Relevant bibliographies by topics / GGDEF / Journal articles
To see the other types of publications on this topic, follow the link: GGDEF.

Journal articles on the topic 'GGDEF'

Author: Grafiati
Published: 4 June 2021
Last updated: 22 February 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'GGDEF.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Holland, Linda M., Sinéad T. O'Donnell, Dmitri A. Ryjenkov, Larissa Gomelsky, Shawn R. Slater, Paul D. Fey, Mark Gomelsky, and James P. O'Gara. "A Staphylococcal GGDEF Domain Protein Regulates Biofilm Formation Independently of Cyclic Dimeric GMP." Journal of Bacteriology 190, no. 15 (May 23, 2008): 5178–89. http://dx.doi.org/10.1128/jb.00375-08.

Full text
Abstract:
ABSTRACT Cyclic 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. In contrast, only one conserved GGDEF domain protein, GdpS (for GGDEF domain protein from Staphylococcus), and a second protein with a highly modified GGDEF domain, GdpP, are present in the sequenced staphylococcal genomes. Here, we investigated the role of GdpS in biofilm formation in Staphylococcus epidermidis. Inactivation of gdpS impaired biofilm formation in medium supplemented with NaCl under static and flow-cell conditions, whereas gdpS overexpression complemented the mutation and enhanced wild-type biofilm development. GdpS increased production of the icaADBC-encoded exopolysaccharide, poly-N-acetyl-glucosamine, by elevating icaADBC mRNA levels. Unexpectedly, c-di-GMP synthesis was found to be irrelevant for the ability of GdpS to elevate icaADBC expression. Mutagenesis of the GGEEF motif essential for diguanylate cyclase activity did not impair GdpS, and the N-terminal fragment of GdpS lacking the GGDEF domain partially complemented the gdpS mutation. Furthermore, heterologous diguanylate cyclases expressed in trans failed to complement the gdpS mutation, and the purified GGDEF domain from GdpS possessed no diguanylate cyclase activity in vitro. The gdpS gene from Staphylococcus aureus exhibited similar characteristics to its S. epidermidis ortholog, suggesting that the GdpS-mediated signal transduction is conserved in staphylococci. Therefore, GdpS affects biofilm formation through a novel c-di-GMP-independent mechanism involving increased icaADBC mRNA levels and exopolysaccharide biosynthesis. Our data raise the possibility that staphylococci cannot synthesize c-di-GMP and have only remnants of a c-di-GMP signaling pathway.
APA, Harvard, Vancouver, ISO, and other styles
2

Ryjenkov, Dmitri A., Marina Tarutina, Oleg V. Moskvin, and Mark Gomelsky. "Cyclic Diguanylate Is a Ubiquitous Signaling Molecule in Bacteria: Insights into Biochemistry of the GGDEF Protein Domain." Journal of Bacteriology 187, no. 5 (March 1, 2005): 1792–98. http://dx.doi.org/10.1128/jb.187.5.1792-1798.2005.

Full text
Abstract:
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. However, biochemical activities of only a few GGDEF domain proteins have been tested. These proteins were shown to be involved in either synthesis or hydrolysis of cyclic-bis(3′→5′) dimeric GMP (c-di-GMP) or in hydrolysis of cyclic AMP. To investigate specificity of the GGDEF domains in Bacteria, six GGDEF domain-encoding genes from randomly chosen representatives of diverse branches of the bacterial phylogenetic tree, i.e., Thermotoga, Deinococcus-Thermus, Cyanobacteria, spirochetes, and α and γ divisions of the Proteobacteria, were cloned and overexpressed. All recombinant proteins were purified and found to possess diguanylate cyclase (DGC) activity involved in c-di-GMP synthesis. The individual GGDEF domains from two proteins were overexpressed, purified, and shown to possess a low level of DGC activity. The oligomeric states of full-length proteins and individual GGDEF domains were similar. This suggests that GGDEF domains are sufficient to encode DGC activity; however, enzymatic activity is highly regulated by the adjacent sensory protein domains. It is shown that DGC activity of the GGDEF domain protein Rrp1 from Borrelia burgdorferi is strictly dependent on phosphorylation status of its input receiver domain. This study establishes that majority of GGDEF domain proteins are c-di-GMP specific, that c-di-GMP synthesis is a wide-spread phenomenon in Bacteria, and that it is highly regulated.
APA, Harvard, Vancouver, ISO, and other styles
3

Hallberg, Zachary F., Xin C. Wang, Todd A. Wright, Beiyan Nan, Omer Ad, Jongchan Yeo, and Ming C. Hammond. "Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3′, 3′-cGAMP)." Proceedings of the National Academy of Sciences 113, no. 7 (February 2, 2016): 1790–95. http://dx.doi.org/10.1073/pnas.1515287113.

Full text
Abstract:
Over 30 years ago, GGDEF domain-containing enzymes were shown to be diguanylate cyclases that produce cyclic di-GMP (cdiG), a second messenger that modulates the key bacterial lifestyle transition from a motile to sessile biofilm-forming state. Since then, the ubiquity of genes encoding GGDEF proteins in bacterial genomes has established the dominance of cdiG signaling in bacteria. However, the observation that proteobacteria encode a large number of GGDEF proteins, nearing 1% of coding sequences in some cases, raises the question of why bacteria need so many GGDEF enzymes. In this study, we reveal that a subfamily of GGDEF enzymes synthesizes the asymmetric signaling molecule cyclic AMP-GMP (cAG or 3′, 3′-cGAMP). This discovery is unexpected because GGDEF enzymes function as symmetric homodimers, with each monomer binding to one substrate NTP. Detailed analysis of the enzyme from Geobacter sulfurreducens showed it is a dinucleotide cyclase capable of switching the major cyclic dinucleotide (CDN) produced based on ATP-to-GTP ratios. We then establish through bioinformatics and activity assays that hybrid CDN-producing and promiscuous substrate-binding (Hypr) GGDEF enzymes are found in other deltaproteobacteria. Finally, we validated the predictive power of our analysis by showing that cAG is present in surface-grown Myxococcus xanthus. This study reveals that GGDEF enzymes make alternative cyclic dinucleotides to cdiG and expands the role of this widely distributed enzyme family to include regulation of cAG signaling.
APA, Harvard, Vancouver, ISO, and other styles
4

Simm, Roger, Astrid Lusch, Abdul Kader, Mats Andersson, and Ute Römling. "Role of EAL-Containing Proteins in Multicellular Behavior of Salmonella enterica Serovar Typhimurium." Journal of Bacteriology 189, no. 9 (February 23, 2007): 3613–23. http://dx.doi.org/10.1128/jb.01719-06.

Full text
Abstract:
ABSTRACT GGDEF and EAL domain proteins are involved in turnover of the novel secondary messenger cyclic di(3′→5′)-guanylic acid (c-di-GMP) in many bacteria. The rdar morphotype, a multicellular behavior of Salmonella enterica serovar Typhimurium characterized by the expression of the extracellular matrix components cellulose and curli fimbriae is controlled by c-di-GMP. In this work the roles of the EAL and GGDEF-EAL domain proteins on rdar morphotype development were investigated. Knockout of four of 15 EAL and GGDEF-EAL domain proteins upregulated rdar morphotype expression and expression of CsgD, the central regulator of the rdar morphotype, and partially downregulated c-di-GMP concentrations. More-detailed analysis showed that the EAL domain protein STM4264 and the GGDEF-EAL domain protein STM1703, which highly downregulated the rdar morphotype, have overlapping yet distinct functions. Another subset of EAL and GGDEF-EAL domain proteins influenced multicellular behavior in liquid culture and flagellum-mediated motility. Consequently, this work has shown that several EAL and GGDEF-EAL domain proteins, which act as phosphodiesterases, play a determinative role in the expression level of multicellular behavior of Salmonella enterica serovar Typhimurium.
APA, Harvard, Vancouver, ISO, and other styles
5

Yan, Weiwei, Yiming Wei, Susu Fan, Chao Yu, Fang Tian, Qi Wang, Fenghuan Yang, and Huamin Chen. "Diguanylate Cyclase GdpX6 with c-di-GMP Binding Activity Involved in the Regulation of Virulence Expression in Xanthomonas oryzae pv. oryzae." Microorganisms 9, no. 3 (February 26, 2021): 495. http://dx.doi.org/10.3390/microorganisms9030495.

