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  • 1
    Language: English
    In: Journal of bacteriology, February 2009, Vol.191(3), pp.683-6
    Description: The small molecule cyclic (5'--〉3')-diguanosine monophosphate (c-di-GMP) created through the condensation of two molecules of GTP is a novel secondary messenger in Bacteria. ...
    Keywords: Anaplasma Phagocytophilum -- Metabolism ; Cyclic Gmp -- Analogs & Derivatives ; Signal Transduction -- Physiology
    ISSN: 00219193
    E-ISSN: 1098-5530
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  • 2
    In: Nature, 2013, Vol.497(7449), p.321
    Description: From the authors' results, it also follows that the frequency distribution of bacterial visits varies as a power of Psl secretion. [...]Zhao and colleagues suggest that, for the bacteria, this system results in some 'elite' bacteria being located at sites that are extremely rich in communally produced Psl, and that this social structure is required for microcolony formation. Here, the exploratory movement facilitates target-site selection and cooperative invasion by the bacteria as they infect these cells. [...]it seems that the onset of biofilm formation and the infection process are governed by similar basic principles, suggesting that this behaviour may be a target for developing new ways to inhibit surface colonization by bacteria or to prevent infection.
    Keywords: Bacteriology ; Microbiology ; Bacteria ; Motility;
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 3
    Language: English
    In: Journal of bacteriology, December 2011, Vol.193(23), pp.6443-51
    Description: In Salmonella enterica serovar Typhimurium, a biofilm mode of growth known as the rdar morphotype is regulated by several networks which sense multiple environmental signals. The transcriptional regulator CsgD is the major target for these regulatory pathways. In this study, we show that two lytic transglycosylases of family I, MltE and MltC, in combination increase CsgD expression and rdar morphotype. MltE and MltC, which share a highly similar transglycosylase SLT domain, work redundantly to regulate CsgD at the transcriptional and posttranscriptional levels. The effect of MltE and MltC on CsgD levels was independent of the known regulatory pathways that sense cell envelope stress. These findings reveal, for the first time, a specific function of lytic transglycosylases in S. Typhimurium and suggest the existence of a new signaling pathway that links cell wall turnover to biofilm formation.
    Keywords: Biofilms ; Gene Expression Regulation, Bacterial ; Bacterial Proteins -- Metabolism ; Cell Wall -- Metabolism ; Glycosyltransferases -- Metabolism ; Salmonella Typhimurium -- Enzymology
    ISSN: 00219193
    E-ISSN: 1098-5530
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  • 4
    Language: English
    In: Journal of bacteriology, 01 March 2017, Vol.199(5)
    Description: Cyclic di-GMP was the first cyclic dinucleotide second messenger described, presaging the discovery of additional cyclic dinucleotide messengers in bacteria and eukaryotes. The GGDEF diguanylate cyclase (DGC) and EAL and HD-GYP phosphodiesterase (PDE) domains conduct the turnover of cyclic di-GMP. These three unrelated domains belong to superfamilies that exhibit significant variations in function, and they include both enzymatically active and inactive members, with a subset involved in synthesis and degradation of other cyclic dinucleotides. Here, we summarize current knowledge of sequence and structural variations that underpin the functional diversification of cyclic di-GMP turnover proteins. Moreover, we highlight that superfamily diversification is not restricted to cyclic di-GMP signaling domains, as particular DHH/DHHA1 domain and HD domain proteins have been shown to act as cyclic di-AMP phosphodiesterases. We conclude with a consideration of the current limitations that such diversity of action places on bioinformatic prediction of the roles of GGDEF, EAL, and HD-GYP domain proteins.
    Keywords: Dhh/Dhha1 Domain ; Eal Domain ; Ggdef Domain ; HD-Gyp Domain ; Cyclic Gamp ; Cyclic Di-Amp ; Cyclic Di-Gmp ; Cyclic Dinucleotide Second Messenger ; Second Messenger ; Bacteria -- Metabolism ; Bacterial Proteins -- Metabolism ; Cyclic Gmp -- Analogs & Derivatives ; Gene Expression Regulation, Bacterial -- Physiology
    ISSN: 00219193
    E-ISSN: 1098-5530
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  • 5
    In: Molecular Microbiology, January 2014, Vol.91(1), pp.1-5
    Description: The major sessility‐motility lifestyle change and additional fundamental aspects of bacterial physiology, behaviour and morphology are regulated by the secondary messenger cyclic di‐ (c‐di‐). Although the c‐di‐ metabolizing enzymes and many receptors have been readily characterized upon discovery, the ‐ domain c‐di‐ phosphodiesterase family remained underinvestigated. In this issue of , ellini . provide an important step towards functional and structural characterization of the previously neglected ‐ domain family by resolving the crystal structure of , a catalytically active family member from the thermophilic bacterium . The crystal structure revealed a novel tri‐nuclear catalytic iron centre involved in c‐di‐ binding and catalysis and provides the structural basis to subsequently characterize in detail the catalytic mechanism of hydrolysis of c‐di‐ to by ‐ domains.
    Keywords: High Definition Television;
    ISSN: 0950-382X
    E-ISSN: 1365-2958
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  • 6
    Language: English
    In: Science signaling, 09 June 2015, Vol.8(380), pp.fs12
    Description: In this issue of Science Signaling, Mills et al. show that the amino acid ʟ-arginine increases the concentration of the second messenger c-di-GMP in Salmonella enterica serovar Typhimurium through a specific diguanylate cyclase, leading to increased production of the exopolysaccharide cellulose, which is an extracellular matrix component of environmental and host-associated biofilms.
