The HD-GYP Domain, Cyclic Di-GMP Signaling, and Bacterial Virulence to Plants [PDF]
Molecular Plant-Microbe Interactions, 2006 Cyclic di-GMP is an almost ubiquitous second messenger in bacteria that was first described as an allosteric activator of cellulose synthase but is now known to regulate a range of functions, including virulence in human and animal pathogens. Two protein
J. Maxwell Dow +3 more
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A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae. [PDF]
BMC Microbiol, 2014 Background The second messenger cyclic diguanylate (c-di-GMP) plays a central role in bacterial adaptation to extracellular stimuli, controlling processes such as motility, biofilm development, cell development and, in some pathogens, virulence.
McKee RW +4 more
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Gas-Selective Catalytic Regulation by a Newly Identified Globin-Coupled Sensor Phosphodiesterase Containing an HD-GYP Domain from the Human Pathogen Vibrio fluvialis. [PDF]
BiochemistryGlobin-coupled sensors constitute an important family of heme-based gas sensors, an emerging class of heme proteins. In this study, we have identified and characterized a globin-coupled sensor phosphodiesterase containing an HD-GYP domain (GCS-HD-GYP ...
Kitanishi K, Aoyama N, Shimonaka M.
europepmc +4 more sources
Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. [PDF]
Mol Microbiol, 2014 Bis-(3',5') cyclic di-guanylate (c-di-GMP) is a key bacterial second messenger that is implicated in the regulation of many crucial processes that include biofilm formation, motility and virulence.
Bellini D +7 more
europepmc +8 more sources
Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris. [PDF]
Proc Natl Acad Sci U S A, 2010 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.
Ryan RP +5 more
europepmc +7 more sources
Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site. [PDF]
J Bacteriol, 2015 The intracellular level of the bacterial secondary messenger cyclic di 3 amp; 8242;,5 amp; 8242; GMP c di GMP is determined by a balance between its biosynthesis and degradation, the latter achieved via dedicated phosphodiesterases PDEs bearing a ...
Rinaldo S +9 more
europepmc +5 more sources
Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction in Xanthomonas campestris [PDF]
Virulence, 2010 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 ...
Robert P. Ryan +3 more
core +4 more sources
Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris [PDF]
Molecular microbiology, 2012 RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris, RpfG together with the sensor kinase RpfC regulates multiple factors as a ...
Dow, J. Maxwell +6 more
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Microbiology Research, 2018 RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris pv.
Shi-qi An, Ji-liang Tang
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HD-GYP domain proteins regulate biofilm formation and virulence in Pseudomonas aeruginosa
Environmental Microbiology, 2009 HD-GYP is a protein domain involved in the hydrolysis of the bacterial second messenger cyclic-di-GMP. The genome of the human pathogen Pseudomonas aeruginosa PAO1 encodes two proteins (PA4108, PA4781) with an HD-GYP domain and a third protein, PA2572 ...
Dow, J. Maxwell +15 more
core +4 more sources