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Volumn 4, Issue 3, 2009, Pages 341-358

Regulation of c-di-GMP metabolism in biofilms

Author keywords

C di GMP; EAL; Environmental signal; GGDEF; Global regulator; Multilayer control; Two component system

Indexed keywords

BACTERIAL PROTEIN; CYCLIC AMP; CYCLIC GMP; GUANYLATE CYCLASE; MERR PROTEIN; PHOSPHODIESTERASE; PHOSPHOTRANSFERASE; PROTEIN CSGD; PROTEIN CSRA; PROTEIN HISTIDINE KINASE; PROTEIN ROCR; PROTEIN RPFC; PROTEIN RPFG; PROTEIN VPS; PROTEIN WSPA; PROTEIN WSPE; PROTEIN WSPF; PROTEIN YCIR; PROTEIN YDAM; PROTEIN YEGE; PROTEIN YHJH; RNA BINDING PROTEIN; RNA POLYMERASE; SIGMA FACTOR; SIGMA FACTOR RPOS; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FLIA; UNCLASSIFIED DRUG; BIS(3',5') CYCLIC DIGUANYLIC ACID; BIS(3',5')-CYCLIC DIGUANYLIC ACID; DRUG DERIVATIVE; ENZYME;

EID: 65549130634     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/fmb.09.7     Document Type: Review
Times cited : (52)

References (129)
  • 1
    • 0023090935 scopus 로고
    • Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid
    • Ross P, Weinhouse H, Aloni Y et al.: Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid. Nature 325, 279-281 (1987).
    • (1987) Nature , vol.325 , pp. 279-281
    • Ross, P.1    Weinhouse, H.2    Aloni, Y.3
  • 2
    • 0031783181 scopus 로고    scopus 로고
    • Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: Genetic organization and occurrence of conserved domains in isoenzymes
    • Tal R, Wong HC, Calhoon R et al.: Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes. J. Bacteriol. 180, 4416-4425 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 4416-4425
    • Tal, R.1    Wong, H.C.2    Calhoon, R.3
  • 3
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel diguanylate cyclase output, domain
    • Paul R, Weiser S, Amiot NC et al.: Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel diguanylate cyclase output, domain. Genes Dev. 18, 715-727 (2004).
    • (2004) Genes Dev , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3
  • 4
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov DA, Tarutina M, Moskvin OV, Gomelsky M: Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187, 1792-1798 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 5
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • Simm R, Morr M, Kader A, Nimtz M, Romling U: GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol. 53, 1123-1134 (2004).
    • (2004) Mol. Microbiol , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 6
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt AJ, Ryjenkov DA, Gomelsky M: The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187, 4774-4781 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 7
    • 33646249963 scopus 로고    scopus 로고
    • Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover
    • Ryan RP, Fouhy Y, Lucey JF et al.: Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover. Proc. Natl Acad. Sci. USA 103, 6712-6717 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6712-6717
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3
  • 8
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • Tamayo R, Tischler AD, Camilli A: The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J. Biol. Chem. 280, 33324-33330 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 9
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen M, Christen B, Folcher M, Schauerte A, Jenal U: Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 280, 30829-30837 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 10
    • 0141818949 scopus 로고    scopus 로고
    • Involvement of bacterial migration in the development of complex multicellular structures in Pseudomonas aeruginosa biofilms
    • Klausen M, Aaes-Jorgensen A, Molin S, Tolker-Nielsen T: Involvement of bacterial migration in the development of complex multicellular structures in Pseudomonas aeruginosa biofilms. Mol. Microbiol. 50, 61-68 (2003).
    • (2003) Mol. Microbiol , vol.50 , pp. 61-68
    • Klausen, M.1    Aaes-Jorgensen, A.2    Molin, S.3    Tolker-Nielsen, T.4
  • 11
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin MY, Nikolskaya AN, Koonin EV: Novel domains of the prokaryotic two-component signal transduction systems. FEMS Mirobiol. Lett. 203, 11-21 (2001).
    • (2001) FEMS Mirobiol. Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 12
    • 2642554922 scopus 로고    scopus 로고
    • Bacterial signal transduction network in a genomic perspective
    • Galperin MY: Bacterial signal transduction network in a genomic perspective. Environ. Microbiol. 6, 552-567 (2004).
    • (2004) Environ. Microbiol , vol.6 , pp. 552-567
    • Galperin, M.Y.1
  • 13
    • 14244256556 scopus 로고    scopus 로고
    • Genome-wide analysis of the general stress response network in Escherichia coli: σS-dependent genes, promoters, and σ factor selectivity
    • Weber H, Polen T, Heuveling J, Wendisch VF, Hengge R: Genome-wide analysis of the general stress response network in Escherichia coli: σS-dependent genes, promoters, and σ factor selectivity. J. Bacteriol. 187, 1591-1603 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 1591-1603
    • Weber, H.1    Polen, T.2    Heuveling, J.3    Wendisch, V.F.4    Hengge, R.5
  • 14
    • 0031896213 scopus 로고    scopus 로고
    • Multicellular and aggregative behavior of Salmonella Typhimurium strains is controlled by mutations in the agfD promoter
    • Romling U, Sierralta WD, Eriksson K, Normark S: Multicellular and aggregative behavior of Salmonella Typhimurium strains is controlled by mutations in the agfD promoter. Mol. Microbiol. 28, 249-264 (1998).
    • (1998) Mol. Microbiol , vol.28 , pp. 249-264
    • Romling, U.1    Sierralta, W.D.2    Eriksson, K.3    Normark, S.4
  • 15
    • 0036208369 scopus 로고    scopus 로고
    • Statistical analysis of Pseudomonas aeruginosa biofilm development: Impact of mutations in genes involved in twitching motility, cell-to-cell signaling, and stationary-phase σ factor expression
    • Heydorn A, Ersboll B, Kato J et al.: Statistical analysis of Pseudomonas aeruginosa biofilm development: impact of mutations in genes involved in twitching motility, cell-to-cell signaling, and stationary-phase σ factor expression. Appl. Environ. Microbiol. 68, 2008-2017 (2002).
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 2008-2017
    • Heydorn, A.1    Ersboll, B.2    Kato, J.3
  • 16
    • 0032851954 scopus 로고    scopus 로고
    • Impact of rpoS deletion on Escherichia coli biofilms
    • Adams JL, McLean RJ: Impact of rpoS deletion on Escherichia coli biofilms. Appl. Environ. Microbiol. 65, 4285-4287 (1999).
