Results 11 to 20 of about 2,948 (189)

Production of 3',3'-cGAMP by a Bdellovibrio bacteriovorus promiscuous GGDEF enzyme, Bd0367, regulates exit from prey by gliding motility.

open access: yesPLoS Genetics, 2022
Bacterial second messengers are important for regulating diverse bacterial lifestyles. Cyclic di-GMP (c-di-GMP) is produced by diguanylate cyclase enzymes, named GGDEF proteins, which are widespread across bacteria.
Rebecca C Lowry   +8 more
doaj   +2 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

The GGDEF protein Dgc2 suppresses both motility and biofilm formation in the filamentous cyanobacterium Leptolyngbya boryana

open access: yesMicrobiology Spectrum, 2023
Colony pattern formations of bacteria with motility manifest complicated morphological self-organization phenomena. Leptolyngbya boryana is a filamentous cyanobacterium, which has been used as a genetic model organism for studying metabolism including ...
Kazuma Toida   +10 more
doaj   +3 more sources

In silico comparative analysis of GGDEF and EAL domain signaling proteins from the Azospirillum genomes [PDF]

open access: yesBMC Microbiology, 2018
Background The cyclic-di-GMP (c-di-GMP) second messenger exemplifies a signaling system that regulates many bacterial behaviors of key importance; among them, c-di-GMP controls the transition between motile and sessile life-styles in bacteria. Cellular c-
Alberto Ramírez Mata   +4 more
doaj   +3 more sources

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)
openaire   +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 ...
Shi-qi An, Ji-liang Tang
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   +4 more sources

Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family [PDF]

open access: yesHeliyon
MabR (Rv2242), a PucR-type transcription factor, plays a crucial role in regulating mycolic acid biosynthesis in Mycobacterium tuberculosis. To understand its regulatory mechanisms, we determined the crystal structures of its N-terminal and C-terminal ...
Véronique Megalizzi   +8 more
doaj   +2 more sources

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