Full text
Abstract:
Cyclic diguanylate monophosphate (c-di-GMP) is a secondary messenger present in bacteria. The GGDEF-domain proteins can participate in the synthesis of c-di-GMP as diguanylate cyclase (DGC) or bind with c-di-GMP to function as a c-di-GMP receptor. In the genome of Xanthomonas oryzae pv. oryzae (Xoo), the causal agent of bacterial blight of rice, there are 11 genes that encode single GGDEF domain proteins. The GGDEF domain protein, PXO_02019 (here GdpX6 [GGDEF-domain protein of Xoo6]) was characterized in the present study. Firstly, the DGC and c-di-GMP binding activity of GdpX6 was confirmed in vitro. Mutation of the crucial residues D403 residue of the I site in GGDEF motif and E411 residue of A site in GGDEF motif of GdpX6 abolished c-di-GMP binding activity and DGC activity of GdpX6, respectively. Additionally, deletion of gdpX6 significantly increased the virulence, swimming motility, and decreased sliding motility and biofilm formation. In contrast, overexpression of GdpX6 in wild-type PXO99A strain decreased the virulence and swimming motility, and increased sliding motility and biofilm formation. Mutation of the E411 residue but not D403 residue of the GGDEF domain in GdpX6 abolished its biological functions, indicating the DGC activity to be imperative for its biological functions. Furthermore, GdpX6 exhibited multiple subcellular localization in bacterial cells, and D403 or E411 did not contribute to the localization of GdpX6. Thus, we concluded that GdpX6 exhibits DGC activity to control the virulence, swimming and sliding motility, and biofilm formation in Xoo.
APA, Harvard, Vancouver, ISO, and other styles
6

Mantoni, Federico, Chiara Scribani Rossi, Alessandro Paiardini, Adele Di Matteo, Loredana Cappellacci, Riccardo Petrelli, Massimo Ricciutelli, et al. "Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts." Life 11, no. 1 (January 6, 2021): 31. http://dx.doi.org/10.3390/life11010031.

Full text
Abstract:
GGDEF-containing proteins respond to different environmental cues to finely modulate cyclic diguanylate (c-di-GMP) levels in time and space, making the allosteric control a distinctive trait of the corresponding proteins. The diguanylate cyclase mechanism is emblematic of this control: two GGDEF domains, each binding one GTP molecule, must dimerize to enter catalysis and yield c-di-GMP. The need for dimerization makes the GGDEF domain an ideal conformational switch in multidomain proteins. A re-evaluation of the kinetic profile of previously characterized GGDEF domains indicated that they are also able to convert GTP to GMP: this unexpected reactivity occurs when conformational issues hamper the cyclase activity. These results create new questions regarding the characterization and engineering of these proteins for in solution or structural studies.
APA, Harvard, Vancouver, ISO, and other styles
7

Sommerfeldt, Nicole, Alexandra Possling, Gisela Becker, Christina Pesavento, Natalia Tschowri, and Regine Hengge. "Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli." Microbiology 155, no. 4 (April 1, 2009): 1318–31. http://dx.doi.org/10.1099/mic.0.024257-0.

Full text
Abstract:
Switching from the motile planktonic bacterial lifestyle to a biofilm existence is stimulated by the signalling molecule bis-(3′-5′)-cyclic-diguanosine monophosphate (cyclic-di-GMP), which is antagonistically controlled by diguanylate cyclases (DGCs; characterized by GGDEF domains) and specific phosphodiesterases (PDEs; mostly featuring EAL domains). Here, we present the expression patterns of all 28 genes that encode GGDEF/EAL domain proteins in Escherichia coli K-12. Twenty-one genes are expressed in Luria–Bertani medium, with 15 being under σ S control. While a small subset of GGDEF/EAL proteins (YeaJ and YhjH) is dominant and modulates motility in post-exponentially growing cells, a diverse battery of GGDEF/EAL proteins is deployed during entry into stationary phase, especially in cells grown at reduced temperature (28 °C). This suggests that multiple signal input into cyclic-di-GMP control is particularly important in growth-restricted cells in an extra-host environment. Six GGDEF/EAL genes differentially control the expression of adhesive curli fimbriae. Besides the previously described ydaM, yciR, yegE and yhjH genes, these are yhdA (csrD), which stimulates the expression of the DGC YdaM and the major curli regulator CsgD, and yeaP, which contributes to expression of the curli structural operon csgBAC. Finally, we discuss why other GGDEF/EAL domain-encoding genes, despite being expressed, do not influence motility and/or curli formation.
APA, Harvard, Vancouver, ISO, and other styles
8

Hengge, Regine, Michael Y. Galperin, Jean-Marc Ghigo, Mark Gomelsky, Jeffrey Green, Kelly T. Hughes, Urs Jenal, and Paolo Landini. "Systematic Nomenclature for GGDEF and EAL Domain-Containing Cyclic Di-GMP Turnover Proteins of Escherichia coli: TABLE 1." Journal of Bacteriology 198, no. 1 (July 6, 2015): 7–11. http://dx.doi.org/10.1128/jb.00424-15.

Full text
Abstract:
In recent years,Escherichia colihas served as one of a few model bacterial species for studying cyclic di-GMP (c-di-GMP) signaling. The widely usedE. coliK-12 laboratory strains possess 29 genes encoding proteins with GGDEF and/or EAL domains, which include 12 diguanylate cyclases (DGC), 13 c-di-GMP-specific phosphodiesterases (PDE), and 4 “degenerate” enzymatically inactive proteins. In addition, six new GGDEF and EAL (GGDEF/EAL) domain-encoding genes, which encode two DGCs and four PDEs, have recently been found in genomic analyses of commensal and pathogenicE. colistrains. As a group of researchers who have been studying the molecular mechanisms and the genomic basis of c-di-GMP signaling inE. coli, we now propose a general and systematicdgcandpdenomenclature for the enzymatically active GGDEF/EAL domain-encoding genes of this model species. This nomenclature is intuitive and easy to memorize, and it can also be applied to additional genes and proteins that might be discovered in various strains ofE. coliin future studies.
APA, Harvard, Vancouver, ISO, and other styles
9

Tan, H., J. A. West, J. P. Ramsay, R. E. Monson, J. L. Griffin, I. K. Toth, and G. P. C. Salmond. "Comprehensive overexpression analysis of cyclic-di-GMP signalling proteins in the phytopathogen Pectobacterium atrosepticum reveals diverse effects on motility and virulence phenotypes." Microbiology 160, no. 7 (July 1, 2014): 1427–39. http://dx.doi.org/10.1099/mic.0.076828-0.

Full text
Abstract:
Bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) is a ubiquitous bacterial signalling molecule produced by diguanylate cyclases of the GGDEF-domain family. Elevated c-di-GMP levels or increased GGDEF protein expression is frequently associated with the onset of sessility and biofilm formation in numerous bacterial species. Conversely, phosphodiesterase-dependent diminution of c-di-GMP levels by EAL- and HD-GYP-domain proteins is often accompanied by increased motility and virulence. In this study, we individually overexpressed 23 predicted GGDEF, EAL or HD-GYP-domain proteins encoded by the phytopathogen Pectobacterium atrosepticum strain SCRI1043. MS-based detection of c-di-GMP and 5′-phosphoguanylyl-(3′-5′)-guanosine in these strains revealed that overexpression of most genes promoted modest 1–10-fold changes in cellular levels of c-di-GMP, with the exception of the GGDEF-domain proteins ECA0659 and ECA3374, which induced 1290- and 7660-fold increases, respectively. Overexpression of most EAL domain proteins increased motility, while overexpression of most GGDEF domain proteins reduced motility and increased poly-β-1,6-N-acetyl-glucosamine-dependent flocculation. In contrast to domain-based predictions, overexpression of the EAL protein ECA3549 or the HD-GYP protein ECA3548 increased c-di-GMP concentrations and reduced motility. Most overexpression constructs altered the levels of secreted cellulases, pectinases and proteases, confirming c-di-GMP regulation of virulence in Pe. atrosepticum. However, there was no apparent correlation between virulence-factor induction and the domain class expressed or cellular c-di-GMP levels, suggesting that regulation was in response to specific effectors within the network, rather than total c-di-GMP concentration. Finally, we demonstrated that the cellular localization patterns vary considerably for GGDEF/EAL/HD-GYP proteins, indicating it is a likely factor restricting specific interactions within the c-di-GMP network.
APA, Harvard, Vancouver, ISO, and other styles
10

Kim, Yun-Kyeong, and Linda L. McCarter. "ScrG, a GGDEF-EAL Protein, Participates in Regulating Swarming and Sticking in Vibrio parahaemolyticus." Journal of Bacteriology 189, no. 11 (March 30, 2007): 4094–107. http://dx.doi.org/10.1128/jb.01510-06.

Full text
Abstract:
ABSTRACT In this work, we describe a new gene controlling lateral flagellar gene expression. The gene encodes ScrG, a protein containing GGDEF and EAL domains. This is the second GGDEF-EAL-encoding locus determined to be involved in the regulation of swarming: the first was previously characterized and named scrABC (for “swarming and capsular polysaccharide regulation”). GGDEF and EAL domain-containing proteins participate in the synthesis and degradation of the nucleotide signal cyclic di-GMP (c-di-GMP) in many bacteria. Overexpression of scrG was sufficient to induce lateral flagellar gene expression in liquid, decrease biofilm formation, decrease cps gene expression, and suppress the ΔscrABC phenotype. Removal of its EAL domain reversed ScrG activity, converting ScrG to an inhibitor of swarming and activator of cps expression. Overexpression of scrG decreased the intensity of a 32P-labeled nucleotide spot comigrating with c-di-GMP standard, whereas overexpression of scrG Δ EAL enhanced the intensity of the spot. Mutants with defects in scrG showed altered swarming and lateral flagellin production and colony morphology (but not swimming motility); furthermore, mutation of two GGDEF-EAL-encoding loci (scrG and scrABC) produced cumulative effects on swarming, lateral flagellar gene expression, lateral flagellin production and colony morphology. Mutant analysis supports the assignment of the primary in vivo activity of ScrG to acting as a phosphodiesterase. The data are consistent with a model in which multiple GGDEF-EAL proteins can influence the cellular nucleotide pool: a low concentration of c-di-GMP favors surface mobility, whereas high levels of this nucleotide promote a more adhesive Vibrio parahaemolyticus cell type.
APA, Harvard, Vancouver, ISO, and other styles
11

Simm, Roger, Jacqueline D. Fetherston, Abdul Kader, Ute Römling, and Robert D. Perry. "Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins." Journal of Bacteriology 187, no. 19 (October 1, 2005): 6816–23. http://dx.doi.org/10.1128/jb.187.19.6816-6823.2005.