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 4285-4287
    • Adams, J.L.1    McLean, R.J.2
  • 17
    • 0043166926 scopus 로고    scopus 로고
    • Complex regulation of csgD promoter activity by global regulatory proteins
    • Gerstel U, Park C, Romling U: Complex regulation of csgD promoter activity by global regulatory proteins. Mol. Microbiol. 49, 639-654 (2003).
    • (2003) Mol. Microbiol , vol.49 , pp. 639-654
    • Gerstel, U.1    Park, C.2    Romling, U.3
  • 18
    • 33644866120 scopus 로고    scopus 로고
    • Gene expression regulation by the Curli activator CsgD protein: Modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion
    • Brombacher E, Baratto A, Dorel C, Landini P: Gene expression regulation by the Curli activator CsgD protein: modulation of cellulose biosynthesis and control of negative determinants for microbial adhesion. J. Bacteriol. 188, 2027-2037 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 2027-2037
    • Brombacher, E.1    Baratto, A.2    Dorel, C.3    Landini, P.4
  • 19
    • 33744717869 scopus 로고    scopus 로고
    • Crl activates transcription initiation of RpoS-regulated genes involved in the multicellular behavior of Salmonella enterica serovar Typhimurium
    • Robbe-Saule V, Jaumouille V, Prevost MC et al.: Crl activates transcription initiation of RpoS-regulated genes involved in the multicellular behavior of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188, 3983-3994 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 3983-3994
    • Robbe-Saule, V.1    Jaumouille, V.2    Prevost, M.C.3
  • 20
    • 0034742539 scopus 로고    scopus 로고
    • MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis by Escherichia coli and Salmonella enterica serovar Typhimurium
    • Brown PK, Dozois CM, Nickerson CA, Zuppardo A, Terlonge J, Curtiss R 3rd: MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis by Escherichia coli and Salmonella enterica serovar Typhimurium. Mol. Microbiol. 41, 349-363 (2001).
    • (2001) Mol. Microbiol , vol.41 , pp. 349-363
    • Brown, P.K.1    Dozois, C.M.2    Nickerson, C.A.3    Zuppardo, A.4    Terlonge, J.5    Curtiss 3rd, R.6
  • 21
    • 33750432511 scopus 로고    scopus 로고
    • Cyclic-di-GMP-mediated signalling within the σ-network of Escherichia coli
    • Weber H, Pesavento C, Possling A, Tischendorf G, Hengge R: Cyclic-di-GMP-mediated signalling within the σ-network of Escherichia coli. Mol. Microbiol. 62, 1014-1034 (2006).
    • (2006) Mol. Microbiol , vol.62 , pp. 1014-1034
    • Weber, H.1    Pesavento, C.2    Possling, A.3    Tischendorf, G.4    Hengge, R.5
  • 22
    • 51149098349 scopus 로고    scopus 로고
    • Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli
    • Pesavento C, Becker G, Sommerfeldt N et al.: Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli. Genes Dev. 22, 2434-2446 (2008).
    • (2008) Genes Dev , vol.22 , pp. 2434-2446
    • Pesavento, C.1    Becker, G.2    Sommerfeldt, N.3
  • 23
    • 34848889244 scopus 로고    scopus 로고
    • A comprehensive genetic characterization of bacterial motility
    • Girgis HS, Liu Y, Ryu WS, Tavazoie S: A comprehensive genetic characterization of bacterial motility. PLoS Genet. 3, 1644-1660 (2007).
    • (2007) PLoS Genet , vol.3 , pp. 1644-1660
    • Girgis, H.S.1    Liu, Y.2    Ryu, W.S.3    Tavazoie, S.4
  • 24
    • 33645819810 scopus 로고    scopus 로고
    • Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium
    • Kader A, Simm R, Gerstel U, Morr M, Romling U: Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 60, 602-616 (2006).
    • (2006) Mol. Microbiol , vol.60 , pp. 602-616
    • Kader, A.1    Simm, R.2    Gerstel, U.3    Morr, M.4    Romling, U.5
  • 25
    • 34247566143 scopus 로고    scopus 로고
    • Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium
    • Simm R, Lusch A, Kader A, Andersson M, Romling U: Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium. J. Bacteriol. 189, 3613-3623 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 3613-3623
    • Simm, R.1    Lusch, A.2    Kader, A.3    Andersson, M.4    Romling, U.5
  • 26
    • 50049101426 scopus 로고    scopus 로고
    • Bringing order to a complex molecular machine: The assembly of the bacterial flagella
    • Apel D, Surette MG: Bringing order to a complex molecular machine: the assembly of the bacterial flagella. Biochim. Biophys. Acta 1778, 1851-1858 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1851-1858
    • Apel, D.1    Surette, M.G.2
  • 27
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FF, Hughes KT: Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6, 455-465 (2008).
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 28
    • 33644861941 scopus 로고    scopus 로고
    • Identification of new flagellar genes of Salmonella enterica serovar Typhimurium
    • Frye J, Karlinsey JE, Felise HR et al.: Identification of new flagellar genes of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188, 2233-2243 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 2233-2243
    • Frye, J.1    Karlinsey, J.E.2    Felise, H.R.3
  • 29
    • 0034721950 scopus 로고    scopus 로고
    • Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli
    • Ko M, Park C: Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli. J. Mol. Biol. 303, 371-382 (2000).
    • (2000) J. Mol. Biol , vol.303 , pp. 371-382
    • Ko, M.1    Park, C.2
  • 30
    • 36348960267 scopus 로고    scopus 로고
    • The flagellar σ-factor FliA regulates adhesion and invasion of Crohn disease-associated Escherichia coli via a cyclic dimeric GMP-dependent pathway
    • Claret L, Miquel S, Vieille N, Ryjenkov DA, Gomelsky M, Darfeuille-Michaud A: The flagellar σ-factor FliA regulates adhesion and invasion of Crohn disease-associated Escherichia coli via a cyclic dimeric GMP-dependent pathway. J. Biol. Chem. 282, 33275-33283 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 33275-33283
    • Claret, L.1    Miquel, S.2    Vieille, N.3    Ryjenkov, D.A.4    Gomelsky, M.5    Darfeuille-Michaud, A.6
  • 31
    • 33750044865 scopus 로고    scopus 로고
    • The PilZ domain is a receptor for the second messenger c-di-GMP: The PilZ domain protein YcgR controls motility in enterobacteria
    • Ryjenkov DA, Simm R, Romling U, Gomelsky M: The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria. J. Biol. Chem. 281, 30310-30314 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Romling, U.3    Gomelsky, M.4
  • 32
    • 3242816202 scopus 로고    scopus 로고
    • Photoresponsive cAMP signal transduction in cyanobacteria
    • Ohmori M, Okamoto S: Photoresponsive cAMP signal transduction in cyanobacteria. Photochem. Photobiol. Sci. 3, 503-511 (2004).
