Structure of the active GGEEF domain of a diguanylate cyclase from Vibrio cholerae

2020 ◽  
Vol 523 (2) ◽  
pp. 287-292 ◽  
Author(s):  
Om Prakash Chouhan ◽  
Yvette Roske ◽  
Udo Heinemann ◽  
Sumit Biswas
Keyword(s):  
Vibrio Cholerae ◽  
Diguanylate Cyclase

scholarly journals Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Min Xu ◽  
Yi-Zhi Wang ◽  
Xiu-An Yang ◽  
Tao Jiang ◽  
Wei Xie
Keyword(s):  
Vibrio Cholerae ◽  
Structural Studies ◽  
Diguanylate Cyclase

N-terminal truncation of VC0395_0300 protein from Vibrio cholerae does not lead to loss of diguanylate cyclase activity

2021 ◽  
Vol 268 ◽  
pp. 106493
Author(s):  
Divya Bandekar ◽  
Swati Mohapatra ◽  
Mousumi Hazra ◽  
Saugata Hazra ◽  
Sumit Biswas
Keyword(s):  
Vibrio Cholerae ◽  
Cyclase Activity ◽  
Diguanylate Cyclase

scholarly journals Exploring Environmental Control of Cyclic di-GMP Signaling in Vibrio cholerae by Using theEx VivoLysate Cyclic di-GMP Assay (TELCA)

2013 ◽  
Vol 79 (17) ◽  
pp. 5233-5241 ◽  
Author(s):  
Benjamin J. Koestler ◽  
Christopher M. Waters
Keyword(s):  
Vibrio Cholerae ◽  
Environmental Control ◽  
Ex Vivo ◽  
Signaling Networks ◽  
Diguanylate Cyclase ◽  
Systematic Analysis ◽  
Content Type ◽  
Extracellular Signals ◽  
Novel Method ◽  
Low Cell Density

ABSTRACTVibrio choleraesenses its environment, including the surrounding bacterial community, using both the second messenger cyclic di-GMP (c-di-GMP) and quorum sensing (QS) to regulate biofilm formation and other bacterial behaviors. Cyclic di-GMP is synthesized by diguanylate cyclase (DGC) enzymes and degraded by phosphodiesterase (PDE) enzymes.V. choleraeencodes a complex network of 61 enzymes predicted to mediate changes to the levels of c-di-GMP in response to extracellular signals, and the transcription of many of these enzymes is influenced by QS. Because of the complexity of the c-di-GMP signaling system inV. cholerae, it is difficult to determine if modulation of intracellular c-di-GMP in response to different stimuli is driven primarily by changes in c-di-GMP synthesis or hydrolysis. Here, we describe a novel method, named theex vivolysate c-di-GMP assay (TELCA), that systematically measures total DGC and PDE cellular activity. We show thatV. choleraegrown in different environments exhibits significantly different intracellular levels of c-di-GMP, and we used TELCA to determine that these differences correspond to changes in both c-di-GMP synthesis and hydrolysis. Furthermore, we show that the increased concentration of c-di-GMP at low cell density is primarily due to increased DGC activity due to the DGC CdgA. Our findings highlight the idea that modulation of both total DGC and PDE activity alters the intracellular concentration of c-di-GMP, and we present a new method that is widely applicable to the systematic analysis of complex c-di-GMP signaling networks.

scholarly journals Genome-wide mapping of Vibrio cholerae VpsT binding identifies a mechanism for c-di-GMP homeostasis

2021 ◽  
Author(s):  
Thomas Guest ◽  
James Haycocks ◽  
Gemma Warren ◽  
David Grainger
Keyword(s):  
Transcription Factors ◽  
Vibrio Cholerae ◽  
Biofilm Formation ◽  
Feedback Loop ◽  
Wide Distribution ◽  
Guanosine Monophosphate ◽  
Diguanylate Cyclase ◽  
Positive Feedback Loop ◽  
Genome Wide ◽  
Dna Palindrome

Many bacteria use cyclic dimeric guanosine monophosphate (c-di-GMP) to control changes in lifestyle. The molecule, synthesised by proteins having diguanylate cyclase activity, is often a signal to transition from motile to sedentary behaviour. In Vibrio cholerae, c-di-GMP can exert its effects via the transcription factors VpsT and VpsR. Together, these proteins activate genes needed for V. cholerae to form biofilms. In this work, we have mapped the genome-wide distribution of VpsT in a search for further regulatory roles. We show that VpsT binds 23 loci and recognises a degenerate DNA palindrome having the consensus 5' W-5R-4[CG]-3Y-2W-1W+1R+2[GC]+3Y+4W+5-3'. Most genes targeted by VpsT encode functions related to motility, biofilm formation, or c-di-GMP metabolism. Most notably, VpsT activates expression of the vpvABC operon that encodes a diguanylate cyclase. This creates a positive feedback loop needed to maintain intracellular levels of c-di-GMP. Mutation of the key VpsT binding site, upstream of vpvABC, severs the loop and c-di-GMP levels fall accordingly. Hence, as well as relaying the c-di-GMP signal, VpsT impacts c-di-GMP homeostasis.