Full text
Abstract:
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. AdrA (Salmonella enterica serovar Typhimurium) and HmsT (Yersinia pestis) contain GGDEF domains and are required for extracellular cellulose production and biofilm formation, respectively. Here we show that hmsT is able to restore cellulose synthesis to a Salmonella serovar Typhimurium adrA mutant and that adrA can replace hmsT in Y. pestis Hms-dependent biofilm formation. Like Y. pestis HmsT overproducers, Y. pestis cells carrying adrA under the control of an arabinose-inducible promoter produced substantial biofilms in the presence of arabinose. Finally, we demonstrate that HmsT is involved in the synthesis of cyclic di-GMP.
APA, Harvard, Vancouver, ISO, and other styles
12

Tarnawski, Miroslaw, Thomas R. M. Barends, and Ilme Schlichting. "Structural analysis of an oxygen-regulated diguanylate cyclase." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 27, 2015): 2158–77. http://dx.doi.org/10.1107/s139900471501545x.

Full text
Abstract:
Cyclic di-GMP is a bacterial second messenger that is involved in switching between motile and sessile lifestyles. Given the medical importance of biofilm formation, there has been increasing interest in understanding the synthesis and degradation of cyclic di-GMPs and their regulation in various bacterial pathogens. Environmental cues are detected by sensing domains coupled to GGDEF and EAL or HD-GYP domains that have diguanylate cyclase and phosphodiesterase activities, respectively, producing and degrading cyclic di-GMP. The Escherichia coli protein DosC (also known as YddV) consists of an oxygen-sensing domain belonging to the class of globin sensors that is coupled to a C-terminal GGDEF domain via a previously uncharacterized middle domain. DosC is one of the most strongly expressed GGDEF proteins in E. coli, but to date structural information on this and related proteins is scarce. Here, the high-resolution structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF domain in apo and substrate-bound forms is described. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. The structural information on the individual domains is combined into a model of the dimeric DosC holoprotein. These findings have direct implications for the oxygen-dependent regulation of the activity of the cyclase domain.
APA, Harvard, Vancouver, ISO, and other styles
13

Povolotsky, Tatyana L., and Regine Hengge. "Genome-Based Comparison of Cyclic Di-GMP Signaling in Pathogenic and Commensal Escherichia coli Strains." Journal of Bacteriology 198, no. 1 (August 24, 2015): 111–26. http://dx.doi.org/10.1128/jb.00520-15.

Full text
Abstract:
ABSTRACTThe ubiquitous bacterial second messenger cyclic di-GMP (c-di-GMP) has recently become prominent as a trigger for biofilm formation in many bacteria. It is generated by diguanylate cyclases (DGCs; with GGDEF domains) and degraded by specific phosphodiesterases (PDEs; containing either EAL or HD-GYP domains). Most bacterial species contain multiples of these proteins with some having specific functions that are based on direct molecular interactions in addition to their enzymatic activities.Escherichia coliK-12 laboratory strains feature 29 genes encoding GGDEF and/or EAL domains, resulting in a set of 12 DGCs, 13 PDEs, and four enzymatically inactive “degenerate” proteins that act by direct macromolecular interactions. We present here a comparative analysis of GGDEF/EAL domain-encoding genes in 61 genomes of pathogenic, commensal, and probioticE. colistrains (including enteric pathogens such as enteroaggregative, enterohemorrhagic, enteropathogenic, enterotoxigenic, and adherent and invasiveEscherichia coliand the 2011 German outbreak O104:H4 strain, as well as extraintestinal pathogenicE. coli, such as uropathogenic and meningitis-associatedE. coli). We describe additional genes for two membrane-associated DGCs (DgcX and DgcY) and four PDEs (the membrane-associated PdeT, as well as the EAL domain-only proteins PdeW, PdeX, and PdeY), thus showing the pangenome ofE. colito contain at least 35 GGDEF/EAL domain proteins. A core set of only eight proteins is absolutely conserved in all 61 strains: DgcC (YaiC), DgcI (YliF), PdeB (YlaB), PdeH (YhjH), PdeK (YhjK), PdeN (Rtn), and the degenerate proteins CsrD and CdgI (YeaI). In all other GGDEF/EAL domain genes, diverse point and frameshift mutations, as well as small or large deletions, were discovered in various strains.IMPORTANCEOur analysis reveals interesting trends in pathogenicEscherichia colithat could reflect different host cell adherence mechanisms. These may either benefit from or be counteracted by the c-di-GMP-stimulated production of amyloid curli fibers and cellulose. Thus, EAEC, which adhere in a “stacked brick” biofilm mode, have a potential for high c-di-GMP accumulation due to DgcX, a strongly expressed additional DGC. In contrast, EHEC and UPEC, which use alternative adherence mechanisms, tend to have extra PDEs, suggesting that low cellular c-di-GMP levels are crucial for these strains under specific conditions. Overall, our study also indicates that GGDEF/EAL domain proteins evolve rapidly and thereby contribute to adaptation to host-specific and environmental niches of various types ofE. coli.
APA, Harvard, Vancouver, ISO, and other styles
14

Yang, Fenghuan, Fang Tian, Xiaotong Li, Susu Fan, Huamin Chen, Maosen Wu, Ching-Hong Yang, and Chenyang He. "The Degenerate EAL-GGDEF Domain Protein Filp Functions as a Cyclic di-GMP Receptor and Specifically Interacts with the PilZ-Domain Protein PXO_02715 to Regulate Virulence in Xanthomonas oryzae pv. oryzae." Molecular Plant-Microbe Interactions® 27, no. 6 (June 2014): 578–89. http://dx.doi.org/10.1094/mpmi-12-13-0371-r.

Full text
Abstract:
Degenerate GGDEF and EAL domain proteins represent major types of cyclic diguanylic acid (c-di-GMP) receptors in pathogenic bacteria. Here, we characterized a FimX-like protein (Filp) which possesses both GGDEF and EAL domains in Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight of rice. Both in silico analysis and enzyme assays indicated that the GGDEF and EAL domains of Filp were degenerate and enzymatically inactive. However, Filp bound to c-di-GMP efficiently within the EAL domain, where Q477, E653, and F654 residues were crucial for the binding. Deletion of the filp gene in X. oryzae pv. oryzae resulted in attenuated virulence in rice and reduced type III secretion system (T3SS) gene expression. Complementation analysis with different truncated proteins indicated that REC, PAS, and EAL domains but not the GGDEF domain were required for the full activity of Filp in vivo. In addition, a PilZ-domain protein (PXO_02715) was identified as a Filp interactor by yeast two-hybrid and glutathione-S-transferase pull-down assays. Deletion of the PXO_02715 gene demonstrated changes in bacterial virulence and T3SS gene expression similar to Δfilp. Moreover, both mutants were impaired in their ability to induce hypersensitive response in nonhost plants. Thus, we concluded that Filp was a novel c-di-GMP receptor of X. oryzae pv. oryzae, and its function to regulate bacterial virulence expression might be via the interaction with PXO_02715.
APA, Harvard, Vancouver, ISO, and other styles
15

Fineran, Peter C., Neil R. Williamson, Kathryn S. Lilley, and George P. C. Salmond. "Virulence and Prodigiosin Antibiotic Biosynthesis in Serratia Are Regulated Pleiotropically by the GGDEF/EAL Domain Protein, PigX." Journal of Bacteriology 189, no. 21 (August 31, 2007): 7653–62. http://dx.doi.org/10.1128/jb.00671-07.

Full text
Abstract:
ABSTRACT Gram-negative bacteria of the genus Serratia are opportunistic human, plant, and insect pathogens. Serratia sp. strain ATCC 39006 secretes pectinases and cellulases and produces the secondary metabolites carbapenem and prodigiosin. Mutation of a gene (pigX) resulted in an extremely pleiotropic phenotype: prodigiosin antibiotic biosynthesis, plant virulence, and pectinase production were all elevated. PigX controlled secondary metabolism by repressing the transcription of the target prodigiosin biosynthetic operon (pigA-pigO). The transcriptional start site of pigX was determined, and pigX expression occurred in parallel with Pig production. Detailed quantitative intracellular proteome analyses enabled the identification of numerous downstream targets of PigX, including OpgG, mutation of which reduced the production of the plant cell wall-degrading enzymes and virulence. The highly pleiotropic PigX regulator contains GGDEF and EAL domains with noncanonical motifs and is predicted to be membrane associated. Genetic evidence suggests that PigX might function as a cyclic dimeric GMP phosphodiesterase. This is the first characterization of a GGDEF and EAL domain protein in Serratia and the first example of the regulation of antibiotic production by a GGDEF/EAL domain protein.
APA, Harvard, Vancouver, ISO, and other styles
16

Patterson, Dayna C., Myrrh Perez Ruiz, Hyerin Yoon, Johnnie A. Walker, Jean-Paul Armache, Neela H. Yennawar, and Emily E. Weinert. "Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme." Proceedings of the National Academy of Sciences 118, no. 36 (September 2, 2021): e2100657118. http://dx.doi.org/10.1073/pnas.2100657118.