    • (2004) Photochem. Photobiol. Sci , vol.3 , pp. 503-511
    • Ohmori, M.1    Okamoto, S.2
  • 34
    • 0037046271 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Choice of the carbon source and autoregulatory limitation of sugar utilization
    • Bruckner R, Titgemeyer F: Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol. Lett. 209, 141-148 (2002).
    • (2002) FEMS Microbiol. Lett , vol.209 , pp. 141-148
    • Bruckner, R.1    Titgemeyer, F.2
  • 35
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb A, Busby S, Buc H, Garges S, Adhya S: Transcriptional regulation by cAMP and its receptor protein. Annu. Rev. Biochem. 62, 749-795 (1993).
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 749-795
    • Kolb, A.1    Busby, S.2    Buc, H.3    Garges, S.4    Adhya, S.5
  • 36
    • 0344153756 scopus 로고    scopus 로고
    • Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: Exploiting the metabolic spectrum by controlling alternative gene programs
    • Korner H, Sofia HJ, Zumft WG: Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol. Rev. 27, 559-592 (2003).
    • (2003) FEMS Microbiol. Rev , vol.27 , pp. 559-592
    • Korner, H.1    Sofia, H.J.2    Zumft, W.G.3
  • 37
    • 60849127612 scopus 로고    scopus 로고
    • Computational prediction of cAMP receptor protein (CRP) binding sites in cyanobacterial genomes
    • Xu M, Su Z: Computational prediction of cAMP receptor protein (CRP) binding sites in cyanobacterial genomes. BMC Genomics 10, 23 (2009).
    • (2009) BMC Genomics , vol.10 , pp. 23
    • Xu, M.1    Su, Z.2
  • 38
    • 44949152721 scopus 로고    scopus 로고
    • The cyclic AMP-dependent catabolite repression system of Serratia marcescens mediates biofilm formation through regulation of type 1 fimbriae
    • Kalivoda EJ, Stella NA, O'Dee DM, Nau GJ, Shanks RM: The cyclic AMP-dependent catabolite repression system of Serratia marcescens mediates biofilm formation through regulation of type 1 fimbriae. Appl. Environ. Microbiol. 74, 3461-3470 (2008).
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 3461-3470
    • Kalivoda, E.J.1    Stella, N.A.2    O'Dee, D.M.3    Nau, G.J.4    Shanks, R.M.5
  • 39
    • 34948829648 scopus 로고    scopus 로고
    • The cyclic AMP receptor protein modulates quorum sensing, motility and multiple genes that affect intestinal colonization in Vibrio cholerae
    • Liang W, Pascual-Montano A, Silva AJ, Benitez JA: The cyclic AMP receptor protein modulates quorum sensing, motility and multiple genes that affect intestinal colonization in Vibrio cholerae. Microbiology 153, 2964-2975 (2007).
    • (2007) Microbiology , vol.153 , pp. 2964-2975
    • Liang, W.1    Pascual-Montano, A.2    Silva, A.J.3    Benitez, J.A.4
  • 40
    • 36649025757 scopus 로고    scopus 로고
    • The cyclic AMP receptor protein modulates colonial morphology in Vibrio cholerae
    • Liang W, Silva AJ, Benitez JA: The cyclic AMP receptor protein modulates colonial morphology in Vibrio cholerae. Appl. Environ. Microbiol. 73, 7482-7487 (2007).
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 7482-7487
    • Liang, W.1    Silva, A.J.2    Benitez, J.A.3
  • 41
    • 13244255243 scopus 로고    scopus 로고
    • Induction of rapid detachment in Shewanella oneidensis MR-1 biofilms
    • Thormann KM, Saville RM, Shukla S, Spormann AM: Induction of rapid detachment in Shewanella oneidensis MR-1 biofilms. J. Bacteriol. 187, 1014-1021 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 1014-1021
    • Thormann, K.M.1    Saville, R.M.2    Shukla, S.3    Spormann, A.M.4
  • 42
    • 0036267354 scopus 로고    scopus 로고
    • Catabolite repression of Escherichia coli biofilm formation
    • Jackson DW, Simecka JW, Romeo T: Catabolite repression of Escherichia coli biofilm formation. J. Bacteriol. 184, 3406-3410 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 3406-3410
    • Jackson, D.W.1    Simecka, J.W.2    Romeo, T.3
  • 43
    • 37549017288 scopus 로고    scopus 로고
    • A novel role for enzyme I of the Vibrio cholerae phosphoenolpyruvate phosphotransferase system in regulation of growth in a biofilm
    • Houot L, Watnick PI: A novel role for enzyme I of the Vibrio cholerae phosphoenolpyruvate phosphotransferase system in regulation of growth in a biofilm. J. Bacteriol. 190, 311-320 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 311-320
    • Houot, L.1    Watnick, P.I.2
  • 44
    • 53849110599 scopus 로고    scopus 로고
    • Interplay between cyclic AMP-cyclic AMP receptor protein and cyclic di-GMP signaling in Vibrio cholerae biofilm formation
    • Fong JC, Yildiz FH: Interplay between cyclic AMP-cyclic AMP receptor protein and cyclic di-GMP signaling in Vibrio cholerae biofilm formation. J. Bacteriol. 190, 6646-6659 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 6646-6659
    • Fong, J.C.1    Yildiz, F.H.2
  • 48
    • 0037123780 scopus 로고    scopus 로고
    • Small talk. Cell-to-cell communication in bacteria
    • Bassler BL: Small talk. Cell-to-cell communication in bacteria. Cell 109, 421-424 (2002).
