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HD‐GYP domain proteins regulate biofilm formation and virulence in Pseudomonas aeruginosa
Environmental Microbiology, 2009Summary 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, which contains
Ryan, Robert P +6 more
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Structure and Function of HD-GYP Phosphodiesterases
2020HD-GYPs represent the least abundant, and somewhat mysterious, class of dedicated cyclic di-GMP phosphodiesterases (PDE). They are metal dependent enzymes, belonging to the HD phosphohydrolase superfamily, and are evolutionarily unrelated to the EAL class of cyclic di-GMP dedicated PDEs.
Rinaldo S. +4 more
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Phenotypic–genotypic analysis of GGDEF/EAL/HD‐GYP domain‐encoding genes in Pseudomonas putida
Environmental Microbiology Reports, 2019Summary Cyclic diguanylate (c‐di‐GMP) is a broadly conserved bacterial signalling molecule that modulates diverse cellular processes, such as biofilm formation, colony morphology and swimming motility. The intracellular level of c‐di‐GMP is controlled by diguanylate cyclases (DGCs) with GGDEF domain and ...
Hailing Nie +6 more
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Biochemistry, 2020
The second messenger bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates numerous important physiological functions in bacteria. In this study, we identified and characterized the first dimeric, full-length, non-heme iron-bound phosphodiesterase (PDE) containing bacterial hemerythrin and HD-GYP domains (Bhr-HD-GYP). We found that the
Kenichi Kitanishi +3 more
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The second messenger bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates numerous important physiological functions in bacteria. In this study, we identified and characterized the first dimeric, full-length, non-heme iron-bound phosphodiesterase (PDE) containing bacterial hemerythrin and HD-GYP domains (Bhr-HD-GYP). We found that the
Kenichi Kitanishi +3 more
openaire +2 more sources
The HD-GYP Domain and Cyclic Di-GMP Signaling
2014A role for the HD-GYP domain in c-di-GMP hydrolysis was then proposed based on examination of the distribution and numbers of GGDEF, EAL, and HD-GYP domains encoded by different bacterial genomes, coupled with the known activities of other members of the HD superfamily of enzymes as metal-dependent hydrolases.
Robert P. Ryan +2 more
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Cyclic di-GMP Signaling Gone Astray: Cyclic GAMP Signaling via Hypr GGDEF and HD-GYP Enzymes
2020GGDEF domain and HD-GYP enzymes are classically associated with cyclic di-GMP signaling. Here we describe our current knowledge of variants of these enzyme classes that instead are involved in cyclic GMP-AMP (cGAMP) signaling, including their discovery, recent elucidation of signature active site residues, specific phenotypes, and regulatory mechanisms.
Todd A. Wright +2 more
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Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, 2013
Brendan Wren, Ozan Gundogdu
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Brendan Wren, Ozan Gundogdu
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