Results 161 to 170 of about 2,948 (189)
Structural Analysis of the GGDEF-EAL Domain-Containing c-di-GMP Receptor FimX [PDF]
Structure, 2009 Bacterial pathogenesis involves social behavior including biofilm formation and swarming, processes that are regulated by the bacterially unique second messenger cyclic di-GMP (c-di-GMP). Diguanylate cyclases containing GGDEF and phosphodiesterases containing EAL domains have been identified as the enzymes controlling cellular c-di-GMP levels, yet less
Marcos V A S Navarro +2 more
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Insights into Biofilm Dispersal Regulation from the Crystal Structure of the PAS-GGDEF-EAL Region of RbdA from Pseudomonas aeruginosa [PDF]
Journal of Bacteriology, 2018 © 2018 American Society for Microbiology. RbdA is a positive regulator of biofilm dispersal of Pseudomonas aeruginosa. Its cytoplasmic region (cRbdA) comprises an N-terminal Per-ARNT-Sim (PAS) domain followed by a diguanylate cyclase (GGDEF) domain and ...
Chong Wai Liew +2 more
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Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity [PDF]
FEMS Microbiology Letters, 2001 A conserved domain, called GGDEF (referring to a conserved central sequence pattern), is detected in many procaryotic proteins, often in various combinations with putative sensory-regulatory components. Most sequenced bacterial genomes contain several different GGDEF proteins.
Nora Ausmees +2 more
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Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins [PDF]
Journal of Bacteriology, 2005 ABSTRACT GGDEF domain-containing proteins have been implicated in bacterial signal transduction and synthesis of the second messenger molecule cyclic-di-GMP. A number of GGDEF proteins are involved in controlling the formation of extracellular matrices.
Roger Simm +2 more
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Cyclic Diguanylate Is a Ubiquitous Signaling Molecule in Bacteria: Insights into Biochemistry of the GGDEF Protein Domain [PDF]
Journal of Bacteriology, 2005 ABSTRACT Proteins containing GGDEF domains are encoded in the majority of sequenced bacterial genomes. In several species, these proteins have been implicated in biosynthesis of exopolysaccharides, formation of biofilms, establishment of a sessile lifestyle, surface motility, and regulation of gene expression.
Oleg V Moskvin, Mark Gomelsky
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GGDEF domain is homologous to adenylyl cyclase
Proteins: Structure, Function, and Genetics, 2000The GGDEF domain is detected in many prokaryotic proteins, most of which are of unknown function. Several bacteria carry 12-22 different GGDEF homologues in their genomes. Conducting extensive profile-based searches, we detect statistically supported sequence similarity between GGDEF domain and adenylyl cyclase catalytic domain.
J, Pei, N V, Grishin
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GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and swimming motility in Escherichia coli [PDF]
Applied Microbiology and Biotechnology, 2010 The second messenger 3'-5'-cyclic diguanylic acid (c-di-GMP) promotes biofilm formation, and c-di-GMP is synthesized by diguanylate cyclases (characterized by a GGDEF domain) and degraded by phosphodiesterases. Here, we evaluated the effect of the 12 E. coli GGDEF-only proteins on biofilm formation and motility.
Viviana Sanchez-Torres +2 more
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GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility [PDF]
Molecular Microbiology, 2004 SummaryCyclic nucleotides represent second messenger molecules in all kingdoms of life. In bacteria, mass sequencing of genomes detected the highly abundant protein domains GGDEF and EAL. We show here that the GGDEF and EAL domains are involved in the turnover of cyclic‐di‐GMP (c‐di‐GMP) in vivo whereby the GGDEF domain stimulates c‐di‐GMP production ...
Roger Simm +2 more
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[Proteins with GGDEF and EAL domains: their role in bacterial metabolism].
Revista latinoamericana de microbiologia, 2007The availability of multiple bacterial genome sequences has led to the discovery of several conserved domains of proteins. Recently, GGDEF and EAL domains have been described as domains responsible for the synthesis and degradation of c-di-GMP, a second messenger in bacteria. c-di-GMP has been involved in cellulose production and identified as a global
Micaela Marcela, Méndez-Ortiz +1 more
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Archives of Microbiology
Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger that regulates multiple bacterial behaviors. It is synthesized by diguanylate cyclase (DGC) with the GGDEF domain, and degraded by phosphodiesterase (PDE) with the EAL or HD-GYP domain. The GepA (VP0117) protein in Vibrio parahaemolyticus contains both GGDEF and EAL domains, but its role
Miaomiao, Zhang +7 more
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Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger that regulates multiple bacterial behaviors. It is synthesized by diguanylate cyclase (DGC) with the GGDEF domain, and degraded by phosphodiesterase (PDE) with the EAL or HD-GYP domain. The GepA (VP0117) protein in Vibrio parahaemolyticus contains both GGDEF and EAL domains, but its role
Miaomiao, Zhang +7 more
openaire +2 more sources