scholarly journals A Bacterial Hemerythrin Domain Regulates the Activity of a Vibrio cholerae Diguanylate Cyclase

Biochemistry ◽  
2012 ◽  
Vol 51 (43) ◽  
pp. 8563-8570 ◽  
Author(s):  
Ruth A. Schaller ◽  
Syed Khalid Ali ◽  
Karl E. Klose ◽  
Donald M. Kurtz
Keyword(s):  
Vibrio Cholerae ◽  
Diguanylate Cyclase

scholarly journals Putative protein VC0395_0300 from Vibrio cholerae is a diguanylate cyclase with a role in biofilm formation

2017 ◽  
Vol 202 ◽  
pp. 61-70 ◽  
Author(s):  
Divya Bandekar ◽  
Om Prakash Chouhan ◽  
Swati Mohapatra ◽  
Mousumi Hazra ◽  
Saugata Hazra ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Biofilm Formation ◽  
Diguanylate Cyclase ◽  
Putative Protein

scholarly journals The Vibrio cholerae Flagellar Regulatory Hierarchy Controls Expression of Virulence Factors

2009 ◽  
Vol 191 (21) ◽  
pp. 6555-6570 ◽  
Author(s):  
Khalid Ali Syed ◽  
Sinem Beyhan ◽  
Nidia Correa ◽  
Jessica Queen ◽  
Jirong Liu ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Virulence Factors ◽  
Expression Patterns ◽  
Regulatory System ◽  
Diguanylate Cyclase ◽  
Regulatory Mutants ◽  
Reverse Transcription Pcr ◽  
Transcription Profiles ◽  
Spatiotemporal Expression ◽  
Type Vi Secretion

ABSTRACT Vibrio cholerae is a motile bacterium responsible for the disease cholera, and motility has been hypothesized to be inversely regulated with virulence. We examined the transcription profiles of V. cholerae strains containing mutations in flagellar regulatory genes (rpoN, flrA, flrC, and fliA) by utilizing whole-genome microarrays. Results revealed that flagellar transcription is organized into a four-tiered hierarchy. Additionally, genes with proven or putative roles in virulence (e.g., ctx, tcp, hemolysin, and type VI secretion genes) were upregulated in flagellar regulatory mutants, which was confirmed by quantitative reverse transcription-PCR. Flagellar regulatory mutants exhibit increased hemolysis of human erythrocytes, which was due to increased transcription of the thermolabile hemolysin (tlh). The flagellar regulatory system positively regulates transcription of a diguanylate cyclase, CdgD, which in turn regulates transcription of a novel hemagglutinin (frhA) that mediates adherence to chitin and epithelial cells and enhances biofilm formation and intestinal colonization in infant mice. Our results demonstrate that the flagellar regulatory system modulates the expression of nonflagellar genes, with induction of an adhesin that facilitates colonization within the intestine and repression of virulence factors maximally induced following colonization. These results suggest that the flagellar regulatory hierarchy facilitates correct spatiotemporal expression patterns for optimal V. cholerae colonization and disease progression.

scholarly journals The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP

2014 ◽  
Vol 14 (1) ◽  
pp. 22 ◽  
Author(s):  
Jessica L Hunter ◽  
Geoffrey B Severin ◽  
Benjamin J Koestler ◽  
Christopher M Waters
Keyword(s):  
Vibrio Cholerae ◽  
Active Site ◽  
Diguanylate Cyclase

In vivo Production of Soluble Inorganic Pyrophosphatases in Two Strains of Vibrio cholerae

1970 ◽  
Vol 24 (1) ◽  
pp. 38-41
Author(s):  
Taslima Taher Lina ◽  
Mohammad Ilias
Keyword(s):  
Vibrio Cholerae ◽  
Specific Activity ◽  
Experimental Conditions ◽  
Environmental Strain ◽  
Cell Extracts ◽  
Atcc Strain ◽  
The Family ◽  
Effects Of Ph ◽  
Vibrio Cholerae O1

The in vivo production of soluble inorganic pyrophosphatases (PPases) was investigated in two strains, namely, Vibrio cholerae EM 004 (environmental strain) and Vibrio cholerae O1 757 (ATCC strain). V. cholerae is known to contain both family I and family II PPase coding sequences. The production of family I and family II PPases were determined by measuring the enzyme activity in cell extracts. The effects of pH, temperature, salinity of the growth medium on the production of soluble PPases were studied. In case of family I PPase, V. cholerae EM 004 gave the highest specific activity at pH 9.0, with 2% NaCl + 0.011% NaF and at 37°C. The strain V. cholerae O1 757 gave the highest specific activity at pH 9.0, with media containing 0% NaCl and at 37°C. On the other hand, under all the conditions family II PPase did not give any significant specific activity, suggesting that the family II PPase was not produced in vivo in either strains of V. cholerae under different experimental conditions. Keywords: Vibrio cholerae, Pyrophosphatases (PPases), Specific activityDOI: http://dx.doi.org/10.3329/bjm.v24i1.1235 Bangladesh J Microbiol, Volume 24, Number 1, June 2007, pp 38-41

Exemplar Abstract for Vibrio cholerae Pacini 1854 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Vibrio Cholerae
Sign in / Sign up

Export Citation Format

Share Document