메뉴 건너뛰기




Volumn 291, Issue 24, 2016, Pages 12547-12555

Biofilms and Cyclic di-GMP (c-di-GMP) signaling: Lessons from Pseudomonas aeruginosa and other bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOCHEMISTRY; BIOFILMS; COMPLEX NETWORKS; MOLECULAR BIOLOGY;

EID: 84974577707     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R115.711507     Document Type: Short Survey
Times cited : (441)

References (100)
  • 2
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: From the natural environment to infectious diseases
    • Hall-Stoodley, L., Costerton, J. W., and Stoodley, P. (2004) Bacterial biofilms: from the natural environment to infectious diseases. Nat. Rev. Microbiol. 2, 95-108
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 3
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: The first 25 years of a universal bacterial second messenger
    • Römling, U., Galperin, M. Y., and Gomelsky, M. (2013) Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol. Mol. Biol. Rev. 77, 1-52
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 1-52
    • Römling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 4
    • 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., and Römling, U. (2004) GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol. 53, 1123-1134
    • (2004) Mol. Microbiol. , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Römling, U.5
  • 5
    • 84930978770 scopus 로고    scopus 로고
    • Diguanylate cyclase NicD-based signalling mechanism of nutrient-induced dispersion by Pseudomonas aeruginosa
    • Basu Roy, A., and Sauer, K. (2014) Diguanylate cyclase NicD-based signalling mechanism of nutrient-induced dispersion by Pseudomonas aeruginosa. Mol. Microbiol. 94, 771-793
    • (2014) Mol. Microbiol. , vol.94 , pp. 771-793
    • Basu Roy, A.1    Sauer, K.2
  • 6
    • 0036157549 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm
    • Sauer, K., Camper, A. K., Ehrlich, G. D., Costerton, J. W., and Davies, D. G. (2002) Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm. J. Bacteriol. 184, 1140-1154
    • (2002) J. Bacteriol. , vol.184 , pp. 1140-1154
    • Sauer, K.1    Camper, A.K.2    Ehrlich, G.D.3    Costerton, J.W.4    Davies, D.G.5
  • 8
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge, R. (2009) Principles of c-di-GMP signalling in bacteria. Nat. Rev. Microbiol. 7, 263-273
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 263-273
    • Hengge, R.1
  • 9
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov, D. A., Tarutina, M., Moskvin, O. V., and Gomelsky, M. (2005) Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187, 1792-1798
    • (2005) J. Bacteriol. , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 10
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt, A. J., Ryjenkov, D. A., and Gomelsky, M. (2005) The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187, 4774-4781
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 11
    • 84953924413 scopus 로고    scopus 로고
    • Diversity of c-di-GMP-binding proteins and mechanisms
    • Chou, S. H., and Galperin, M. Y. (2016) Diversity of c-di-GMP-binding proteins and mechanisms. J. Bacteriol. 198, 32-46
    • (2016) J. Bacteriol. , vol.198 , pp. 32-46
    • Chou, S.H.1    Galperin, M.Y.2
  • 12
    • 77949911836 scopus 로고    scopus 로고
    • Diversity of structure and function of response regulator output domains
    • Galperin, M. Y. (2010) Diversity of structure and function of response regulator output domains. Curr. Opin. Microbiol. 13, 150-159
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 150-159
    • Galperin, M.Y.1
  • 13
    • 84940836760 scopus 로고    scopus 로고
    • A Pterin-dependent signaling pathway regulates a dual-function diguanylate cyclase-phosphodiesterase controlling surface attachment in Agrobacterium tumefaciens
    • Feirer, N., Xu, J., Allen, K. D., Koestler, B. J., Bruger, E. L., Waters, C. M., White, R. H., and Fuqua, C. (2015) A Pterin-dependent signaling pathway regulates a dual-function diguanylate cyclase-phosphodiesterase controlling surface attachment in Agrobacterium tumefaciens. MBio 6, e00156
    • (2015) MBio , vol.6
    • Feirer, N.1    Xu, J.2    Allen, K.D.3    Koestler, B.J.4    Bruger, E.L.5    Waters, C.M.6    White, R.H.7    Fuqua, C.8
  • 14
