Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity

Ausmees, Nora

doi:10.1016/s0378-1097(01)00394-9

Cited by 86 publications

(119 citation statements)

References 22 publications

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“…Although genetic data suggested that a PleD homolog in Rhizobium had DGC activity (Ausmees et al 2001), the following evidence presented in this work strongly suggests that the GGDEF domain of PleD possesses DGC, but no PDE activity: First, in vitro synthesis of c-di-GMP with C. crescentus cell extracts is dependent on the presence of a constitutively active form of PleD. Second, purified PleD protein is able to efficiently convert GTP into a nucleotide species with a molecular mass corresponding exactly to that expected for c-di-GMP.…”

Section: Discussionmentioning

confidence: 99%

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain

Paul¹,

Weiser²,

Amiot³

et al. 2004

Genes Dev.

559

662

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Pole development is coordinated with the Caulobacter crescentus cell cycle by two-component signaling proteins. We show that an unusual response regulator, PleD, is required for polar differentiation and is sequestered to the cell pole only when it is activated by phosphorylation. Dynamic localization of PleD to the cell pole provides a mechanism to temporally and spatially control the signaling output of PleD during development. Targeting of PleD to the cell pole is coupled to the activation of a C-terminal guanylate cyclase domain, which catalyzes the synthesis of cyclic di-guanosine monophosphate. We propose that the local action of this novel-type guanylate cyclase might constitute a general regulatory principle in bacterial growth and development. During developmental transitions, localized changes of cellular morphology are mediated by adaptation in levels and arrangement of proteins. Temporal and spatial control often relies on the timed synthesis or activation of transcriptional regulators and on the establishment of gradients through the compartmentalization of signaling complexes. Although the regulatory mechanisms of gene expression are relatively well understood, it is often not clear how morphogenetic changes are controlled and coordinated locally. In prokaryotes, the major paradigm for signal transduction is the two-component regulatory system (Parkinson and Kofoid 1992). On signal input, the first component, a sensor kinase, autophosphorylates on a histidine residue. The second component, a soluble response regulator, often functions as a transcriptional regulator. Its phosphorylation by the cognate histidine kinase on a conserved aspartate residue in the N-terminal receiver domain usually results in increased DNA binding affinity (Parkinson and Kofoid 1992). Here we present evidence that a novel-type response regulator acts at a distinct subcellular site where it contributes to local changes in cell morphology through the production of a novel signaling molecule.The unicellular bacterium Caulobacter crescentus goes through an obligate developmental transition that allows it to switch between a sessile, adhesive, and a motile, planktonic cell during its cell cycle. As a consequence, cell poles are continuously remodeled during cell differentiation to facilitate assembly and removal of motility and surface adherence organelles at the right time and in the correct order. Asymmetry is established in the predivisional cell with a single flagellum, a chemotaxis machinery, and pili being assembled at one pole, whereas the opposite pole consists of a stalk and an adhesive organelle, the holdfast (Fig. 1). As a result, division generates two cell types with distinct properties: a surface-attached stalked cell and a motile swarmer cell. The swarmer progeny first differentiates into a stalked cell before it initiates DNA replication and cell division. During this transition the pili retract, flagella are released, and the adhesive organelles are synthesized at the same pole. Here we investigate the function...

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Section: Discussionmentioning

confidence: 99%

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain

Paul¹,

Weiser²,

Amiot³

et al. 2004

Genes Dev.

559

662

View full text Add to dashboard Cite

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“…The intracellular concentration of c-di-GMP is regulated by the opposing activities of diguanylate cyclase (DGC) and phosphodiesterase A (PDEA) enzymes (14,15). DGCs catalyze formation of c-di-GMP through the 3Ј to 5Ј linkage of two GTP molecules into a cyclic molecule releasing two pyrophosphate molecules.…”

Section: Bis(3ј5ј)-cyclic Diguanylic Acid (C-di-gmp)mentioning

confidence: 99%

PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

Pratt

Tamayo

Tischler³

et al. 2007

Journal of Biological Chemistry

180

205

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Cyclic diguanylate (c-di-GMP) is an allosteric activator and second messenger implicated in the regulation of a variety of biological processes in diverse bacteria. In Vibrio cholerae, c-di-GMP has been shown to inversely regulate biofilm-specific and virulence gene expression, suggesting that c-di-GMP signaling is important for the transition of V. cholerae from the environment to the host. However, the mechanism behind this regulation remains unknown. Recently, it was proposed that the PilZ protein domain represents a c-di-GMP-binding domain. Here we show that V. cholerae PilZ proteins bind c-di-GMP specifically and are involved in the regulation of biofilm formation, motility, and virulence. These findings confirm a role for PilZ proteins as c-di-GMP-sensing proteins within the c-di-GMP signaling network.

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“…There are 12 genes encoding proteins containing the GGDEF motif, seven of which are organized in tandem in chromosome I (LIC11131 to LIC11125), and they also have a PAS/ PAC sensor domain in the amino-terminal region, suggesting that they are the product of gene duplication. The diguanylate cyclase activity of the GGDEF domain is required for a novel regulatory mechanism involving bis-(2',5')-cyclic diguanylic acid (c-di-GMP) as an allosteric activator (28). Two of the GGDEF-containing proteins also have the Cache domain, which is involved in chemotaxis signal transduction (29), an important feature for Leptospira.…”

Section: Regulatory Systems and Signal Transductionmentioning

confidence: 99%

Genome features of Leptospira interrogans serovar Copenhageni

Nascimento

Verjovski-Almeida

Sluys

et al. 2004

Braz J Med Biol Res

194

183

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We report novel features of the genome sequence of Leptospira interrogans serovar Copenhageni, a highly invasive spirochete. Leptospira species colonize a significant proportion of rodent populations worldwide and produce life-threatening infections in mammals. Genomic sequence analysis reveals the presence of a competent transport system with 13 families of genes encoding for major transporters including a three-member component efflux system compatible with the long-term survival of this organism. The leptospiral genome contains a broad array of genes encoding regulatory system, signal transduction and methyl-accepting chemotaxis proteins, reflecting the organism's ability to respond to diverse environmental stimuli. The identification of a complete set of genes encoding the enzymes for the cobalamin biosynthetic pathway and the novel coding genes related to lipopolysaccharide biosynthesis should bring new light to the study of Leptospira physiology. Genes related to toxins, lipoproteins and several surface-exposed proteins may facilitate a better understanding of the Leptospira pathogenesis and may serve as potential candidates for vaccine.

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Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity

Cited by 86 publications

References 22 publications

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain

PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

Genome features of Leptospira interrogans serovar Copenhageni

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