Full text
Abstract:
Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a second messenger that modulates bacterial cellular processes, including biofilm formation. While proteins containing both c-di-GMP synthesizing (GGDEF) and c-di-GMP hydrolyzing (EAL) domains are widely predicted in bacterial genomes, it is poorly understood how domains with opposing enzymatic activity are regulated within a single polypeptide. Herein, we report the characterization of a globin-coupled sensor protein (GCS) from Paenibacillus dendritiformis (DcpG) with bifunctional c-di-GMP enzymatic activity. DcpG contains a regulatory sensor globin domain linked to diguanylate cyclase (GGDEF) and phosphodiesterase (EAL) domains that are differentially regulated by gas binding to the heme; GGDEF domain activity is activated by the Fe(II)-NO state of the globin domain, while EAL domain activity is activated by the Fe(II)-O2 state. The in vitro activity of DcpG is mimicked in vivo by the biofilm formation of P. dendritiformis in response to gaseous environment, with nitric oxide conditions leading to the greatest amount of biofilm formation. The ability of DcpG to differentially control GGDEF and EAL domain activity in response to ligand binding is likely due to the unusual properties of the globin domain, including rapid ligand dissociation rates and high midpoint potentials. Using structural information from small-angle X-ray scattering and negative stain electron microscopy studies, we developed a structural model of DcpG, providing information about the regulatory mechanism. These studies provide information about full-length GCS protein architecture and insight into the mechanism by which a single regulatory domain can selectively control output domains with opposing enzymatic activities.
APA, Harvard, Vancouver, ISO, and other styles
17

Shang, Fei, Ting Xue, Haipeng Sun, Lei Xing, Shuo Zhang, Zhenjun Yang, Lihe Zhang, and Baolin Sun. "The Staphylococcus aureus GGDEF Domain-Containing Protein, GdpS, Influences Protein A Gene Expression in a Cyclic Diguanylic Acid-Independent Manner." Infection and Immunity 77, no. 7 (April 20, 2009): 2849–56. http://dx.doi.org/10.1128/iai.01405-08.

Full text
Abstract:
ABSTRACT Staphylococcus aureus is an important human pathogen that is the principal cause of a variety of diseases, ranging from localized skin infections to life-threatening systemic infections. The success of the organism as a pathogen and its ability to cause such a wide range of infections are due to its extensive virulence factors. In this study, we identified the role of the only GGDEF domain protein (GdpS [GGDEF domain protein from Staphylococcus]) in the virulence of S. aureus NCTC8325. Inactivation of gdpS results in an alteration in the production of a range of virulence factors, such as serine and cysteine proteases, fibrinogen-binding proteins, and, specifically, protein A (Spa), a major surface protein of S. aureus. The transcript level of spa decreases eightfold in the gdpS mutant compared with the parental NCTC8325 strain. Furthermore, the transcript level of sarS, which encodes a direct positive regulator of spa, also decreases in the gdpS mutant compared with the wild type, while the transcript levels of agr, sarA, sarT, and rot display no apparent changes in the gdpS mutant, suggesting that GdpS affects the expression of spa through interaction with SarS by unknown mechanisms. Furthermore, the complementation assays show that the influences of GdpS on spa and sarS depend on its N-terminal domain, which is predicted to be the sensor of a two-component system, rather than its C-terminal GGDEF domain with conserved GGDEF, suggesting that GdpS functions in S. aureus by an unknown mechanism independent of 3′,5′-cyclic diguanylic acid signaling.
APA, Harvard, Vancouver, ISO, and other styles
18

D'Argenio, David A., and Samuel I. Miller. "Cyclic di-GMP as a bacterial second messenger." Microbiology 150, no. 8 (August 1, 2004): 2497–502. http://dx.doi.org/10.1099/mic.0.27099-0.

Full text
Abstract:
Environmental signals trigger changes in the bacterial cell surface, including changes in exopolysaccharides and proteinaceous appendages that ultimately favour bacterial persistence and proliferation. Such adaptations are regulated in diverse bacteria by proteins with GGDEF and EAL domains. These proteins are predicted to regulate cell surface adhesiveness by controlling the level of a second messenger, the cyclic dinucleotide c-di-GMP. Genetic evidence suggests that the GGDEF domain acts as a nucleotide cyclase for c-di-GMP synthesis while the EAL domain is a good candidate for the opposing activity, a phosphodiesterase for c-di-GMP degradation.
APA, Harvard, Vancouver, ISO, and other styles
19

Pei, Jimin, and Nick V. Grishin. "GGDEF domain is homologous to adenylyl cyclase." Proteins: Structure, Function, and Genetics 42, no. 2 (2000): 210–16. http://dx.doi.org/10.1002/1097-0134(20010201)42:2<210::aid-prot80>3.0.co;2-8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
20

Chen, Xianyi, Shaoxuan Qu, Xin Luo, Shi-En Lu, Youzhou Liu, Huiping Li, Lijuan Hou, Jinsheng Lin, Ning Jiang, and Lin Ma. "PafS Containing GGDEF-Domain Regulates Life Activities of Pseudomonas glycinae MS82." Microorganisms 10, no. 12 (November 26, 2022): 2342. http://dx.doi.org/10.3390/microorganisms10122342.

Full text
Abstract:
Cyclic dimeric guanosine monophosphate (c-di-GMP) is synthesized by diguanylate cyclase (DGC) with the GGDEF domain. As a ubiquitous bacterial second messenger, it regulates diverse life-activity phenotypes in some bacteria. Although 38 genes encoding GGDEF-domain-containing proteins have been identified in the genome of the Pseudomonas glycinae strain MS82, whether c-di-GMP functions as a facilitator or repressor of life-activity phenotypes is poorly understood. In this study, one of the 38 genes containing a GGDEF domain in MS82, PafS was investigated to explore its regulatory function in bacterial life activities. The PafS-deletion mutant ΔPafS and reversion mutant PafS-comp were constructed by the method of biparental conjugation and homologous recombination. The life activities of the mutants, such as antifungal activity, biofilm formation ability, polysaccharide content, and motor behavior, were explored. The results showed that all life-activity phenotypes were significantly reduced after knocking out PafS, whereas all were significantly restored to a similar level to that of MS82 after the complementation of PafS. These results suggested that PafS plays an important role in the regulation of a range of cellular activities by c-di-GMP in P. glycinae MS82.
APA, Harvard, Vancouver, ISO, and other styles
21

An, Shuwen, Ji'en Wu, and Lian-Hui Zhang. "Modulation of Pseudomonas aeruginosa Biofilm Dispersal by a Cyclic-Di-GMP Phosphodiesterase with a Putative Hypoxia-Sensing Domain." Applied and Environmental Microbiology 76, no. 24 (October 22, 2010): 8160–73. http://dx.doi.org/10.1128/aem.01233-10.

Full text
Abstract:
ABSTRACT Pseudomonas aeruginosa encodes many enzymes that are potentially associated with the synthesis or degradation of the widely conserved second messenger cyclic-di-GMP (c-di-GMP). In this study, we show that mutation of rbdA, which encodes a fusion protein consisting of PAS-PAC-GGDEF-EAL multidomains, results in decreased biofilm dispersal. RbdA contains a highly conserved GGDEF domain and EAL domain, which are involved in the synthesis and degradation of c-di-GMP, respectively. However, in vivo and in vitro analyses show that the full-length RbdA protein only displays phosphodiesterase activity, causing c-di-GMP degradation. Further analysis reveals that the GGDEF domain of RbdA plays a role in activating the phosphodiesterase activity of the EAL domain in the presence of GTP. Moreover, we show that deletion of the PAS domain or substitution of the key residues implicated in sensing low-oxygen stress abrogates the functionality of RbdA. Subsequent study showed that RbdA is involved in positive regulation of bacterial motility and production of rhamnolipids, which are associated with biofilm dispersal, and in negative regulation of production of exopolysaccharides, which are required for biofilm formation. These data indicate that the c-di-GMP-degrading regulatory protein RbdA promotes biofilm dispersal through its two-pronged effects on biofilm development, i.e., downregulating biofilm formation and upregulating production of the factors associated with biofilm dispersal.
APA, Harvard, Vancouver, ISO, and other styles
22

Lacey, Melissa M., Jonathan D. Partridge, and Jeffrey Green. "Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response." Microbiology 156, no. 9 (September 1, 2010): 2873–86. http://dx.doi.org/10.1099/mic.0.037887-0.