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turn-over of the second messenger c-di-GMP
    • Tarutina, M., Ryjenkov, D. A., and Gomelsky, M. (2006) An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turn-over of the second messenger c-di-GMP. J. Biol. Chem. 281, 34751-34758
    • (2006) J. Biol. Chem. , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 15
    • 0036837981 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus scrABC, a novel operon affecting swarming and capsular polysaccharide regulation
    • Boles, B. R., and McCarter, L. L. (2002) Vibrio parahaemolyticus scrABC, a novel operon affecting swarming and capsular polysaccharide regulation. J. Bacteriol. 184, 5946-5954
    • (2002) J. Bacteriol. , vol.184 , pp. 5946-5954
    • Boles, B.R.1    McCarter, L.L.2
  • 16
    • 59949088230 scopus 로고    scopus 로고
    • MucR, a novel membrane-associated regulator of alginate biosynthesis in Pseudomonas aeruginosa
    • Hay, I. D., Remminghorst, U., and Rehm, B. H. (2009) MucR, a novel membrane-associated regulator of alginate biosynthesis in Pseudomonas aeruginosa. Appl. Environ. Microbiol. 75, 1110-1120
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1110-1120
    • Hay, I.D.1    Remminghorst, U.2    Rehm, B.H.3
  • 17
    • 78049426911 scopus 로고    scopus 로고
    • Comparative genomics of cyclic-di-GMP signalling in bacteria: Post-translational regulation and catalytic activity
    • Seshasayee, A. S., Fraser, G. M., and Luscombe, N. M. (2010) Comparative genomics of cyclic-di-GMP signalling in bacteria: post-translational regulation and catalytic activity. Nucleic Acids Res. 38, 5970-5981
    • (2010) Nucleic Acids Res , vol.38 , pp. 5970-5981
    • Seshasayee, A.S.1    Fraser, G.M.2    Luscombe, N.M.3
  • 18
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: Bacterial IQ, extroverts and introverts
    • Galperin, M. Y. (2005) A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts. BMC Microbiol. 5, 35
    • (2005) BMC Microbiol , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 19
    • 84866351420 scopus 로고    scopus 로고
    • Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling
    • Chen, M. W., Kotaka, M., Vonrhein, C., Bricogne, G., Rao, F., Chuah, M. L., Svergun, D., Schneider, G., Liang, Z. X., and Lescar, J. (2012) Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling. J. Bacteriol. 194, 4837-4846
    • (2012) J. Bacteriol. , vol.194 , pp. 4837-4846
    • Chen, M.W.1    Kotaka, M.2    Vonrhein, C.3    Bricogne, G.4    Rao, F.5    Chuah, M.L.6    Svergun, D.7    Schneider, G.8    Liang, Z.X.9    Lescar, J.10
  • 20
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul, R., Weiser, S., Amiot, N. C., Chan, C., Schirmer, T., Giese, B., and Jenal, U. (2004) Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 18, 715-727
    • (2004) Genes Dev , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 21
    • 26444582915 scopus 로고    scopus 로고
    • A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels
    • Hickman, J. W., Tifrea, D. F., and Harwood, C. S. (2005) A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc. Natl. Acad. Sci. U.S.A. 102, 14422-14427
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 14422-14427
    • Hickman, J.W.1    Tifrea, D.F.2    Harwood, C.S.3
  • 22
    • 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
    • Güvener, Z. T., and Harwood, C. S. (2007) 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) Mol. Microbiol. , vol.66 , pp. 1459-1473
    • Güvener, Z.T.1    Harwood, C.S.2
  • 23
    • 84879571298 scopus 로고    scopus 로고
    • Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity
    • Huangyutitham, V., Güvener, Z. T., and Harwood, C. S. (2013) Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity. MBio 4, e00242-00213
    • (2013) MBio , vol.4 , pp. e00242-e100213
    • Huangyutitham, V.1    Güvener, Z.T.2    Harwood, C.S.3
  • 25
    • 79952201735 scopus 로고    scopus 로고
    • Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation
    • De, N., Navarro, M. V., Wang, Q., Krasteva, P. V., and Sondermann, H. (2010) Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation. Methods Enzymol. 471, 161-184
    • (2010) Methods Enzymol , vol.471 , pp. 161-184
    • De, N.1    Navarro, M.V.2    Wang, Q.3    Krasteva, P.V.4    Sondermann, H.5