    Keywords: Signal Transduction ; Arginine -- Metabolism ; Cyclic Gmp -- Analogs & Derivatives ; Periplasm -- Metabolism ; Salmonella Typhimurium -- Metabolism
    ISSN: 19450877
    E-ISSN: 1937-9145
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  • 7
    Language: English
    In: Environmental microbiology, August 2012, Vol.14(8), pp.1817-29
    Description: The secondary messenger cyclic di-GMP coordinately regulates the transition between motility/sessility/virulence in bacterial populations and upon adaptation to novel habitats. Thereby, multiple independent regulatory circuits regulate a diversity of targets. This specific output response is surprising considering the diverse physiological processes regulated by this signalling molecule, which range from transcription to proteolysis and clearly demonstrates the presence of sophisticated developmental programmes in these so-called simple organisms.
    Keywords: Bacterial Physiological Phenomena ; Cyclic Gmp -- Analogs & Derivatives ; Second Messenger Systems -- Physiology
    ISSN: 14622912
    E-ISSN: 1462-2920
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  • 8
    Language: English
    In: PLoS ONE, 01 January 2014, Vol.9(8), p.e106095
    Description: In Salmonella enterica serovar Typhimurium (S. Typhimurium), biofilm-formation is controlled by the cytoplasmic intracellular small-molecular second messenger cyclic 3', 5'-di- guanosine monophosphate (c-di-GMP) through the activities of GGDEF and EAL domain proteins. Here we describe that deleting either dsbA or dsbB, respectively encoding a periplasmic protein disulfide oxidase and a cytoplasmic membrane disulfide oxidoreductase, resulted in increased biofilm-formation on solid medium. This increased biofilm-formation, defined as a red, dry and rough (rdar) colony morphotype, paralleled with enhanced expression of the biofilm master regulator CsgD and the biofilm-associated fimbrial subunit CsgA. Deleting csgD in either dsb mutant abrogated the enhanced biofilm-formation. Likewise, overexpression of the c-di-GMP phosphodiesterase YhjH, or mutationally inactivating the CsgD activator EAL-domain protein YdiV, reduced biofilm-formation in either of the dsb mutants. Intriguingly, deleting the GGDEF-EAL domain protein gene STM3615 (yhjK), previously not connected to rdar morphotype development, also abrogated the escalated rdar morphotype formation in dsb mutant backgrounds. Enhanced biofilm-formation in dsb mutants was furthermore annulled by exposure to the protein disulfide catalyst copper chloride. When analyzed for the effect of exogenous reducing stress on biofilm-formation, both dsb mutants initially showed an escalated rdar morphotype development that later dissolved to reveal a smooth mucoid colony morphotype. From these results we conclude that biofilm-development in S. Typhimurium is affected by periplasmic protein disulphide bond status through CsgD, and discuss the involvement of selected GGDEF/EAL domain protein(s) as signaling mediators.
    Keywords: Sciences (General)
    E-ISSN: 1932-6203
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  • 9
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 09 January 2018, Vol.115(2), pp.E273-E282
    Description: AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species and subsequently abundant clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of primarily in stationary phase and boosts heat resistance 100-fold when expressed in This qualifies ClpG as a potential persistence and virulence factor in .
    Keywords: AAA+ Protein ; Hsp100 ; Heat Tolerance ; Mobile Genetic Element ; Protein Disaggregation ; Adaptation, Physiological ; Hot Temperature ; Bacterial Proteins -- Metabolism ; Pseudomonas Aeruginosa -- Enzymology
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 10
    In: Molecular Microbiology, August 2010, Vol.77(3), pp.771-786
    Description: The transcriptional regulator CsgD of serovar Typhimurium ( Typhimurium) is a major regulator of biofilm formation required for the expression of , which encodes curli fimbriae, and , coding for a diguanylate cyclase. CsgD is a response regulator with an N‐terminal receiver domain with a conserved aspartate (D59) as a putative target site for phosphorylation and a C‐terminal LuxR‐like helix–turn–helix DNA binding motif, but the mechanisms of target gene activation remained unclear. To study the DNA‐binding properties of CsgD we used electrophoretic mobility shift assays and DNase I footprint analysis to show that unphosphorylated CsgD‐His binds specifically to the and promoter regions. transcription analysis revealed that CsgD‐His is crucial for the expression of and . CsgD‐His is phosphorylated by acetyl phosphate , which decreases its DNA‐binding properties. The functional impact of D59 was demonstrated as Typhimurium strains expressing modified CsgD protein (D59E and D59N) were dramatically reduced in biofilm formation due to decreased protein stability and DNA‐binding properties in the case of D59E. In summary, our findings suggest that the response regulator CsgD functions in its unphosphorylated form under the conditions of biofilm formation investigated in this study.
    Keywords: Promoters ; Phosphorylation ; Pili ; DNA ; Transcription ; Acetyl Phosphate ; Deoxyribonuclease ; Biofilms ; Electrophoretic Mobility ; Transcription Activation ; Salmonella Enterica ; Salmonella Typhimurium ; Animal Diseases;
    ISSN: 0950-382X
    E-ISSN: 1365-2958
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