Full text
Abstract:
The Escherichia coli K-12 yfgF gene encodes a protein with domains associated with cyclic di-GMP signalling: GGDEF (associated with diguanylate cyclase activity) and EAL (associated with cyclic di-GMP phosphodiesterase activity). Here, it is shown that yfgF is expressed under anaerobic conditions from a class II FNR (regulator of fumarate and nitrate reduction)-dependent promoter. Anaerobic expression of yfgF is greatest in stationary phase, and in cultures grown at 28 °C, suggesting that low growth rates promote yfgF expression. Mutation of yfgF resulted in altered cell surface properties and enhanced sensitivity when anaerobic cultures were exposed to peroxides. The purified YfgF GGDEF-EAL (YfgFGE) and EAL (YfgFE) domains possessed cyclic di-GMP-specific phosphodiesterase activity, but lacked diguanylate cyclase activity. However, the catalytically inactive GGDEF domain was required for YfgFGE dimerization and enhanced cyclic di-GMP phosphodiesterase activity in the presence of physiological concentrations of Mg2+. The cyclic di-GMP phosphodiesterase activity of YfgFGE and YfgFE was inhibited by the product of the reaction, 5′-phosphoguanylyl-(3′–5′)-guanosine (pGpG). Thus, it is shown that the yfgF gene encodes an anaerobic cyclic di-GMP phosphodiesterase that is involved in remodelling the cell surface of E. coli K-12 and in the response to peroxide shock, with implications for integrating three global regulatory networks, i.e. oxygen regulation, cyclic di-GMP signalling and the oxidative stress response.
APA, Harvard, Vancouver, ISO, and other styles
23

Simm, Roger, Jacqueline D. Fetherston, Abdul Kader, Ute Römling, and Robert D. Perry. "Phenotypic Convergence Mediated by GGDEF-Domain-Containing Proteins." Journal of Bacteriology 188, no. 5 (March 1, 2006): 2024. http://dx.doi.org/10.1128/jb.188.5.2024.2006.

Full text
APA, Harvard, Vancouver, ISO, and other styles
24

Marmont, Lindsey S., John C. Whitney, Howard Robinson, Kelly M. Colvin, Matthew R. Parsek, and P. Lynne Howell. "Expression, purification, crystallization and preliminary X-ray analysis ofPseudomonas aeruginosaPelD." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (January 26, 2012): 181–84. http://dx.doi.org/10.1107/s1744309111052109.

Full text
Abstract:
The production of the PEL polysaccharide inPseudomonas aeruginosarequires the binding of bis-(3′,5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) to the cytoplasmic GGDEF domain of the inner membrane protein PelD. Here, the overexpression, purification and crystallization of a soluble construct of PelD that encompasses the GGDEF domain and a predicted GAF domain is reported. Diffraction-quality crystals were grown using the hanging-drop vapour-diffusion method. The crystals grew as flat plates, with unit-cell parametersa = 88.3,b= 114.0,c= 61.9 Å, α = β = γ = 90.0°. The PelD crystals exhibited the symmetry of space groupP21212 and diffracted to a minimumd-spacing of 2.2 Å. On the basis of the Matthews coefficient (VM= 2.29 Å3 Da−1), it was estimated that two molecules are present in the asymmetric unit.
APA, Harvard, Vancouver, ISO, and other styles
25

Rakshe, Shauna, Maija Leff, and Alfred M. Spormann. "Indirect Modulation of the Intracellular c-Di-GMP Level inShewanella oneidensisMR-1 by MxdA." Applied and Environmental Microbiology 77, no. 6 (January 28, 2011): 2196–98. http://dx.doi.org/10.1128/aem.01985-10.

Full text
Abstract:
ABSTRACTThe GGDEF domain protein MxdA, which is important for biofilm formation inShewanella oneidensisMR-1, was hypothesized to possess diguanylate cyclase activity. Here, we demonstrate that while MxdA controls the cellular level of c-di-GMP inS. oneidensis, it modulates the c-di-GMP pool indirectly.
APA, Harvard, Vancouver, ISO, and other styles
26

Dow, J. Maxwell, Yvonne Fouhy, Jean F. Lucey, and Robert P. Ryan. "The HD-GYP Domain, Cyclic Di-GMP Signaling, and Bacterial Virulence to Plants." Molecular Plant-Microbe Interactions® 19, no. 12 (December 2006): 1378–84. http://dx.doi.org/10.1094/mpmi-19-1378.

Full text
Abstract:
Cyclic di-GMP is an almost ubiquitous second messenger in bacteria that was first described as an allosteric activator of cellulose synthase but is now known to regulate a range of functions, including virulence in human and animal pathogens. Two protein domains, GGDEF and EAL, are implicated in the synthesis and degradation, respectively, of cyclic di-GMP. These domains are widely distributed in bacteria, including plant pathogens. The majority of proteins with GGDEF and EAL domains contain additional signal input domains, suggesting that their activities are responsive to environmental cues. Recent studies have demonstrated that a third domain, HD-GYP, is also active in cyclic di-GMP degradation. In the plant pathogen Xanthomonas campestris pv. campestris, a two-component signal transduction system comprising the HD-GYP domain regulatory protein RpfG and cognate sensor RpfC positively controls virulence. The signals recognized by RpfC may include the cell-cell signal DSF, which also acts to regulate virulence in X. campestris pv. campestris. Here, we review these recent advances in our understanding of cyclic di-GMP signaling with particular reference to one or more roles in the bacterial pathogenesis of plants.
APA, Harvard, Vancouver, ISO, and other styles
27

Thomas, Colleen, Carol R. Andersson, Shannon R. Canales, and Susan S. Golden. "PsfR, a factor that stimulates psbAI expression in the cyanobacterium Synechococcus elongatus PCC 7942." Microbiology 150, no. 4 (April 1, 2004): 1031–40. http://dx.doi.org/10.1099/mic.0.26915-0.

Full text
Abstract:
In this paper a gene (psfR) is reported that regulates psbAI activity in Synechococcus elongatus, a unicellular photoautotrophic cyanobacterium that carries out oxygenic (plant-type) photosynthesis and exhibits global circadian regulation of gene expression. In S. elongatus, a family of three psbA genes encodes the D1 protein of the photosystem II reaction centre. Overexpression of psfR results in increased expression of psbAI, but does not affect the circadian timing of psbAI expression. psfR overexpression affected some, but not all of the genes routinely surveyed for circadian expression. PsfR acts (directly or indirectly) on the psbAI basal promoter region. psfR knockout mutants exhibit wild-type psbAI expression, suggesting that other factors can regulate psbAI expression in the absence of functional PsfR. PsfR contains two receiver-like domains (found in bacterial two-component signal transduction systems), one of which lacks the conserved aspartyl residue required for phosphoryl transfer. PsfR also contains a GGDEF domain. The presence of these domains and the absence of a detectable conserved DNA-binding domain suggest that PsfR may regulate psbAI expression via protein–protein interactions or GGDEF activity (the production of cyclic dinucleotides) rather than direct interaction with the psbAI promoter.
APA, Harvard, Vancouver, ISO, and other styles
28

Liu, Xianxian, Sinem Beyhan, Bentley Lim, Roger G. Linington, and Fitnat H. Yildiz. "Identification and Characterization of a Phosphodiesterase That Inversely Regulates Motility and Biofilm Formation in Vibrio cholerae." Journal of Bacteriology 192, no. 18 (July 9, 2010): 4541–52. http://dx.doi.org/10.1128/jb.00209-10.

Full text
Abstract:
ABSTRACT Vibrio cholerae switches between free-living motile and surface-attached sessile lifestyles. Cyclic diguanylate (c-di-GMP) is a signaling molecule controlling such lifestyle changes. C-di-GMP is synthesized by diguanylate cyclases (DGCs) that contain a GGDEF domain and is degraded by phosphodiesterases (PDEs) that contain an EAL or HD-GYP domain. We constructed in-frame deletions of all V. cholerae genes encoding proteins with GGDEF and/or EAL domains and screened mutants for altered motility phenotypes. Of 52 mutants tested, four mutants exhibited an increase in motility, while three mutants exhibited a decrease in motility. We further characterized one mutant lacking VC0137 (cdgJ), which encodes an EAL domain protein. Cellular c-di-GMP quantifications and in vitro enzymatic activity assays revealed that CdgJ functions as a PDE. The cdgJ mutant had reduced motility and exhibited a small decrease in flaA expression; however, it was able to produce a flagellum. This mutant had enhanced biofilm formation and vps gene expression compared to that of the wild type, indicating that CdgJ inversely regulates motility and biofilm formation. Genetic interaction analysis revealed that at least four DGCs, together with CdgJ, control motility in V. cholerae.
APA, Harvard, Vancouver, ISO, and other styles
29

Gjermansen, Morten, Paula Ragas, and Tim Tolker-Nielsen. "Proteins with GGDEF and EAL domains regulatePseudomonas putidabiofilm formation and dispersal." FEMS Microbiology Letters 265, no. 2 (December 2006): 215–24. http://dx.doi.org/10.1111/j.1574-6968.2006.00493.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
30

Gomelsky, Mark. "A Zinc Lock on GGDEF Domain Dimerization Inhibits E. coli Biofilms." Structure 21, no. 7 (July 2013): 1067–68. http://dx.doi.org/10.1016/j.str.2013.06.011.