    • (2002) Cell , vol.109 , pp. 421-424
    • Bassler, B.L.1
  • 49
    • 27944442272 scopus 로고    scopus 로고
    • Quorum sensing: Cell-to-cell communication in bacteria
    • Waters CM, Bassler BL: Quorum sensing: cell-to-cell communication in bacteria. Annu. Rev. Cell Dev. Biol. 21, 319-346 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 319-346
    • Waters, C.M.1    Bassler, B.L.2
  • 50
    • 58149511939 scopus 로고    scopus 로고
    • Distinct sensory pathways in Vibrio cholerae El Tor and classical biotypes modulate c-di-GMP levels to control biofilm formation
    • Hammer BK, Bassler BL: Distinct sensory pathways in Vibrio cholerae El Tor and classical biotypes modulate c-di-GMP levels to control biofilm formation. J. Bacteriol. 191 (1), 169-177 (2008).
    • (2008) J. Bacteriol , vol.191 , Issue.1 , pp. 169-177
    • Hammer, B.K.1    Bassler, B.L.2
  • 51
    • 41549091882 scopus 로고    scopus 로고
    • Quorum sensing controls biofilm formation in Vibrio cholerae through modulation of cyclic di-GMP levels and repression of vpsT
    • Waters CM, Lu W, Rabinowitz JD, Bassler BL: Quorum sensing controls biofilm formation in Vibrio cholerae through modulation of cyclic di-GMP levels and repression of vpsT. J. Bacteriol. 190, 2527-2536 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 2527-2536
    • Waters, C.M.1    Lu, W.2    Rabinowitz, J.D.3    Bassler, B.L.4
  • 52
    • 33644517930 scopus 로고    scopus 로고
    • Bacterial small-molecule signaling pathways
    • Camilli A, Bassler BL: Bacterial small-molecule signaling pathways. Science 311, 1113-1116 (2006).
    • (2006) Science , vol.311 , pp. 1113-1116
    • Camilli, A.1    Bassler, B.L.2
  • 53
    • 0030696361 scopus 로고    scopus 로고
    • Characterization of hapR, a positive regulator of the Vibrio cholerae HA/protease gene hap, and its identification as a functional homologue of the Vibrio harveyi luxR gene
    • Jobling MG, Holmes RK: Characterization of hapR, a positive regulator of the Vibrio cholerae HA/protease gene hap, and its identification as a functional homologue of the Vibrio harveyi luxR gene. Mol. Microbiol. 26, 1023-1034 (1997).
    • (1997) Mol. Microbiol , vol.26 , pp. 1023-1034
    • Jobling, M.G.1    Holmes, R.K.2
  • 55
    • 3142564584 scopus 로고    scopus 로고
    • The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae
    • Lenz DH, Mok KC, Lilley BN, Kulkarni RV, Wingreen NS, Bassler BL: The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae. Cell 118, 69-82 (2004).
    • (2004) Cell , vol.118 , pp. 69-82
    • Lenz, D.H.1    Mok, K.C.2    Lilley, B.N.3    Kulkarni, R.V.4    Wingreen, N.S.5    Bassler, B.L.6
  • 56
    • 1342325445 scopus 로고    scopus 로고
    • VpsT is a transcriptional regulator required for expression of vps biosynthesis genes and the development of rugose colonial morphology in Vibrio cholerae O1 El Tor
    • Casper-Lindley C, Yildiz FH: VpsT is a transcriptional regulator required for expression of vps biosynthesis genes and the development of rugose colonial morphology in Vibrio cholerae O1 El Tor. J. Bacteriol. 186, 1574-1578 (2004).
    • (2004) J. Bacteriol , vol.186 , pp. 1574-1578
    • Casper-Lindley, C.1    Yildiz, F.H.2
  • 57
    • 0035114220 scopus 로고    scopus 로고
    • VpsR, a member of the response regulators of the two-component regulatory systems, is required for expression of vps biosynthesis genes and EPS (ETr)-associated phenotypes in Vibrio cholerae O1 El Tor
    • Yildiz FH, Dolganov NA, Schoolnik GK: VpsR, a member of the response regulators of the two-component regulatory systems, is required for expression of vps biosynthesis genes and EPS (ETr)-associated phenotypes in Vibrio cholerae O1 El Tor. J. Bacteriol 183, 1716-1726 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 1716-1726
    • Yildiz, F.H.1    Dolganov, N.A.2    Schoolnik, G.K.3
  • 58
    • 31844439534 scopus 로고    scopus 로고
    • Genetic and phehotypic diversity of quorum-sensing systems in clinical and environmental isolates of Vibrio cholerae
    • Joelsson A, Liu Z, Zhu J: Genetic and phehotypic diversity of quorum-sensing systems in clinical and environmental isolates of Vibrio cholerae. Infect. Immun. 74, 1141-1147 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 1141-1147
    • Joelsson, A.1    Liu, Z.2    Zhu, J.3
  • 59
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler AD, Camilli A: Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol. Microbiol. 53, 857-869 (2004).
    • (2004) Mol. Microbiol , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 60
    • 52649135568 scopus 로고    scopus 로고
    • The Vibrio cholerae hybrid sensor kinase VieS contributes to motility and biofilm regulation by altering the cyclic diguanylate level
    • Martinez-Wilson HF, Tamayo R, Tischler AD, Lazinski DW, Camilli A: The Vibrio cholerae hybrid sensor kinase VieS contributes to motility and biofilm regulation by altering the cyclic diguanylate level. J. Bacteriol. 190, 6439-6447 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 6439-6447
    • Martinez-Wilson, H.F.1    Tamayo, R.2    Tischler, A.D.3    Lazinski, D.W.4    Camilli, A.5
  • 61
    • 0034128490 scopus 로고    scopus 로고
    • AgfD, the checkpoint of multicellular and aggregative behavior in Salmonella Typhimurium regulates at least two independent pathways
    • Romling U, Rohde M, Olsen A, Normark S, Reinkoster J: AgfD, the checkpoint of multicellular and aggregative behavior in Salmonella Typhimurium regulates at least two independent pathways. Mol. Microbiol. 36, 10-23 (2000).
    • (2000) Mol. Microbiol , vol.36 , pp. 10-23
    • Romling, U.1    Rohde, M.2    Olsen, A.3    Normark, S.4    Reinkoster, J.5
  • 62
    • 0035065254 scopus 로고    scopus 로고
    • The multicellular morphotypes of Salmonella Typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
    • Zogaj X, Nimtz M, Rohde M, Bokranz W, Romling U: The multicellular morphotypes of Salmonella Typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix. Mol. Microbiol. 39, 1452-1463 (2001).