  • 26
    • 34247202706 scopus 로고    scopus 로고
    • The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain
    • Malone, J. G., Williams, R., Christen, M., Jenal, U., Spiers, A. J., and Rainey, P. B. (2007) The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain. Microbiology 153, 980-994
    • (2007) Microbiology , vol.153 , pp. 980-994
    • Malone, J.G.1    Williams, R.2    Christen, M.3    Jenal, U.4    Spiers, A.J.5    Rainey, P.B.6
  • 28
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes
    • Kulasekara, H. D., Ventre, I., Kulasekara, B. R., Lazdunski, A., Filloux, A., and Lory, S. (2005) A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol. Microbiol. 55, 368-380
    • (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
  • 29
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: A study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao, F., Yang, Y., Qi, Y., and Liang, Z. X. (2008) Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J. Bacteriol. 190, 3622-3631
    • (2008) J. Bacteriol. , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.X.4
  • 31
    • 84884194723 scopus 로고    scopus 로고
    • C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: Analysis of the reaction mechanism and novel roles for pGpG
    • Stelitano, V., Giardina, G., Paiardini, A., Castiglione, N., Cutruzzolà, F., and Rinaldo, S. (2013) C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG. PLoS ONE 8, e74920
    • (2013) PLoS ONE , vol.8
    • Stelitano, V.1    Giardina, G.2    Paiardini, A.3    Castiglione, N.4    Cutruzzolà, F.5    Rinaldo, S.6
  • 33
    • 84930786571 scopus 로고    scopus 로고
    • Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site
    • Rinaldo, S., Paiardini, A., Stelitano, V., Brunotti, P., Cervoni, L., Fernicola, S., Protano, C., Vitali, M., Cutruzzolà, F., and Giardina, G. (2015) Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site. J. Bacteriol. 197, 1525-1535
    • (2015) J. Bacteriol. , vol.197 , pp. 1525-1535
    • Rinaldo, S.1    Paiardini, A.2    Stelitano, V.3    Brunotti, P.4    Cervoni, L.5    Fernicola, S.6    Protano, C.7    Vitali, M.8    Cutruzzolà, F.9    Giardina, G.10
  • 34
    • 84941254999 scopus 로고    scopus 로고
    • Oligoribonuclease is the primary degradative enzyme for pGpG in Pseudomonas aeruginosa that is required for cyclic-di-GMP turnover
    • Orr, M. W., Donaldson, G. P., Severin, G. B., Wang, J., Sintim, H. O., Waters, C. M., and Lee, V. T. (2015) Oligoribonuclease is the primary degradative enzyme for pGpG in Pseudomonas aeruginosa that is required for cyclic-di-GMP turnover. Proc. Natl. Acad. Sci. U.S.A. 112, E5048-5057
    • (2015) Proc. Natl. Acad. Sci. U.S.A , vol.112 , pp. E5048-E5057
    • Orr, M.W.1    Donaldson, G.P.2    Severin, G.B.3    Wang, J.4    Sintim, H.O.5    Waters, C.M.6    Lee, V.T.7
  • 36
    • 79960891629 scopus 로고    scopus 로고
    • Modulation of Pseudomonas aeruginosa surface-associated group behaviors by individual amino acids through c-di-GMP signaling
    • Bernier, S. P., Ha, D. G., Khan, W., Merritt, J. H., and O'Toole, G. A. (2011) Modulation of Pseudomonas aeruginosa surface-associated group behaviors by individual amino acids through c-di-GMP signaling. Res. Microbiol. 162, 680-688
    • (2011) Res. Microbiol. , vol.162 , pp. 680-688
    • Bernier, S.P.1    Ha, D.G.2    Khan, W.3    Merritt, J.H.4    O'Toole, G.A.5
  • 37
    • 79952168685 scopus 로고    scopus 로고
    • Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases
    • Merritt, J. H., Ha, D. G., Cowles, K. N., Lu, W., Morales, D. K., Rabinowitz, J., Gitai, Z., and O'Toole, G. A. (2010) Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases. MBio 1, e00183-10
    • (2010) MBio , vol.1 , pp. e00183-e00210
    • Merritt, J.H.1    Ha, D.G.2    Cowles, K.N.3    Lu, W.4    Morales, D.K.5    Rabinowitz, J.6    Gitai, Z.7    O'Toole, G.A.8
  • 38
    • 71249115222 scopus 로고    scopus 로고
    • SiaA and SiaD are essential for inducing autoaggregation as a specific response to detergent stress in Pseudomonas aeruginosa
    • Klebensberger, J., Birkenmaier, A., Geffers, R., Kjelleberg, S., and Philipp, B. (2009) SiaA and SiaD are essential for inducing autoaggregation as a specific response to detergent stress in Pseudomonas aeruginosa. Environ. Microbiol. 11, 3073-3086