Full text
APA, Harvard, Vancouver, ISO, and other styles
31

Chen, Chuan, Xu Zhang, Fei Shang, Haipeng Sun, Baolin Sun, and Ting Xue. "The Staphylococcus aureus Protein-Coding GenegdpSModulatessarSExpression via mRNA-mRNA Interaction." Infection and Immunity 83, no. 8 (June 8, 2015): 3302–10. http://dx.doi.org/10.1128/iai.00159-15.

Full text
Abstract:
Staphylococcus aureusis an important Gram-positive pathogen responsible for numerous diseases ranging from localized skin infections to life-threatening systemic infections. The virulence ofS. aureusis essentially determined by a wide spectrum of factors, including cell wall-associated proteins and secreted toxins that are precisely controlled in response to environmental changes. GGDEF domain protein fromStaphylococcus(GdpS) is the only conserved staphylococcal GGDEF domain protein that is involved not in c-di-GMP synthesis but in the virulence regulation ofS. aureusNCTC8325. Our previous study showed that the inactivation ofgdpSgenerates an extensive change of virulence factors together with, in particular, a major Spa (protein A) surface protein. As reported,sarSis a direct positive regulator ofspa. The decreased transcript levels ofsarSin thegdpSmutant compared with the parental NCTC8325 strain suggest thatgdpSaffectsspathrough interaction withsarS. In this study, site mutation and complementary experiments showed that the translation product ofgdpSwas not involved in the regulation of transcript levels ofsarS. We found thatgdpSfunctioned through direct RNA-RNA base pairing with the 5′ untranslated region (5′UTR) ofsarSmRNA and that a putative 18-nucleotide region played a significant role in the regulatory process. Furthermore, the mRNA half-life analysis ofsarSin thegdpSmutant showed thatgdpSpositively regulates the mRNA levels ofsarSby contributing to the stabilization ofsarSmRNA, suggesting thatgdpSmRNA may regulatespaexpression in an RNA-dependent pathway.
APA, Harvard, Vancouver, ISO, and other styles
32

Lacey, Melissa, Agnieshka Agasing, Rebecca Lowry, and Jeffrey Green. "Identification of the YfgF MASE1 domain as a modulator of bacterial responses to aspartate." Open Biology 3, no. 6 (June 2013): 130046. http://dx.doi.org/10.1098/rsob.130046.

Full text
Abstract:
Complex 3′-5′-cyclic diguanylic acid (c-di-GMP) responsive regulatory networks that are modulated by the action of multiple diguanylate cyclases (DGC; GGDEF domain proteins) and phosphodiesterases (PDE; EAL domain proteins) have evolved in many bacteria. YfgF proteins possess a membrane-anchoring domain (MASE1), a catalytically inactive GGDEF domain and a catalytically active EAL domain. Here, sustained expression of the Salmonella enterica spp. Enterica ser. Enteritidis YfgF protein is shown to mediate inhibition of the formation of the aspartate chemotactic ring on motility agar under aerobic conditions. This phenomenon was c-di-GMP-independent because it occurred in a Salmonella strain that lacked the ability to synthesize c-di-GMP and also when PDE activity was abolished by site-directed mutagenesis of the EAL domain. YfgF-mediated inhibition of aspartate chemotactic ring formation was impaired in the altered redox environment generated by exogenous p- benzoquinone. This ability of YfgF to inhibit the response to aspartate required a motif, 213 Lys-Lys-Glu 215 , in the predicted cytoplasmic loop between trans-membrane regions 5 and 6 of the MASE1 domain. Thus, for the first time the function of a MASE1 domain as a redox-responsive regulator of bacterial responses to aspartate has been shown.
APA, Harvard, Vancouver, ISO, and other styles
33

Tamayo, Rita, Stefan Schild, Jason T. Pratt, and Andrew Camilli. "Role of Cyclic Di-GMP during El Tor Biotype Vibrio cholerae Infection: Characterization of the In Vivo-Induced Cyclic Di-GMP Phosphodiesterase CdpA." Infection and Immunity 76, no. 4 (January 28, 2008): 1617–27. http://dx.doi.org/10.1128/iai.01337-07.

Full text
Abstract:
ABSTRACT In Vibrio cholerae, the second messenger cyclic di-GMP (c-di-GMP) positively regulates biofilm formation and negatively regulates virulence and is proposed to play an important role in the transition from persistence in the environment to survival in the host. Herein we describe a characterization of the infection-induced gene cdpA, which encodes both GGDEF and EAL domains, which are known to mediate diguanylate cyclase and c-di-GMP phosphodiesterase (PDE) activities, respectively. CdpA is shown to possess PDE activity, and this activity is regulated by its inactive degenerate GGDEF domain. CdpA inhibits biofilm formation but has no effect on colonization of the infant mouse small intestine. Consistent with these observations, cdpA is expressed during in vitro growth in a biofilm but is not expressed in vivo until the late stage of infection, after colonization has occurred. To test for a role of c-di-GMP in the early stages of infection, we artificially increased c-di-GMP and observed reduced colonization. This was attributed to a significant reduction in toxT transcription during infection. Cumulatively, these results support a model of the V. cholerae life cycle in which c-di-GMP must be down-regulated early after entering the small intestine and maintained at a low level to allow virulence gene expression, colonization, and motility at appropriate stages of infection.
APA, Harvard, Vancouver, ISO, and other styles
34

Hengge, Regine. "Trigger phosphodiesterases as a novel class of c-di-GMP effector proteins." Philosophical Transactions of the Royal Society B: Biological Sciences 371, no. 1707 (November 5, 2016): 20150498. http://dx.doi.org/10.1098/rstb.2015.0498.

Full text
Abstract:
The bacterial second messenger c-di-GMP controls bacterial biofilm formation, motility, cell cycle progression, development and virulence. It is synthesized by diguanylate cyclases (with GGDEF domains), degraded by specific phosphodiesterases (PDEs, with EAL of HD-GYP domains) and sensed by a wide variety of c-di-GMP-binding effectors that control diverse targets. c-di-GMP-binding effectors can be riboswitches as well as proteins with highly diverse structures and functions. The latter include ‘degenerate’ GGDEF/EAL domain proteins that are enzymatically inactive but still able to bind c-di-GMP. Surprisingly, two enzymatically active ‘trigger PDEs’, the Escherichia coli proteins PdeR and PdeL, have recently been added to this list of c-di-GMP-sensing effectors. Mechanistically, trigger PDEs are multifunctional. They directly and specifically interact with a macromolecular target (e.g. with a transcription factor or directly with a promoter region), whose activity they control by their binding and degradation of c-di-GMP—their PDE activity thus represents the c-di-GMP sensor or effector function. In this process, c-di-GMP serves as a regulatory ligand, but in contrast to classical allosteric control, this ligand is also degraded. The resulting kinetics and circuitry of control are ideally suited for trigger PDEs to serve as key components in regulatory switches. This article is part of the themed issue ‘The new bacteriology’.
APA, Harvard, Vancouver, ISO, and other styles
35

Lim, Bentley, Sinem Beyhan, and Fitnat H. Yildiz. "Regulation of Vibrio Polysaccharide Synthesis and Virulence Factor Production by CdgC, a GGDEF-EAL Domain Protein, in Vibrio cholerae." Journal of Bacteriology 189, no. 3 (February 1, 2007): 717–29. http://dx.doi.org/10.1128/jb.00834-06.

Full text
Abstract:
ABSTRACT In Vibrio cholerae, the second messenger 3′,5′-cyclic diguanylic acid (c-di-GMP) regulates several cellular processes, such as formation of corrugated colony morphology, biofilm formation, motility, and virulence factor production. Both synthesis and degradation of c-di-GMP in the cell are modulated by proteins containing GGDEF and/or EAL domains, which function as a diguanylate cyclase and a phosphodiesterase, respectively. The expression of two genes, cdgC and mbaA, which encode proteins harboring both GGDEF and EAL domains is higher in the rugose phase variant of V. cholerae than in the smooth variant. In this study, we carried out gene expression analysis to determine the genes regulated by CdgC in the rugose and smooth phase variants of V. cholerae. We determined that CdgC regulates expression of genes required for V. cholerae polysaccharide synthesis and of the transcriptional regulator genes vpsR, vpsT, and hapR. CdgC also regulates expression of genes involved in extracellular protein secretion, flagellar biosynthesis, and virulence factor production. We then compared the genes regulated by CdgC and by MbaA, during both exponential and stationary phases of growth, to elucidate processes regulated by them. Identification of the regulons of CdgC and MbaA revealed that the regulons overlap, but the timing of regulation exerted by CdgC and MbaA is different, suggesting the interplay and complexity of the c-di-GMP signal transduction pathways operating in V. cholerae.
APA, Harvard, Vancouver, ISO, and other styles
36

Beyhan, Sinem, Kivanc Bilecen, Sofie R. Salama, Catharina Casper-Lindley, and Fitnat H. Yildiz. "Regulation of Rugosity and Biofilm Formation in Vibrio cholerae: Comparison of VpsT and VpsR Regulons and Epistasis Analysis of vpsT, vpsR, and hapR." Journal of Bacteriology 189, no. 2 (January 15, 2007): 388–402. http://dx.doi.org/10.1128/jb.00981-06.