    • (2001) Mol. Microbiol , vol.39 , pp. 1452-1463
    • Zogaj, X.1    Nimtz, M.2    Rohde, M.3    Bokranz, W.4    Romling, U.5
  • 63
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto K, Ishihama A: Transcriptional response of Escherichia coli to external copper. Mol. Microbiol. 56, 215-227 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 64
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • Yamamoto K, Ishihama A: Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci. Biotechnol Biochem. 70, 1688-1695 (2006).
    • (2006) Biosci. Biotechnol Biochem , vol.70 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2
  • 65
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio TL: Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56, 1119-1128 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 66
    • 51649096200 scopus 로고    scopus 로고
    • The RNA binding protein CsrA controls cyclic di-GMP metabolism by direcdy regulating the expression of GGDEF proteins
    • Jonas K, Edwards AN, Simm R, Romeo T, Romling U, Melefors O: The RNA binding protein CsrA controls cyclic di-GMP metabolism by direcdy regulating the expression of GGDEF proteins. Mol. Microbiol. 70, 236-257 (2008).
    • (2008) Mol. Microbiol , vol.70 , pp. 236-257
    • Jonas, K.1    Edwards, A.N.2    Simm, R.3    Romeo, T.4    Romling, U.5    Melefors, O.6
  • 67
    • 37349027967 scopus 로고    scopus 로고
    • Gac/Rsm signal transduction pathway of γ-proteobacteria: From RNA recognition to regulation of social behavior
    • Lapouge K, Schubert M, Allain FH, Haas D: Gac/Rsm signal transduction pathway of γ-proteobacteria: from RNA recognition to regulation of social behavior. Mol. Microbiol. 67, 241-253 (2008).
    • (2008) Mol. Microbiol , vol.67 , pp. 241-253
    • Lapouge, K.1    Schubert, M.2    Allain, F.H.3    Haas, D.4
  • 68
    • 38849168148 scopus 로고    scopus 로고
    • The post-transcriptional regulator CsrA plays a central role in the adaptation of bacterial pathogens to different stages of infection in animal hosts
    • Lucchetti-Miganeh C, Burrowes E, Baysse C, Ermel G: The post-transcriptional regulator CsrA plays a central role in the adaptation of bacterial pathogens to different stages of infection in animal hosts. Microbiology 154, 16-29 (2008).
    • (2008) Microbiology , vol.154 , pp. 16-29
    • Lucchetti-Miganeh, C.1    Burrowes, E.2    Baysse, C.3    Ermel, G.4
  • 69
    • 34247169597 scopus 로고    scopus 로고
    • CsrB sRNA family: Sequestration of RNA-binding regulatory proteins
    • Babitzke P, Romeo T: CsrB sRNA family: sequestration of RNA-binding regulatory proteins. Curr. Opin Microbiol. 10, 156-163 (2007).
    • (2007) Curr. Opin Microbiol , vol.10 , pp. 156-163
    • Babitzke, P.1    Romeo, T.2
  • 70
    • 20344405462 scopus 로고    scopus 로고
    • CsrA post-transcriptionally represses pgaABCD, responsible for synthesis of a biofilm potysaccharide adhesin of Escherichia coli
    • Wang X, Dubey AK, Suzuki K, Baker CS, Babitzke P, Romeo T: CsrA post-transcriptionally represses pgaABCD, responsible for synthesis of a biofilm potysaccharide adhesin of Escherichia coli. Mol. Microbiol. 56, 1648-1663 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 1648-1663
    • Wang, X.1    Dubey, A.K.2    Suzuki, K.3    Baker, C.S.4    Babitzke, P.5    Romeo, T.6
  • 71
    • 47049129510 scopus 로고    scopus 로고
    • Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1,6-N-acetyl-D-glucosamine
    • Itoh Y, Rice JD, Goller C et al.: Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1,6-N-acetyl-D-glucosamine. J. Bacteriol. 190, 3670-3680 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 3670-3680
    • Itoh, Y.1    Rice, J.D.2    Goller, C.3
  • 72
    • 0035048862 scopus 로고    scopus 로고
    • Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli
    • Wei BL, Brun-Zinkernagel AM, Simecka JW, Pruss BM, Babitzke P, Romeo T: Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli. Mol. Microbiol. 40, 245-256 (2001).
    • (2001) Mol. Microbiol , vol.40 , pp. 245-256
    • Wei, B.L.1    Brun-Zinkernagel, A.M.2    Simecka, J.W.3    Pruss, B.M.4    Babitzke, P.5    Romeo, T.6
  • 73
    • 0037309144 scopus 로고    scopus 로고
    • The Escherichia coli BarA - UvrY two-component system is needed for efficient switching between glycolytic and gluconeogenic carbon sources
    • Pernestig AK, Georgellis D, Romeo T et al.: The Escherichia coli BarA - UvrY two-component system is needed for efficient switching between glycolytic and gluconeogenic carbon sources. J. Bacteriol. 185, 843-853 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 843-853
    • Pernestig, A.K.1    Georgellis, D.2    Romeo, T.3
  • 74
    • 33751563309 scopus 로고    scopus 로고
    • pH-dependent activation of the BarA-UvrY two-component system in Escherichia coli
    • Mondragon V, Franco B, Jonas K et al.: pH-dependent activation of the BarA-UvrY two-component system in Escherichia coli. J. Bacteriol. 188, 8303-8306 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 8303-8306
    • Mondragon, V.1    Franco, B.2    Jonas, K.3
  • 75
    • 21144439731 scopus 로고    scopus 로고
    • Characterization of the rdar morphotype, a multicellular behavior in Enterobacteriaceae
    • Romling U: Characterization of the rdar morphotype, a multicellular behavior in Enterobacteriaceae. Cell. Mol. Life Sci. 62, 1234-1246 (2005).
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 1234-1246
    • Romling, U.1
  • 76
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig A, Abel S, Folcher M et al.: Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev. 23, 93-104 (2009).
    • (2009) Genes Dev , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3
  • 77
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E
    • Suzuki K, Babitzke P, Kushner SR, Romeo T: Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E. Genes Dev. 20, 2605-2617 (2006).
    • (2006) Genes Dev , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 78
    • 35648979519 scopus 로고    scopus 로고
    • Virulence and prodigiosin antibiotic biosynthesis in Serratia are regulated pleiotropically by the GGDEF/EAL domain protein, PigX
    • Fineran PC, Williamson NR, Lilley KS, Salmond GP: Virulence and prodigiosin antibiotic biosynthesis in Serratia are regulated pleiotropically by the GGDEF/EAL domain protein, PigX. J. Bacteriol. 189, 7653-7662 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 7653-7662
    • Fineran, P.C.1    Williamson, N.R.2    Lilley, K.S.3    Salmond, G.P.4
  • 79
    • 55549090691 scopus 로고    scopus 로고
    • Identification and characterization of cyclic diguanylate signaling systems controlling rugosity in Vibrio cholerae
    • Beyhan S, Odell LS, Yildiz FH: Identification and characterization of cyclic diguanylate signaling systems controlling rugosity in Vibrio cholerae. J. Bacteriol. 190, 7392-7405 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 7392-7405
    • Beyhan, S.1    Odell, L.S.2    Yildiz, F.H.3
  • 80
    • 34249079154 scopus 로고    scopus 로고
    • Network motifs: Theory and experimental approaches
    • Alon U: Network motifs: theory and experimental approaches. Nat. Rev. Genet. 8, 450-461 (2007).
    • (2007) Nat. Rev. Genet , vol.8 , pp. 450-461
    • Alon, U.1
  • 81
    • 57649220029 scopus 로고    scopus 로고
    • Control of RpoS in global gene expression of Escherichia coli in minimal media
    • Dong T, Schellhorn HE: Control of RpoS in global gene expression of Escherichia coli in minimal media. Mol. Genet. Genomics 281, 19-33 (2009).
    • (2009) Mol. Genet. Genomics , vol.281 , pp. 19-33
    • Dong, T.1    Schellhorn, H.E.2
  • 82
    • 0028176450 scopus 로고
    • The cellular concentration of the σS subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability
    • Lange R, R Hengge-Aronis: The cellular concentration of the σS subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability. Genes Dev. 8, 1600-1612 (1994).
    • (1994) Genes Dev , vol.8 , pp. 1600-1612
    • Lange, R.1    Hengge-Aronis, R.2
  • 83
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operan
    • Soutourina O, Kolb A, Krin E et al.: Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operan. J. Bacteriol. 181, 7500-7508 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 7500-7508
    • Soutourina, O.1    Kolb, A.2    Krin, E.3
  • 84
    • 41649102927 scopus 로고    scopus 로고
    • Control of cell fate by the formation of an architecturally complex bacterial community
    • Vlamakis H, Aguilar C, Losick R, Kolter R: Control of cell fate by the formation of an architecturally complex bacterial community. Genes Dev. 22, 945-953 (2008).
    • (2008) Genes Dev , vol.22 , pp. 945-953
    • Vlamakis, H.1    Aguilar, C.2    Losick, R.3    Kolter, R.4
  • 85
    • 33744729365 scopus 로고    scopus 로고
    • A complex transcription network controls the early stages of biofilm development by Escherichia coli
    • Pruss BM, Besemann C, Denton A, Wolfe AJ: A complex transcription network controls the early stages of biofilm development by Escherichia coli. J. Bacteriol. 188, 3731-3739 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 3731-3739
    • Pruss, B.M.1    Besemann, C.2    Denton, A.3    Wolfe, A.J.4
  • 86
    • 0036400593 scopus 로고    scopus 로고
    • Histidine protein kinases: Key signal transducers outside the animal kingdom
    • 310, REVIEWS3013
    • Wolanin PM, Thomason PA, Stock JB: Histidine protein kinases: key signal transducers outside the animal kingdom. Genome Biol. 3(10), REVIEWS3013 (2002).
    • (2002) Genome Biol
    • Wolanin, P.M.1    Thomason, P.A.2    Stock, J.B.3
  • 87
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch JA: Two-component and phosphorelay signal transduction. Curr. Opin Microbiol. 3, 165-170 (2000).
    • (2000) Curr. Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 88
    • 0028844985 scopus 로고
    • Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus
    • Hecht GB, Newton A: Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. J. Bacteriol. 177, 6223-6229 (1995).
    • (1995) J. Bacteriol , vol.177 , pp. 6223-6229
    • Hecht, G.B.1    Newton, A.2
  • 89
    • 0029120523 scopus 로고
    • An essential single domain response regulator required for normal cell division and differentiation in Caulobacter crescentus
    • Hecht GB, Lane T, Ohta N, Sommer JM, Newton A: An essential single domain response regulator required for normal cell division and differentiation in Caulobacter crescentus. EMBO J. 14, 3915-3924 (1995).
    • (1995) EMBO J , vol.14 , pp. 3915-3924
    • Hecht, G.B.1    Lane, T.2    Ohta, N.3    Sommer, J.M.4    Newton, A.5
  • 90
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
    • Paul R, Abel S, Wassmann P, Beck A, Heerklotz H, Jenal U: Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J. Biol. Chem. 282, 29170-29177 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 91
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • Chan C, Paul R, Samoray D et al.: Structural basis of activity and allosteric control of diguanylate cyclase. Proc. Natl Acad. Sci. USA 101, 17084-17089 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17084-17089
    • Chan, C.1    Paul, R.2    Samoray, D.3
  • 92
    • 42949140533 scopus 로고    scopus 로고
    • Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate
    • Paul R, Jaeger T, Abel S et al.: Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate. Cell 133, 452-461 (2008).
    • (2008) Cell , vol.133 , pp. 452-461
    • Paul, R.1    Jaeger, T.2    Abel, S.3
  • 93
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge P, Paul R, Goymer P, Rainey P, Jenal U: Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol. Microbiol. 47, 1695-1708 (2003).
    • (2003) Mol. Microbiol , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 94
    • 33745402876 scopus 로고    scopus 로고
    • Adaptive divergence in experimental populations of Pseudomonas flucrescens. II. Role of the GGDEF regulator WspR in evolution and development of the wrinkly spreader phenotype
    • Goymer P, Kahn SG, Malone JG, Gehrig SM, Spiers AJ, Rainey PB: Adaptive divergence in experimental populations of Pseudomonas flucrescens. II. Role of the GGDEF regulator WspR in evolution and development of the wrinkly spreader phenotype. Genetics 173, 515-526 (2006).
    • (2006) Genetics , vol.173 , pp. 515-526
    • Goymer, P.1    Kahn, S.G.2    Malone, J.G.3    Gehrig, S.M.4    Spiers, A.J.5    Rainey, P.B.6
  • 95
    • 26444582915 scopus 로고    scopus 로고
    • A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels
    • Hickman JW, Tifrea DF, Hatwood CS: A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc. Natl Acad. Sci. USA 102, 14422-14427 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 14422-14427
    • Hickman, J.W.1    Tifrea, D.F.2    Hatwood, C.S.3
  • 96
    • 0036889484 scopus 로고    scopus 로고
    • Autolysis and autoaggregation in Pseudomonas aeruginosa colony morphology mutants
    • D'Argenio DA, Calfee MW, Rainey PB, Pesci EC: Autolysis and autoaggregation in Pseudomonas aeruginosa colony morphology mutants. J. Bacteriol. 184, 6481-6489 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 6481-6489
    • D'Argenio, D.A.1    Calfee, M.W.2    Rainey, P.B.3    Pesci, E.C.4
  • 97
    • 36549080792 scopus 로고    scopus 로고
    • Subcellular location characteristics of the Pseudomonas aeruginosa GGDEF protein, WspR, indicate that it produces cyclic-di-GMP in response to growth on surfaces
    • Guvener ZT, Harwood CS: Subcellular location characteristics of the Pseudomonas aeruginosa GGDEF protein, WspR, indicate that it produces cyclic-di-GMP in response to growth on surfaces. Mol. Microbiol. 66, 1459-1473 (2007).
    • (2007) Mol. Microbiol , vol.66 , pp. 1459-1473
    • Guvener, Z.T.1    Harwood, C.S.2
  • 98
    • 48849086360 scopus 로고    scopus 로고
    • Diversification of the function of cell-to-cell signaling in regulation of virulence within plant pathogenic xanthomonads
    • 1, pe23
    • Dow M: Diversification of the function of cell-to-cell signaling in regulation of virulence within plant pathogenic xanthomonads. Sci. Signal 1, pe23 (2008).
    • (2008) Sci. Signal
    • Dow, M.1
  • 99
    • 33846078828 scopus 로고    scopus 로고
    • Cyclic di-GMP signalling in the virulence and environmental adaptation of Xanthomonas campestris
    • Ryan RP, Fouhy Y, Lucey JF et al.: Cyclic di-GMP signalling in the virulence and environmental adaptation of Xanthomonas campestris. Mol. Microbiol. 63, 429-442 (2007).
    • (2007) Mol. Microbiol , vol.63 , pp. 429-442
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3
  • 100
    • 34547178695 scopus 로고    scopus 로고
    • Cell-cell signaling, cyclic di-GMP turnover and regulation of virulence in Xanthomonas campestris
    • Fouhy Y, Lucey JF, Ryan RP, Dow JM: Cell-cell signaling, cyclic di-GMP turnover and regulation of virulence in Xanthomonas campestris. Res. Microbiol. 157, 899-904 (2006).
    • (2006) Res. Microbiol , vol.157 , pp. 899-904
    • Fouhy, Y.1    Lucey, J.F.2    Ryan, R.P.3    Dow, J.M.4
  • 101
    • 40649127724 scopus 로고    scopus 로고
    • A cell-cell signaling sensor is required for virulence and insect transmission of Xylella fastidiosa
    • Chatterjee S, Wistrom C, Lindow SE: A cell-cell signaling sensor is required for virulence and insect transmission of Xylella fastidiosa. Proc. Natl Acad. Sci. USA 105, 2670-2675 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 2670-2675
    • Chatterjee, S.1    Wistrom, C.2    Lindow, S.E.3
  • 102
    • 40849093159 scopus 로고    scopus 로고
    • Virulence of plant pathogenic bacteria attenuated by degradation of fatty acid cell-to-cell signaling factors
    • Newman KL, Chatterjee S, Ho KA, Lindow SE: Virulence of plant pathogenic bacteria attenuated by degradation of fatty acid cell-to-cell signaling factors. Mol. Plant Microbe Interact. 21, 326-334 (2008).
    • (2008) Mol. Plant Microbe Interact , vol.21 , pp. 326-334
    • Newman, K.L.1    Chatterjee, S.2    Ho, K.A.3    Lindow, S.E.4
  • 103
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes
    • Kulasekara HD, Ventre I, Kulasekara BR, Lazdunski A, Filloux A, Lory S: A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol. Microbiol. 55, 368-380 (2005).
    • (2005) Mol. Microbiol , vol.55 , pp. 368-380
    • Kulasekara, H.D.1    Ventre, I.2    Kulasekara, B.R.3    Lazdunski, A.4    Filloux, A.5    Lory, S.6
  • 104
    • 0031944977 scopus 로고    scopus 로고
    • Characterization of the bvgR locus of Bordetella pertussis
    • Merkel TJ, Barros C, Stibitz S: Characterization of the bvgR locus of Bordetella pertussis. J. Bacteriol. 180, 1682-1690 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 1682-1690
    • Merkel, T.J.1    Barros, C.2    Stibitz, S.3
  • 105
    • 0026093011 scopus 로고
    • Cellulose biosynthesis and function in bacteria
    • Ross P, Mayer R, Benziman M: Cellulose biosynthesis and function in bacteria. Microbiol. Rev. 55, 35-58 (1991).
    • (1991) Microbiol. Rev , vol.55 , pp. 35-58
    • Ross, P.1    Mayer, R.2    Benziman, M.3
  • 106
    • 0035957226 scopus 로고    scopus 로고
    • Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor
    • Chang AL, Tuckerman JR, Gonzalez G et al.: Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor. Biochemistry 40, 3420-3426 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3420-3426
    • Chang, A.L.1    Tuckerman, J.R.2    Gonzalez, G.3
  • 107
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon VM, Gonzalez G, Gilles-Gonzalez MA: Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39, 2685-2691 (2000).