    • (2009) Environ. Microbiol. , vol.11 , pp. 3073-3086
    • Klebensberger, J.1    Birkenmaier, A.2    Geffers, R.3    Kjelleberg, S.4    Philipp, B.5
  • 40
    • 84903896321 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa diguanylate cyclase GcbA, a homolog of P. Fluorescens GcbA, promotes initial attachment to surfaces, but not biofilm formation, via regulation of motility
    • Petrova, O. E., Cherny, K. E., and Sauer, K. (2014) The Pseudomonas aeruginosa diguanylate cyclase GcbA, a homolog of P. fluorescens GcbA, promotes initial attachment to surfaces, but not biofilm formation, via regulation of motility. J. Bacteriol. 196, 2827-2841
    • (2014) J. Bacteriol. , vol.196 , pp. 2827-2841
    • Petrova, O.E.1    Cherny, K.E.2    Sauer, K.3
  • 41
    • 84864003643 scopus 로고    scopus 로고
    • The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion
    • Roy, A. B., Petrova, O. E., and Sauer, K. (2012) The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion. J. Bacteriol. 194, 2904-2915
    • (2012) J. Bacteriol. , vol.194 , pp. 2904-2915
    • Roy, A.B.1    Petrova, O.E.2    Sauer, K.3
  • 42
    • 78650396058 scopus 로고    scopus 로고
    • Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-Di-GMP phosphodiesterase with a putative hypoxia-sensing domain
    • An, S., Wu, J., and Zhang, L. H. (2010) Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-Di-GMP phosphodiesterase with a putative hypoxia-sensing domain. Appl. Environ. Microbiol. 76, 8160-8173
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 8160-8173
    • An, S.1    Wu, J.2    Zhang, L.H.3
  • 43
    • 84881001909 scopus 로고    scopus 로고
    • NO-induced biofilm dispersion in Pseudomonas aeruginosa is mediated by an MHYT domain-coupled phosphodiesterase
    • Li, Y., Heine, S., Entian, M., Sauer, K., and Frankenberg-Dinkel, N. (2013) NO-induced biofilm dispersion in Pseudomonas aeruginosa is mediated by an MHYT domain-coupled phosphodiesterase. J. Bacteriol. 195, 3531-3542
    • (2013) J. Bacteriol. , vol.195 , pp. 3531-3542
    • Li, Y.1    Heine, S.2    Entian, M.3    Sauer, K.4    Frankenberg-Dinkel, N.5
  • 44
    • 67650863623 scopus 로고    scopus 로고
    • Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885)
    • Ueda, A., and Wood, T. K. (2009) Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885). PLoS Pathog. 5, e1000483
    • (2009) PLoS Pathog , vol.5
    • Ueda, A.1    Wood, T.K.2
  • 45
    • 79959813634 scopus 로고    scopus 로고
    • Key two-component regulatory systems that control biofilm formation in Pseudomonas aeruginosa
    • Mikkelsen, H., Sivaneson, M., and Filloux, A. (2011) Key two-component regulatory systems that control biofilm formation in Pseudomonas aeruginosa. Environ. Microbiol. 13, 1666-1681
    • (2011) Environ. Microbiol. , vol.13 , pp. 1666-1681
    • Mikkelsen, H.1    Sivaneson, M.2    Filloux, A.3
  • 46
    • 84910011732 scopus 로고    scopus 로고
    • The diguanylate cyclase SadC is a central player in Gac/Rsm-mediated biofilm formation in Pseudomonas aeruginosa
    • Moscoso, J. A., Jaeger, T., Valentini, M., Hui, K., Jenal, U., and Filloux, A. (2014) The diguanylate cyclase SadC is a central player in Gac/Rsm-mediated biofilm formation in Pseudomonas aeruginosa. J. Bacteriol. 196, 4081-4088
    • (2014) J. Bacteriol. , vol.196 , pp. 4081-4088
    • Moscoso, J.A.1    Jaeger, T.2    Valentini, M.3    Hui, K.4    Jenal, U.5    Filloux, A.6
  • 47
    • 84886045100 scopus 로고    scopus 로고
    • Antimicrobial tolerance of Pseudomonas aeruginosa biofilms is activated during an early developmental stage and requires the two-component hybrid SagS
    • Gupta, K., Marques, C. N., Petrova, O. E., and Sauer, K. (2013) Antimicrobial tolerance of Pseudomonas aeruginosa biofilms is activated during an early developmental stage and requires the two-component hybrid SagS. J. Bacteriol. 195, 4975-4987
    • (2013) J. Bacteriol. , vol.195 , pp. 4975-4987
    • Gupta, K.1    Marques, C.N.2    Petrova, O.E.3    Sauer, K.4
  • 48
    • 84899642382 scopus 로고    scopus 로고
    • Elevated levels of the second messenger c-di-GMP contribute to antimicrobial resistance of Pseudomonas aeruginosa
    • Gupta, K., Liao, J., Petrova, O. E., Cherny, K. E., and Sauer, K. (2014) Elevated levels of the second messenger c-di-GMP contribute to antimicrobial resistance of Pseudomonas aeruginosa. Mol. Microbiol. 92, 488-506
    • (2014) Mol. Microbiol. , vol.92 , pp. 488-506
    • Gupta, K.1    Liao, J.2    Petrova, O.E.3    Cherny, K.E.4    Sauer, K.5
  • 49
    • 85028139131 scopus 로고    scopus 로고
    • Convergent evolution and adaptation of Pseudomonas aeruginosa within patients with cystic fibrosis
    • Marvig, R. L., Sommer, L. M., Molin, S., and Johansen, H. K. (2015) Convergent evolution and adaptation of Pseudomonas aeruginosa within patients with cystic fibrosis. Nat. Genet. 47, 57-64
    • (2015) Nat. Genet. , vol.47 , pp. 57-64
    • Marvig, R.L.1    Sommer, L.M.2    Molin, S.3    Johansen, H.K.4
  • 52
    • 84947926795 scopus 로고    scopus 로고
    • Structural insights into YfiR sequestering by YfiB in Pseudomonas aeruginosa PAO1
    • Li, S., Li, T., Xu, Y., Zhang, Q., Zhang, W., Che, S., Liu, R., Wang, Y., and Bartlam, M. (2015) Structural insights into YfiR sequestering by YfiB in Pseudomonas aeruginosa PAO1. Sci. Rep. 5, 16915
    • (2015) Sci. Rep. , vol.5
    • Li, S.1    Li, T.2    Xu, Y.3    Zhang, Q.4    Zhang, W.5    Che, S.6    Liu, R.7    Wang, Y.8    Bartlam, M.9
  • 53
    • 84864052471 scopus 로고    scopus 로고
    • The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways
    • Malone, J. G., Jaeger, T., Manfredi, P., Dötsch, A., Blanka, A., Bos, R., Cornelis, G. R., Häussler, S., and Jenal, U. (2012) The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways. PLoS Pathog. 8, e1002760
    • (2012) PLoS Pathog , vol.8
    • Malone, J.G.1    Jaeger, T.2    Manfredi, P.3    Dötsch, A.4    Blanka, A.5    Bos, R.6    Cornelis, G.R.7    Häussler, S.8    Jenal, U.9
  • 55
    • 0037129218 scopus 로고    scopus 로고
    • Pseudomonas biofilm formation and antibiotic resistance are linked to phenotypic variation
    • Drenkard, E., and Ausubel, F. M. (2002) Pseudomonas biofilm formation and antibiotic resistance are linked to phenotypic variation. Nature 416, 740-743
    • (2002) Nature , vol.416 , pp. 740-743
    • Drenkard, E.1    Ausubel, F.M.2
  • 56
    • 78649407798 scopus 로고    scopus 로고
    • Cyclic-di-GMP reaches out into the bacterial RNA world
    • Hengge, R. (2010) Cyclic-di-GMP reaches out into the bacterial RNA world. Sci. Signal. 3, pe44
    • (2010) Sci. Signal , vol.3 , pp. e44
    • Hengge, R.1
  • 57
    • 34548303826 scopus 로고    scopus 로고
    • A cyclic-di-GMP receptor required for bacterial exopolysaccharide production
    • Lee, V. T., Matewish, J. M., Kessler, J. L., Hyodo, M., Hayakawa, Y., and Lory, S. (2007) A cyclic-di-GMP receptor required for bacterial exopolysaccharide production. Mol. Microbiol. 65, 1474-1484
    • (2007) Mol. Microbiol. , vol.65 , pp. 1474-1484
    • Lee, V.T.1    Matewish, J.M.2    Kessler, J.L.3    Hyodo, M.4    Hayakawa, Y.5    Lory, S.6
  • 58
    • 84865741837 scopus 로고    scopus 로고
    • Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1
    • Li, Z., Chen, J. H., Hao, Y., and Nair, S. K. (2012) Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 287, 30191-30204
    • (2012) J. Biol. Chem. , vol.287 , pp. 30191-30204
    • Li, Z.1    Chen, J.H.2    Hao, Y.3    Nair, S.K.4
  • 59
    • 84863611012 scopus 로고    scopus 로고
    • Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa
    • Whitney, J. C., Colvin, K. M., Marmont, L. S., Robinson, H., Parsek, M. R., and Howell, P. L. (2012) Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa. J. Biol. Chem. 287, 23582-23593
    • (2012) J. Biol. Chem. , vol.287 , pp. 23582-23593
    • Whitney, J.C.1    Colvin, K.M.2    Marmont, L.S.3    Robinson, H.4    Parsek, M.R.5    Howell, P.L.6
  • 60
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam, D., and Galperin, M. Y. (2006) PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22, 3-6
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 61
    • 34547682212 scopus 로고    scopus 로고
    • The second messenger bis-(3′-5′)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa
    • Merighi, M., Lee, V. T., Hyodo, M., Hayakawa, Y., and Lory, S. (2007) The second messenger bis-(3′-5′)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa. Mol. Microbiol. 65, 876-895
    • (2007) Mol. Microbiol. , vol.65 , pp. 876-895
    • Merighi, M.1    Lee, V.T.2    Hyodo, M.3    Hayakawa, Y.4    Lory, S.5
  • 62
    • 48449097813 scopus 로고    scopus 로고
    • Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization
    • Oglesby, L. L., Jain, S., and Ohman, D. E. (2008) Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization. Microbiology 154, 1605-1615
    • (2008) Microbiology , vol.154 , pp. 1605-1615
    • Oglesby, L.L.1    Jain, S.2    Ohman, D.E.3
  • 63
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman, J. W., and Harwood, C. S. (2008) Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol. Microbiol. 69, 376-389
    • (2008) Mol. Microbiol. , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 64
    • 84887482378 scopus 로고    scopus 로고
    • Cyclic diguanosine monophosphate represses bacterial flagella synthesis by interacting with the Walker A motif of the enhancer-binding protein FleQ
    • Baraquet, C., and Harwood, C. S. (2013) Cyclic diguanosine monophosphate represses bacterial flagella synthesis by interacting with the Walker A motif of the enhancer-binding protein FleQ. Proc. Natl. Acad. Sci. U.S.A. 110, 18478-18483
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 18478-18483
    • Baraquet, C.1    Harwood, C.S.2
  • 65
    • 84952872839 scopus 로고    scopus 로고
    • The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator
    • Su, T., Liu, S., Wang, K., Chi, K., Zhu, D., Wei, T., Huang, Y., Guo, L., Hu, W., Xu, S., Lin, Z., and Gu, L. (2015) The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator. J. Struct. Biol. 192, 1-13
    • (2015) J. Struct. Biol. , vol.192 , pp. 1-13
    • Su, T.1    Liu, S.2    Wang, K.3    Chi, K.4    Zhu, D.5    Wei, T.6    Huang, Y.7    Guo, L.8    Hu, W.9    Xu, S.10    Lin, Z.11    Gu, L.12
  • 66
    • 84867302540 scopus 로고    scopus 로고
    • The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP
    • Baraquet, C., Murakami, K., Parsek, M. R., and Harwood, C. S. (2012) The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP. Nucleic Acids Res. 40, 7207-7218
    • (2012) Nucleic Acids Res , vol.40 , pp. 7207-7218
    • Baraquet, C.1    Murakami, K.2    Parsek, M.R.3    Harwood, C.S.4
  • 67
    • 84899629752 scopus 로고    scopus 로고
    • BrlR from Pseudomonas aeruginosa is a c-di-GMP-responsive transcription factor
    • Chambers, J. R., Liao, J., Schurr, M. J., and Sauer, K. (2014) BrlR from Pseudomonas aeruginosa is a c-di-GMP-responsive transcription factor. Mol. Microbiol. 92, 471-487
    • (2014) Mol. Microbiol. , vol.92 , pp. 471-487
    • Chambers, J.R.1    Liao, J.2    Schurr, M.J.3    Sauer, K.4
  • 68
    • 84866358418 scopus 로고    scopus 로고
    • The MerR-like transcriptional regulator BrlR contributes to Pseudomonas aeruginosa biofilm tolerance
    • Liao, J., and Sauer, K. (2012) The MerR-like transcriptional regulator BrlR contributes to Pseudomonas aeruginosa biofilm tolerance. J. Bacteriol. 194, 4823-4836
    • (2012) J. Bacteriol. , vol.194 , pp. 4823-4836
    • Liao, J.1    Sauer, K.2
  • 69
    • 84880649547 scopus 로고    scopus 로고
    • The MerR-like regulator BrlR confers biofilm tolerance by activating multidrug efflux pumps in Pseudomonas aeruginosa biofilms
    • Liao, J., Schurr, M. J., and Sauer, K. (2013) The MerR-like regulator BrlR confers biofilm tolerance by activating multidrug efflux pumps in Pseudomonas aeruginosa biofilms. J. Bacteriol. 195, 3352-3363
    • (2013) J. Bacteriol. , vol.195 , pp. 3352-3363
    • Liao, J.1    Schurr, M.J.2    Sauer, K.3
  • 70
    • 84943279589 scopus 로고    scopus 로고
    • Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP
    • Trampari, E., Stevenson, C. E., Little, R. H., Wilhelm, T., Lawson, D. M., and Malone, J. G. (2015) Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP. J. Biol. Chem. 290, 24470-24483
    • (2015) J. Biol. Chem. , vol.290 , pp. 24470-24483
    • Trampari, E.1    Stevenson, C.E.2    Little, R.H.3    Wilhelm, T.4    Lawson, D.M.5    Malone, J.G.6
  • 72
    • 84941248644 scopus 로고    scopus 로고
    • Capture compound mass spectrometry: A powerful tool to identify novel c-di-GMP effector proteins
    • Laventie, B. J., Nesper, J., Ahrne, E., Glatter, T., Schmidt, A., and Jenal, U. (2015) Capture compound mass spectrometry: a powerful tool to identify novel c-di-GMP effector proteins. J. Vis. Exp. 10.3791/51404
    • (2015) J. Vis. Exp.
    • Laventie, B.J.1    Nesper, J.2    Ahrne, E.3    Glatter, T.4    Schmidt, A.5    Jenal, U.6
  • 73
    • 84864078697 scopus 로고    scopus 로고
    • A novel capture compound for the identification and analysis of cyclic di-GMP binding proteins
    • Nesper, J., Reinders, A., Glatter, T., Schmidt, A., and Jenal, U. (2012) A novel capture compound for the identification and analysis of cyclic di-GMP binding proteins. J. Proteomics 75, 4874-4878
    • (2012) J. Proteomics , vol.75 , pp. 4874-4878
    • Nesper, J.1    Reinders, A.2    Glatter, T.3    Schmidt, A.4    Jenal, U.5
  • 74
    • 80053091424 scopus 로고    scopus 로고
    • Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions
    • Roelofs, K. G., Wang, J., Sintim, H. O., and Lee, V. T. (2011) Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions. Proc. Natl. Acad. Sci. U.S.A. 108, 15528-15533
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 15528-15533
    • Roelofs, K.G.1    Wang, J.2    Sintim, H.O.3    Lee, V.T.4
  • 79
    • 77950370030 scopus 로고    scopus 로고
    • The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism
    • Paul, K., Nieto, V., Carlquist, W. C., Blair, D. F., and Harshey, R. M. (2010) The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol. Cell 38, 128-139
    • (2010) Mol. Cell , vol.38 , pp. 128-139
    • Paul, K.1    Nieto, V.2    Carlquist, W.C.3    Blair, D.F.4    Harshey, R.M.5
  • 80
    • 84878261687 scopus 로고    scopus 로고
    • Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis
    • Guzzo, C. R., Dunger, G., Salinas, R. K., and Farah, C. S. (2013) Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis. J. Mol. Biol. 425, 2174-2197
    • (2013) J. Mol. Biol. , vol.425 , pp. 2174-2197
    • Guzzo, C.R.1    Dunger, G.2    Salinas, R.K.3    Farah, C.S.4
  • 81
    • 80052519940 scopus 로고    scopus 로고
    • Systematic analysis of diguanylate cyclases that promote biofilm formation by Pseudomonas fluorescens Pf0-1
    • Newell, P. D., Yoshioka, S., Hvorecny, K. L., Monds, R. D., and O'Toole, G. A. (2011) Systematic analysis of diguanylate cyclases that promote biofilm formation by Pseudomonas fluorescens Pf0-1. J. Bacteriol. 193, 4685-4698
    • (2011) J. Bacteriol. , vol.193 , pp. 4685-4698
    • Newell, P.D.1    Yoshioka, S.2    Hvorecny, K.L.3    Monds, R.D.4    O'Toole, G.A.5
  • 82
    • 62149131337 scopus 로고    scopus 로고
    • Compartmentalized signalling: Spatial regulation of cAMP by the action of compartmentalized phosphodiesterases
    • Baillie, G. S. (2009) Compartmentalized signalling: spatial regulation of cAMP by the action of compartmentalized phosphodiesterases. FEBS J. 276, 1790-1799
    • (2009) FEBS J , vol.276 , pp. 1790-1799
    • Baillie, G.S.1
  • 83
    • 77953244382 scopus 로고    scopus 로고
    • Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division
    • Christen, M., Kulasekara, H. D., Christen, B., Kulasekara, B. R., Hoffman, L. R., and Miller, S. I. (2010) Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division. Science 328, 1295-1297
    • (2010) Science , vol.328 , pp. 1295-1297
    • Christen, M.1    Kulasekara, H.D.2    Christen, B.3    Kulasekara, B.R.4    Hoffman, L.R.5    Miller, S.I.6
  • 84
  • 85
    • 73649147693 scopus 로고    scopus 로고
    • Bistable expression of CsgD in biofilm development of Salmonella enterica serovar typhimurium
    • Grantcharova, N., Peters, V., Monteiro, C., Zakikhany, K., and Römling, U. (2010) Bistable expression of CsgD in biofilm development of Salmonella enterica serovar typhimurium. J. Bacteriol. 192, 456-466
    • (2010) J. Bacteriol. , vol.192 , pp. 456-466
    • Grantcharova, N.1    Peters, V.2    Monteiro, C.3    Zakikhany, K.4    Römling, U.5
  • 86
    • 0037322193 scopus 로고    scopus 로고
    • Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway
    • Wolfgang, M. C., Lee, V. T., Gilmore, M. E., and Lory, S. (2003) Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway. Dev. Cell 4, 253-263
    • (2003) Dev. Cell , vol.4 , pp. 253-263
    • Wolfgang, M.C.1    Lee, V.T.2    Gilmore, M.E.3    Lory, S.4
  • 88
  • 89
    • 84870542263 scopus 로고    scopus 로고
    • Nucleotide, c-di-GMP, c-di-AMP, cGMP, cAMP, (p)ppGpp signaling in bacteria and implications in pathogenesis
    • Kalia, D., Merey, G., Nakayama, S., Zheng, Y., Zhou, J., Luo, Y., Guo, M., Roembke, B. T., and Sintim, H. O. (2013) Nucleotide, c-di-GMP, c-di-AMP, cGMP, cAMP, (p)ppGpp signaling in bacteria and implications in pathogenesis. Chem. Soc. Rev. 42, 305-341
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 305-341
    • Kalia, D.1    Merey, G.2    Nakayama, S.3    Zheng, Y.4    Zhou, J.5    Luo, Y.6    Guo, M.7    Roembke, B.T.8    Sintim, H.O.9
  • 91
    • 84925379769 scopus 로고    scopus 로고
    • Novel functions of (p)ppGpp and cyclic di-GMP in mycobacterial physiology revealed by phenotype microarray analysis of wild-type and isogenic strains of Mycobacterium smegmatis
    • Gupta, K. R., Kasetty, S., and Chatterji, D. (2015) Novel functions of (p)ppGpp and cyclic di-GMP in mycobacterial physiology revealed by phenotype microarray analysis of wild-type and isogenic strains of Mycobacterium smegmatis. Appl. Environ. Microbiol. 81, 2571-2578
    • (2015) Appl. Environ. Microbiol. , vol.81 , pp. 2571-2578
    • Gupta, K.R.1    Kasetty, S.2    Chatterji, D.3
  • 92
    • 0021992199 scopus 로고
    • Tobramycin resistance of Pseudomonas aeruginosa cells growing as a biofilm on urinary catheter material
    • Nickel, J. C., Ruseska, I., Wright, J. B., and Costerton, J. W. (1985) Tobramycin resistance of Pseudomonas aeruginosa cells growing as a biofilm on urinary catheter material. Antimicrob. Agents Chemother. 27, 619-624
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 619-624
    • Nickel, J.C.1    Ruseska, I.2    Wright, J.B.3    Costerton, J.W.4
  • 93
    • 0242569490 scopus 로고    scopus 로고
    • Antimicrobial resistance of Pseudomonas aeruginosa biofilms
    • Drenkard, E. (2003) Antimicrobial resistance of Pseudomonas aeruginosa biofilms. Microbes Infect. 5, 1213-1219
    • (2003) Microbes Infect , vol.5 , pp. 1213-1219
    • Drenkard, E.1
  • 94
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah, T. F., and O'Toole, G. A. (2001) Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol. 9, 34-39
    • (2001) Trends Microbiol , vol.9 , pp. 34-39
    • Mah, T.F.1    O'Toole, G.A.2
  • 98
    • 84900462701 scopus 로고    scopus 로고
    • High-throughput screening using the differential radial capillary action of ligand assay identifies ebselen as an inhibitor of diguanylate cyclases
    • Lieberman, O. J., Orr, M. W., Wang, Y., and Lee, V. T. (2014) High-throughput screening using the differential radial capillary action of ligand assay identifies ebselen as an inhibitor of diguanylate cyclases. ACS Chem. Biol. 9, 183-192
    • (2014) ACS Chem. Biol. , vol.9 , pp. 183-192
    • Lieberman, O.J.1    Orr, M.W.2    Wang, Y.3    Lee, V.T.4
  • 99
    • 37349027967 scopus 로고    scopus 로고
    • Gac/Rsm signal transduction pathway of gamma-proteobacteria: From RNA recognition to regulation of social behaviour
    • Lapouge, K., Schubert, M., Allain, F. H., and Haas, D. (2008) Gac/Rsm signal transduction pathway of gamma-proteobacteria: from RNA recognition to regulation of social behaviour. Mol. Microbiol. 67, 241-253
    • (2008) Mol. Microbiol. , vol.67 , pp. 241-253
    • Lapouge, K.1    Schubert, M.2    Allain, F.H.3    Haas, D.4
  • 100
    • 82155202495 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa sensor RetS switches type III and type VI secretion via c-di-GMP signalling
    • Moscoso, J. A., Mikkelsen, H., Heeb, S., Williams, P., and Filloux, A. (2011) The Pseudomonas aeruginosa sensor RetS switches type III and type VI secretion via c-di-GMP signalling. Environ. Microbiol. 13, 3128-3138
    • (2011) Environ. Microbiol. , vol.13 , pp. 3128-3138
    • Moscoso, J.A.1    Mikkelsen, H.2    Heeb, S.3    Williams, P.4    Filloux, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.