Full text
Abstract:
ABSTRACT Vibrio cholerae undergoes phenotypic variation that generates two morphologically different variants, termed smooth and rugose. The transcriptional profiles of the two variants differ greatly, and many of the differentially regulated genes are controlled by a complex regulatory circuitry that includes the transcriptional regulators VpsR, VpsT, and HapR. In this study, we identified the VpsT regulon and compared the VpsT and VpsR regulons to elucidate the contribution of each positive regulator to the rugose variant transcriptional profile and associated phenotypes. We have found that although the VpsT and VpsR regulons are very similar, the magnitude of the gene regulation accomplished by each regulator is different. We also determined that cdgA, which encodes a GGDEF domain protein, is partially responsible for the altered vps gene expression between the vpsT and vpsR mutants. Analysis of epistatic relationships among hapR, vpsT, and vpsR with respect to a whole-genome expression profile, colony morphology, and biofilm formation revealed that vpsR is epistatic to hapR and vpsT. Expression of virulence genes was increased in a vpsR hapR double mutant relative to a hapR mutant, suggesting that VpsR negatively regulates virulence gene expression in the hapR mutant. These results show that a complex regulatory interplay among VpsT, VpsR, HapR, and GGDEF/EAL family proteins controls transcription of the genes required for Vibrio polysaccharide and virulence factor production in V. cholerae.
APA, Harvard, Vancouver, ISO, and other styles
37

Aldridge, Phillip, Ralf Paul, Patrick Goymer, Paul Rainey, and Urs Jenal. "Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus." Molecular Microbiology 47, no. 6 (March 5, 2003): 1695–708. http://dx.doi.org/10.1046/j.1365-2958.2003.03401.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
38

Kuchma, Sherry L., Kimberly M. Brothers, Judith H. Merritt, Nicole T. Liberati, Frederick M. Ausubel, and George A. O'Toole. "BifA, a Cyclic-Di-GMP Phosphodiesterase, Inversely Regulates Biofilm Formation and Swarming Motility by Pseudomonas aeruginosa PA14." Journal of Bacteriology 189, no. 22 (June 22, 2007): 8165–78. http://dx.doi.org/10.1128/jb.00586-07.

Full text
Abstract:
ABSTRACT The intracellular signaling molecule, cyclic-di-GMP (c-di-GMP), has been shown to influence bacterial behaviors, including motility and biofilm formation. We report the identification and characterization of PA4367, a gene involved in regulating surface-associated behaviors in Pseudomonas aeruginosa. The PA4367 gene encodes a protein with an EAL domain, associated with c-di-GMP phosphodiesterase activity, as well as a GGDEF domain, which is associated with a c-di-GMP-synthesizing diguanylate cyclase activity. Deletion of the PA4367 gene results in a severe defect in swarming motility and a hyperbiofilm phenotype; thus, we designate this gene bifA, for biofilm formation. We show that BifA localizes to the inner membrane and, in biochemical studies, that purified BifA protein exhibits phosphodiesterase activity in vitro but no detectable diguanylate cyclase activity. Furthermore, mutational analyses of the conserved EAL and GGDEF residues of BifA suggest that both domains are important for the observed phosphodiesterase activity. Consistent with these data, the ΔbifA mutant exhibits increased cellular pools of c-di-GMP relative to the wild type and increased synthesis of a polysaccharide produced by the pel locus. This increased polysaccharide production is required for the enhanced biofilm formed by the ΔbifA mutant but does not contribute to the observed swarming defect. The ΔbifA mutation also results in decreased flagellar reversals. Based on epistasis studies with the previously described sadB gene, we propose that BifA functions upstream of SadB in the control of biofilm formation and swarming.
APA, Harvard, Vancouver, ISO, and other styles
39

Chou, Shan-Ho. "Structure of a Novel Bacterial c-GMP Binding Protein." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1637. http://dx.doi.org/10.1107/s2053273314083624.

Full text
Abstract:
cAMP is an important secondary messenger molecule widely distributed across all living kingdoms, whereas cGMP is generally considered to be restricted to eukaryotes. Recently, solid evidences for cGMP signaling in Rhodospirillum centenum have been provided, and it is proposed that cGMP could also be adapted to deliver messages to diverse outputs via unknown mechanisms. While the structures and functions of binding between cAMP and its receptor protein CRP have been well studied in the past, currently no structure of prokaryotic cGMP-binding protein complex is known. Here we report the first determination of a cGMP-receptor crystal structure from the plant pathogen Xanthomonas campestris (Xcc) to a resolution of 2.2 Å. The new cGMP receptor Xcc0249 is found to belong to the CRP/FNR family protein containing both a cyclic-Nucleotide Binding Domain (cNBD) and a GGDEF domains, and exhibits strong cGMP binding and diguanylate cyclase activities. Mutations of crucial amino acid residues responsible for cGMP binding to Xcc0249 are found to significantly reduce the biofilm formation and virulence in Xcc. Isothermal calorimetry (ITC) measurements demonstrate that Xcc0249 can bind preferentially to cGMP with a much stronger affinity (KD: 2.93E-7) than cAMP (KD: 1.79E-5). cGMP binding to Xcc0249 is also found to enhance the GGDEF diguanylate cyclase activity, implying a broader functional role of cGMP and a possible linkage between the cGMP and c-di-GMP interaction networks in bacteria. References
APA, Harvard, Vancouver, ISO, and other styles
40

Ausmees, Nora, Raphael Mayer, Haim Weinhouse, Gail Volman, Dorit Amikam, Moshe Benziman, and Martin Lindberg. "Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity." FEMS Microbiology Letters 204, no. 1 (October 2001): 163–67. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10880.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
41

García, Begoña, Cristina Latasa, Cristina Solano, Francisco García-del Portillo, Carlos Gamazo, and Iñigo Lasa. "Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation." Molecular Microbiology 54, no. 1 (August 12, 2004): 264–77. http://dx.doi.org/10.1111/j.1365-2958.2004.04269.x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
42

Navarro, Marcos V. A. S., Nabanita De, Narae Bae, Qi Wang, and Holger Sondermann. "Structural Analysis of the GGDEF-EAL Domain-Containing c-di-GMP Receptor FimX." Structure 17, no. 8 (August 2009): 1104–16. http://dx.doi.org/10.1016/j.str.2009.06.010.

Full text
APA, Harvard, Vancouver, ISO, and other styles
43

Ruíz, Lina María, Wolfgang Sand, Carlos A. Jerez, and Nicolas Guiliani. "C-di-GMP Pathway in Acidithiobacillus ferrooxidans: Analysis of Putative Diguanylate Cyclases (DGCs) and Phosphodiesterases (PDEs) Bifunctional Proteins." Advanced Materials Research 20-21 (July 2007): 551–55. http://dx.doi.org/10.4028/www.scientific.net/amr.20-21.551.

Full text
Abstract:
Acidithiobacillus ferrooxidans, an acidophilic, chemolithotrophic, γ-proteobacterium, is involved in the bioleaching of metal sulfides. For this process, bacterial attachment to mineral surface and biofilm development play a pivotal role. Generally, biofilm formation and production of exopolysaccharides is regulated by the second messenger cyclic diguanylic acid (c-di-GMP) whose cellular level depends on the synthesis and degradation activities of diguanylate cyclase (DGCs, with GGDEF domain) and phosphodiesterase (PDE, with EAL or HD-GYP domains), respectively. The analysis of the genomic sequence of A. ferrooxidans ATCC 23270 allowed us to identify 5 putative orfs encoding DGC and/or PDE-like proteins. Four of them encode for bifunctional putative proteins with GGDEF and EAL domains and are named AFE_0053, AFE_1360, AFE_1373 and AFE_1379. The fifth one named AFE_1852 has an EAL domain. The putative proteins also include PAS and GAF domains involved in signal transduction. These features suggest an involvement in signalling transduction through the metabolism of c-di-GMP. The amino acid sequences of these putative proteins were aligned with known DGCs and PDEs. Alignments indicate that AFE_1360 and AFE_1373 share more consensus sequences with active PDEs, whereas AFE_0053 and AFE_1379 do with active DGCs. On the other hand, in AFE_1852 some conserved residues of known active PDEs are changed. RT-PCR-experiments revealed that the genes that encode for these putative DGCs and/or PDEs are expressed by growth on two different substrates. These preliminary results suggest that A. ferrooxidans possesses a c-di-GMP pathway that should be involved in biofilm formation, as it occurs in many bacteria.
APA, Harvard, Vancouver, ISO, and other styles
44

Beyhan, Sinem, Lindsay S. Odell, and Fitnat H. Yildiz. "Identification and Characterization of Cyclic Diguanylate Signaling Systems Controlling Rugosity in Vibrio cholerae." Journal of Bacteriology 190, no. 22 (September 12, 2008): 7392–405. http://dx.doi.org/10.1128/jb.00564-08.

