Results 171 to 180 of about 4,652 (199)

Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3′, 3′-cGAMP) [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2016
Significance Cyclic di-GMP (cdiG) is an important bacterial signaling molecule because it regulates motility and affects surface colonization and biofilm formation. It has long been established that cdiG is made by GGDEF enzymes, which are named after five conserved amino acids in the catalytic domain.
Zachary Francis Hallberg, Beiyan Nan, Ming C Hammond   +2 more
exaly   +7 more sources

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, Ute Römling
exaly   +4 more sources

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 Navarro, Nabanita De, Holger Sondermann   +2 more
exaly   +3 more sources

A Staphylococcal GGDEF Domain Protein Regulates Biofilm Formation Independently of Cyclic Dimeric GMP [PDF]

Journal of Bacteriology, 2008
ABSTRACTCyclic dimeric GMP (c-di-GMP) is an important biofilm regulator that allosterically activates enzymes of exopolysaccharide biosynthesis. Proteobacterial genomes usually encode multiple GGDEF domain-containing diguanylate cyclases responsible for c-di-GMP synthesis.
Sinead O'Donnell, Paul D Fey, Mark Gomelsky   +2 more
exaly   +3 more sources

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.
Thomas K Wood, Hongbo Hu
exaly   +3 more sources

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, Manfred Nimtz, Ute Römling
exaly   +3 more sources

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GGDEF domain is homologous to adenylyl cyclase

Proteins: Structure, Function, and Genetics, 2000
The 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
openaire   +2 more sources

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 Moskvin, Mark Gomelsky
exaly   +3 more sources

Phenotypic–genotypic analysis of GGDEF/EAL/HD‐GYP domain‐encoding genes in Pseudomonas putida

Environmental Microbiology Reports, 2019
Summary 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, Yujie Xiao, Jinzhi He, Huizhong Liu, Liang Nie, Wenli Chen, Qiaoyun Huang   +6 more
openaire   +2 more sources

Tandem GGDEF–EAL Domain Proteins Pleiotropically Modulate c-di-GMP Metabolism Enrolled in Bacterial Cellulose Biosynthesis

Journal of Agricultural and Food Chemistry
Cyclic diguanosine monophosphate (c-di-GMP) is a crucial secondary messenger that regulates bacterial cellulose (BC) synthesis. It is synthesized by diguanylate cyclase (DGC) containing a Gly-Gly-Asp/Glu-Glu-Phe (GGDEF) domain and degraded by phosphodiesterase (PDE) with a Glu-Ala-Leu (EAL) domain.
Cheng Zhong
exaly   +3 more sources