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 109
    • 0345097587 scopus 로고    scopus 로고
    • Fim X, a multidomain protein connecting environmental signals to twitching motiliry in Pseudomonas aeruginosa
    • Huang B, Whitchurch CB, Mattick JS: Fim X, a multidomain protein connecting environmental signals to twitching motiliry in Pseudomonas aeruginosa. J. Bacteriol. 185, 7068-7076 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 7068-7076
    • Huang, B.1    Whitchurch, C.B.2    Mattick, J.S.3
  • 110
    • 27144544090 scopus 로고    scopus 로고
    • NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine
    • Karatan E, Duncan TR, Watnick PI: NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine. J. Bacteriol. 187, 7434-7443 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 7434-7443
    • Karatan, E.1    Duncan, T.R.2    Watnick, P.I.3
  • 111
    • 33751378939 scopus 로고    scopus 로고
    • Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri
    • O'Shea TM, Klein AH, Geszvain K, Wolfe AJ, Visick KL: Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri. J. Bacteriol. 188, 8196-8205 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 8196-8205
    • O'Shea, T.M.1    Klein, A.H.2    Geszvain, K.3    Wolfe, A.J.4    Visick, K.L.5
  • 113
    • 33750441136 scopus 로고    scopus 로고
    • Allosteric control of cyclic di-GMP signaling
    • Christen B, Christen M, Paul R et al.: Allosteric control of cyclic di-GMP signaling. J. Biol. Chem. 281, 32015-32024 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 32015-32024
    • Christen, B.1    Christen, M.2    Paul, R.3
  • 114
  • 116
    • 33749180794 scopus 로고    scopus 로고
    • The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri
    • Andrade MO, Alegria MC, Guzzo CR et al.: The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri. Mol. Microbiol. 62, 537-551 (2006).
    • (2006) Mol. Microbiol , vol.62 , pp. 537-551
    • Andrade, M.O.1    Alegria, M.C.2    Guzzo, C.R.3
  • 117
    • 43449104220 scopus 로고    scopus 로고
    • Insights into Yersinia pestis biofilm development: Topology and co-interaction of Hms inner membrane proteins involved in exopolysaccharide production
    • Bobrov AG, Kirillina O, Forman S, Mack D, Perry RD: Insights into Yersinia pestis biofilm development: topology and co-interaction of Hms inner membrane proteins involved in exopolysaccharide production. Environ. Microbiol. 10, 1419-1432 (2008).
    • (2008) Environ. Microbiol , vol.10 , pp. 1419-1432
    • Bobrov, A.G.1    Kirillina, O.2    Forman, S.3    Mack, D.4    Perry, R.D.5
  • 118
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP
    • Tarutina M, Ryjenkov DA, Gomelsky M: An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP. J. Biol. Chem. 281, 34751-34758 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 119
    • 4744337730 scopus 로고    scopus 로고
    • HmsP, a putative phosphodiesterase, and HmsT, a purative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis
    • Kirillina O, Fetherston JD, Bobrov AG, Abney J, Perry RD: HmsP, a putative phosphodiesterase, and HmsT, a purative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis. Mol. Microbiol. 54, 75-88 (2004).
    • (2004) Mol. Microbiol , vol.54 , pp. 75-88
    • Kirillina, O.1    Fetherston, J.D.2    Bobrov, A.G.3    Abney, J.4    Perry, R.D.5
  • 120
    • 10744225048 scopus 로고    scopus 로고
    • The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries two pathogenicity islands harboring plant and animal virulence genes
    • He J, Baldini RL, Deziel E et al.: The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries two pathogenicity islands harboring plant and animal virulence genes. Proc. Natl Acad. Sci. USA 101, 2530-2535 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2530-2535
    • He, J.1    Baldini, R.L.2    Deziel, E.3
  • 121
    • 33846616323 scopus 로고    scopus 로고
    • Smooth to rugose phase variation in Vibrio cholerae can be mediated by a single nucleotide change that targets c-di-GMP signalling pathway
    • Beyhan S, Yildiz FH: Smooth to rugose phase variation in Vibrio cholerae can be mediated by a single nucleotide change that targets c-di-GMP signalling pathway. Mol. Microbiol. 63, 995-1007 (2007).
    • (2007) Mol. Microbiol , vol.63 , pp. 995-1007
    • Beyhan, S.1    Yildiz, F.H.2
  • 122
    • 25144497412 scopus 로고    scopus 로고
    • Phenotypic convergence mediated by GGDEF-domain-containing proteins
    • Simm R, Fetherston JD, Kader A, Romling U, Perry RD: Phenotypic convergence mediated by GGDEF-domain-containing proteins. J. Bacteriol. 187, 6816-6823 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 6816-6823
    • Simm, R.1    Fetherston, J.D.2    Kader, A.3    Romling, U.4    Perry, R.D.5
  • 123
    • 47749152941 scopus 로고    scopus 로고
    • Riboswitches in eubacteria sense the second messenger cyclic di-GMP
    • Sudarsan N, Lee ER, Weinberg Z et al.: Riboswitches in eubacteria sense the second messenger cyclic di-GMP. Science 321, 411-413 (2008).
    • (2008) Science , vol.321 , pp. 411-413
    • Sudarsan, N.1    Lee, E.R.2    Weinberg, Z.3
  • 124
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam D, Galperin MY: PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22, 3-6 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 126
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman JW, Harwood CS: Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol. Microbiol. 69, 376-389 (2008).
    • (2008) Mol. Microbiol , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 127
    • 37149042731 scopus 로고    scopus 로고
    • The structural basis of cyclic diguanylate signal transduction by PilZ domains
    • Benach J, Swaminathan SS, Tamayo R et al.: The structural basis of cyclic diguanylate signal transduction by PilZ domains. EMBO J. 26, 5153-5166 (2007).
    • (2007) EMBO J , vol.26 , pp. 5153-5166
    • Benach, J.1    Swaminathan, S.S.2    Tamayo, R.3
  • 128
    • 55949131187 scopus 로고    scopus 로고
    • Design and synthesis of bis-carbamate analogs of cyclic bis-(3′-5′)-diguanylic acid (c-di-GMP) and the acyclic dimer pGpG
    • Kline T, Jackson SR, Deng W, Verlinde CL, Miller SI: Design and synthesis of bis-carbamate analogs of cyclic bis-(3′-5′)-diguanylic acid (c-di-GMP) and the acyclic dimer pGpG. Nucleosides Nucleotides Nucleic Acids 27, 1282-1300 (2008).
    • (2008) Nucleosides Nucleotides Nucleic Acids , vol.27 , pp. 1282-1300
    • Kline, T.1    Jackson, S.R.2    Deng, W.3    Verlinde, C.L.4    Miller, S.I.5
  • 129
    • 0036723748 scopus 로고    scopus 로고
    • Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli
    • Suzuki K, Wang X, Weilbacher T et al.: Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli. J. Bacteriol. 184, 5130-5140 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 5130-5140
    • Suzuki, K.1    Wang, X.2    Weilbacher, T.3


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