Affiliation:
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Department of Microbiology, BIOMERIT Research Centre, BioSciences Institute, University College Cork, Cork, Ireland. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution Bacterial Proteins / chemistry, genetics, physiology Fluorescence Resonance Energy Transfer Microbial Interactions Mutagenesis, Site-Directed Plants / microbiology Protein Interaction Domains and Motifs Protein Structure, Tertiary Recombinant Proteins / chemistry, genetics, metabolism Signal Transduction Two-Hybrid System Techniques Virulence / genetics, physiology Xanthomonas campestris / genetics, pathogenicity*, physiology* |
| Grant Support | |
ID/Acronym/Agency:
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//Biotechnology and Biological Sciences Research Council |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Recombinant Proteins; 0/RpfG protein, Xanthomonas campestris |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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