Results 21 to 30 of about 3,106 (185)

GGDEF-EAL domain proteins in bacterial physiology

open access: yes, 2008
GGDEF and EAL domain proteins were identified in the chromosome of many bacteria. GGDEF domain proteins are generally diguanyl cyclases which synthesize the secondary messenger cyclic di-GMP. EAL domain proteins are generally c-di-GMP specific phosphodiesterase which degrade c-di-GMP.
Abdul Kader (33837)
core   +3 more sources

Dual-function enzyme acts as a global c-di-GMP sink and local anti sigma factor antagonist to drive cellular differentiation. [PDF]

open access: yesPLoS Genetics
Soil bacteria of the genus Streptomyces are natural producers of over two-thirds of clinically used antibiotics. Their ability to generate these valuable metabolites is tightly linked to a developmental program involving the transition from vegetative ...
Buse Cınar Cakmak   +7 more
doaj   +2 more sources

Expression Patterns, Genomic Conservation and Input Into Developmental Regulation of the GGDEF/EAL/HD-GYP Domain Proteins in Streptomyces [PDF]

open access: yesFrontiers in Microbiology, 2018
To proliferate, antibiotic-producing Streptomyces undergo a complex developmental transition from vegetative growth to the production of aerial hyphae and spores.
Mahmoud M. Al-Bassam   +4 more
doaj   +2 more sources

Systematic Analysis of Two Tandem GGDEF/EAL Domain Genes Regulating Antifungal Activities in Pseudomonas glycinae MS82

open access: yesHorticulturae, 2023
Cyclic diguanylate (c-di-GMP) affects bacterial physiological and biochemical functions like biofilm, motility, virulence, and bacterial secretion systems. GGDEF/EAL-domain proteins, participating in c-di-GMP synthesis and degradation, are widely present
Jinsheng Lin   +8 more
doaj   +2 more sources

Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain protein STM3615. [PDF]

open access: yesPLoS ONE, 2014
In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is controlled by the cytoplasmic intracellular small-molecular second messenger cyclic 3', 5'-di- guanosine monophosphate (c-di-GMP) through the activities of GGDEF and EAL ...
Naeem Anwar   +3 more
doaj   +2 more sources

Discovery of Novel c-di-GMP-Related Genes in Leptospira interrogans [PDF]

open access: yesPathogens
Cyclic di-GMP (bis-(3′→5′) cyclic dimeric guanosine monophosphate) is a ubiquitous bacterial second messenger that regulates a wide range of cellular processes, including biofilm formation, motility, virulence, and environmental adaptation.
Anielle Salviano de Almeida Ferrari   +9 more
doaj   +2 more sources

Systematic Nomenclature for GGDEF and EAL Domain-Containing Cyclic Di-GMP Turnover Proteins of Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 2016
ABSTRACT In recent years, Escherichia coli has served as one of a few model bacterial species for studying cyclic di-GMP (c-di-GMP) signaling. The widely used E. coli K-12 laboratory strains possess 29 genes encoding proteins with GGDEF and/or EAL domains, which include 12 ...
Hengge, Regine   +7 more
openaire   +7 more sources

Formation of a complex between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris

open access: yesMicrobiology 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. campestris (Xcc), RpfG together with the sensor kinase RpfC regulates the synthesis of a range of virulence factors as a response to the cell-cell Diffusible Signaling ...
An, Shi-qi, Tang, Ji-liang
openaire   +3 more sources

A systematic analysis of the role of GGDEF-EAL domain proteins in virulence and motility in Xanthomonas oryzae pv. oryzicola [PDF]

open access: yesScientific Reports, 2016
AbstractThe second messenger c-di-GMP is implicated in regulation of various aspects of the lifestyles and virulence of Gram-negative bacteria. Cyclic di-GMP is formed by diguanylate cyclases with a GGDEF domain and degraded by phosphodiesterases with either an EAL or HD-GYP domain.
Wei, Chao   +8 more
openaire   +5 more sources

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