Full text
Abstract:
ABSTRACT Vibrio cholerae, the causative agent of the disease cholera, can generate rugose variants that have an increased capacity to form biofilms. Rugosity and biofilm formation are critical for the environmental survival and transmission of the pathogen, and these processes are controlled by cyclic diguanylate (c-di-GMP) signaling systems. c-di-GMP is produced by diguanylate cyclases (DGCs) and degraded by phosphodiesterases (PDEs). Proteins that contain GGDEF domains act as DGCs, whereas proteins that contain EAL or HD-GYP domains act as PDEs. In the V. cholerae genome there are 62 genes that are predicted to encode proteins capable of modulating the cellular c-di-GMP concentration. We previously identified two DGCs, VpvC and CdgA, that can control the switch between smooth and rugose. To identify other c-di-GMP signaling proteins involved in rugosity, we generated in-frame deletion mutants of all genes predicted to encode proteins with GGDEF and EAL domains and then searched for mutants with altered rugosity. In this study, we identified two new genes, cdgG and cdgH, involved in rugosity control. We determined that CdgH acts as a DGC and positively regulates rugosity, whereas CdgG does not have DGC activity and negatively regulates rugosity. In addition, epistasis analysis with CdgG, CdgH, and other DGCs and PDEs controlling rugosity revealed that CdgG and CdgH act in parallel with previously identified c-di-GMP signaling proteins to control rugosity in V. cholerae. We also determined that PilZ domain-containing c-di-GMP binding proteins contribute minimally to rugosity, indicating that there are additional c-di-GMP binding proteins controlling rugosity in V. cholerae.
APA, Harvard, Vancouver, ISO, and other styles
45

Güvener, Zehra Tüzün, and Linda L. McCarter. "Multiple Regulators Control Capsular Polysaccharide Production in Vibrio parahaemolyticus." Journal of Bacteriology 185, no. 18 (September 15, 2003): 5431–41. http://dx.doi.org/10.1128/jb.185.18.5431-5441.2003.

Full text
Abstract:
ABSTRACT Vibrio parahaemolyticus, a biofouling marine bacterium and human pathogen, undergoes phase variation displaying translucent (TR) and opaque (OP) colony morphologies. Prior studies demonstrated that OP colonies produce more capsular polysaccharide (CPS) than TR colonies and that opacity is controlled by the Vibrio harveyi LuxR-type transcriptional activator OpaR. CPS has also been shown to be regulated by the scrABC signaling pathway, which involves a GGDEF-EAL motif-containing sensory protein. The present study identifies cps genes and examines their regulation. Transposon insertions in the cps locus, which contains 11 genes, abolished opacity. Such mutants failed to produce CPS and were defective in pellicle formation in microtiter wells and in a biofilm attachment assay. Reporter fusions to cpsA, the first gene in the locus, showed ∼10-fold-enhanced transcription in the OP (opaR +) strain compared to a TR (ΔopaR) strain. Two additional transcriptional regulators were discovered. One potential activator, CpsR, participates in the scrABC GGDEF-EAL-signaling pathway; CpsR was required for the increased cps expression observed in scrA ΔopaR strains. CpsR, which contains a conserved module found in members of the AAA+ superfamily of ATP-interacting proteins, is homologous to Vibrio cholerae VpsR; however, unlike VpsR, CpsR was not essential for cps expression. CpsS, the second newly identified regulator, contains a CsgD-type DNA-binding domain and appears to act as a repressor. Mutants with cpsS defects have greatly elevated cps transcription; their high level of cpsA expression was CpsR dependent in ΤR strains and primarily OpaR dependent in OP strains. Thus, a network of positive and negative regulators modulates CPS production in V. parahaemolyticus.
APA, Harvard, Vancouver, ISO, and other styles
46

Nie, Hailing, Yujie Xiao, Jinzhi He, Huizhong Liu, Liang Nie, Wenli Chen, and Qiaoyun Huang. "Phenotypic–genotypic analysis of GGDEF/EAL/HD‐GYP domain‐encoding genes in Pseudomonas putida." Environmental Microbiology Reports 12, no. 1 (November 25, 2019): 38–48. http://dx.doi.org/10.1111/1758-2229.12808.

Full text
APA, Harvard, Vancouver, ISO, and other styles
47

Kumagai, Yumi, Junji Matsuo, Yoshihiro Hayakawa, and Yasuko Rikihisa. "Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes." Journal of Bacteriology 192, no. 16 (June 18, 2010): 4122–33. http://dx.doi.org/10.1128/jb.00132-10.

Full text
Abstract:
ABSTRACT Cyclic di-GMP (c-di-GMP) is a bacterial second messenger produced by GGDEF domain-containing proteins. The genome of Ehrlichia chaffeensis, an obligatory intracellular bacterium that causes human monocytic ehrlichiosis, encodes a single protein that contains a GGDEF domain, called PleD. In this study, we investigated the effects of c-di-GMP signaling on E. chaffeensis infection of the human monocytic cell line THP-1. Recombinant E. chaffeensis PleD showed diguanylate cyclase activity as it generated c-di-GMP in vitro. Because c-di-GMP is not cell permeable, the c-di-GMP hydrophobic analog 2′-O-di(tert-butyldimethylsilyl)-c-di-GMP (CDGA) was used to examine intracellular c-di-GMP signaling. CDGA activity was first tested with Salmonella enterica serovar Typhimurium. CDGA inhibited well-defined c-di-GMP-regulated phenomena, including cellulose synthesis, clumping, and upregulation of csgD and adrA mRNA, indicating that CDGA acts as an antagonist in c-di-GMP signaling. [32P]c-di-GMP bound several E. chaffeensis native proteins and two E. chaffeensis recombinant I-site proteins, and this binding was blocked by CDGA. Although pretreatment of E. chaffeensis with CDGA did not reduce bacterial binding to THP-1 cells, bacterial internalization was reduced. CDGA facilitated protease-dependent degradation of particular, but not all, bacterial surface-exposed proteins, including TRP120, which is associated with bacterial internalization. Indeed, the serine protease HtrA was detected on the surface of E. chaffeensis, and TRP120 was degraded by treatment of E. chaffeensis with recombinant E. chaffeensis HtrA. Furthermore, anti-HtrA inhibited CDGA-induced TRP120 degradation. Our results suggest that E. chaffeensis invasion is regulated by c-di-GMP signaling, which stabilizes some bacterial surface-exposed proteins against proteases.
APA, Harvard, Vancouver, ISO, and other styles
48

Skotnicka, Dorota, Tobias Petters, Jan Heering, Michael Hoppert, Volkhard Kaever, and Lotte Søgaard-Andersen. "Cyclic Di-GMP Regulates Type IV Pilus-Dependent Motility in Myxococcus xanthus." Journal of Bacteriology 198, no. 1 (June 29, 2015): 77–90. http://dx.doi.org/10.1128/jb.00281-15.

Full text
Abstract:
ABSTRACTThe nucleotide-based second messenger bis-(3′-5′)-cyclic dimeric GMP (c-di-GMP) is involved in regulating a plethora of processes in bacteria that are typically associated with lifestyle changes.Myxococcus xanthusundergoes major lifestyle changes in response to nutrient availability, with the formation of spreading colonies in the presence of nutrients and spore-filled fruiting bodies in the absence of nutrients. Here, we investigated the function of c-di-GMP inM. xanthusand show that this bacterium synthesizes c-di-GMP during growth. Manipulation of the c-di-GMP level by expression of either an active, heterologous diguanylate cyclase or an active, heterologous phosphodiesterase correlated with defects in type IV pilus (T4P)-dependent motility, whereas gliding motility was unaffected. An increased level of c-di-GMP correlated with reduced transcription of thepilAgene (which encodes the major pilin of T4P), reduced the assembly of T4P, and altered cell agglutination, whereas a decreased c-di-GMP level correlated with altered cell agglutination. The systematic inactivation of the 24 genes inM. xanthusencoding proteins containing GGDEF, EAL, or HD-GYP domains, which are associated with c-di-GMP synthesis, degradation, or binding, identified three genes encoding proteins important for T4P-dependent motility, whereas all mutants had normal gliding motility. Purified DmxA had diguanylate cyclase activity, whereas the hybrid histidine protein kinases TmoK and SgmT, each of which contains a GGDEF domain, did not have diguanylate cyclase activity. These results demonstrate that c-di-GMP is important for T4P-dependent motility inM. xanthus.IMPORTANCEWe provide the first direct evidence thatM. xanthussynthesizes c-di-GMP and demonstrate that c-di-GMP is important for T4P-dependent motility, whereas we did not obtain evidence that c-di-GMP regulates gliding motility. The data presented uncovered a novel mechanism for regulation of T4P-dependent motility, in which increased levels of c-di-GMP inhibit transcription of thepilAgene (which encodes the major pilin of T4P), ultimately resulting in the reduced assembly of T4P. Moreover, we identified an enzymatically active diguanylate cyclase that is important for T4P-dependent motility.
APA, Harvard, Vancouver, ISO, and other styles
49

Ryan, Robert P., and J. Maxwell Dow. "Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction inXanthomonas campestris." Virulence 1, no. 5 (September 2010): 404–8. http://dx.doi.org/10.4161/viru.1.5.12704.

Full text
APA, Harvard, Vancouver, ISO, and other styles
50

Ryan, Robert P., Yvonne McCarthy, Patrick A. Kiely, Rosemary O'Connor, Chuck S. Farah, Judith P. Armitage, and J. Maxwell Dow. "Retracted: Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility inXanthomonas campestris." Molecular Microbiology 86, no. 3 (August 31, 2012): 557–67. http://dx.doi.org/10.1111/mmi.12000.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the bibliographies on the topic 'GGDEF' for other source types:
Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography