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Volumn 40, Issue 15, 2012, Pages 7207-7218

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

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CYCLIC DIMERIC GMP; CYCLIC GMP; FELN PROTEIN; FLEQ PROTEIN; UNCLASSIFIED DRUG;

EID: 84867302540     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks384     Document Type: Article
Times cited : (208)

References (74)
  • 1
    • 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. USA, 102, 14422-14427.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14422-14427
    • Hickman, J.W.1    Tifrea, D.F.2    Harwood, C.S.3
  • 2
    • 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 Romling, 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    Romling, U.5
  • 3
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler, A. D. and Camilli, A. (2004) Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol. Microbiol., 53, 857-869.
    • (2004) Mol. Microbiol. , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 4
    • 38749146920 scopus 로고    scopus 로고
    • Get the message out: Cyclic-Di-GMP regulates multiple levels of flagellum-based motility
    • Wolfe, A. J. and Visick, K. L. (2008) Get the message out: cyclic-Di-GMP regulates multiple levels of flagellum-based motility. J. Bacteriol., 190, 463-475.
    • (2008) J. Bacteriol. , vol.190 , pp. 463-475
    • Wolfe, A.J.1    Visick, K.L.2
  • 5
    • 33645213032 scopus 로고    scopus 로고
    • Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP
    • Thormann, K. M., Duttler, S., Saville, R. M., Hyodo, M., Shukla, S., Hayakawa, Y. and Spormann, A. M. (2006) Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP. J. Bacteriol., 188, 2681-2691.
    • (2006) J. Bacteriol. , vol.188 , pp. 2681-2691
    • Thormann, K.M.1    Duttler, S.2    Saville, R.M.3    Hyodo, M.4    Shukla, S.5    Hayakawa, Y.6    Spormann, A.M.7
  • 7
    • 33645296297 scopus 로고    scopus 로고
    • Cyclic-diGMP signal transduction systems in Vibrio cholerae: Modulation of rugosity and biofilm formation
    • Lim, B., Beyhan, S., Meir, J. and Yildiz, F. H. (2006) Cyclic-diGMP signal transduction systems in Vibrio cholerae: modulation of rugosity and biofilm formation. Mol. Microbiol., 60, 331-348.
    • (2006) Mol. Microbiol. , vol.60 , pp. 331-348
    • Lim, B.1    Beyhan, S.2    Meir, J.3    Yildiz, F.H.4
  • 8
    • 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. and Jenal, U. (2003) Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol. Microbiol., 47, 1695-1708.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 9
    • 33846847846 scopus 로고    scopus 로고
    • C-di-GMP-mediated regulation of virulence and biofilm formation
    • Cotter, P. A. and Stibitz, S. (2007) c-di-GMP-mediated regulation of virulence and biofilm formation. Curr. Opin. Microbiol., 10, 17-23.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 17-23
    • Cotter, P.A.1    Stibitz, S.2
  • 10
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo, R., Pratt, J. T. and Camilli, A. (2007) Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu. Rev. Microbiol., 61, 131-148.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 11
    • 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
  • 12
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal, U. and Malone, J. (2006) Mechanisms of cyclic-di-GMP signaling in bacteria. Ann. Rev. Genet., 40, 385-407.
    • (2006) Ann. Rev. Genet. , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 13
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: Mechanisms of signalling
    • Mills, E., Pultz, I. S., Kulasekara, H. D. and Miller, S. I. (2011) The bacterial second messenger c-di-GMP: mechanisms of signalling. Cell Microbiol., 13, 1122-1129.
    • (2011) Cell Microbiol. , vol.13 , pp. 1122-1129
    • Mills, E.1    Pultz, I.S.2    Kulasekara, H.D.3    Miller, S.I.4
  • 14
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer, T. and Jenal, U. (2009) Structural and mechanistic determinants of c-di-GMP signalling. Nat. Rev. Microbiol., 7, 724-735.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 15
    • 77954933973 scopus 로고    scopus 로고
    • 30, 50-Cyclic diguanylic acid: A small nucleotide that makes big impacts
    • Yan, H. and Chen, W. (2010) 30, 50-Cyclic diguanylic acid: a small nucleotide that makes big impacts. Chem. Soc. Rev., 39, 2914-2924.
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 2914-2924
    • Yan, H.1    Chen, W.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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, D. A., Simm, R., Romling, U. and Gomelsky, M. (2006) 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) J. Biol. Chem. , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Romling, U.3    Gomelsky, M.4
  • 19
    • 34547682212 scopus 로고    scopus 로고
    • The second messenger bis-(30-50)-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-(30-50)-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
  • 20
    • 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
  • 21
    • 62549150834 scopus 로고    scopus 로고
    • LapD is a bis-(30, 50)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1
    • Newell, P. D., Monds, R. D. and O'Toole, G. A. (2009) LapD is a bis-(30, 50)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc. Natl. Acad. Sci. USA, 106, 3461-3466.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'Toole, G.A.3
  • 23
    • 80053932725 scopus 로고    scopus 로고
    • The CRP/FNR family protein Bcam1349 is a c-di-GMP effector that regulates biofilm formation in the respiratory pathogen Burkholderia cenocepacia
    • Fazli, M., O'Connell, A., Nilsson, M., Niehaus, K., Dow, J. M., Givskov, M., Ryan, R. P. and Tolker-Nielsen, T. (2011) The CRP/FNR family protein Bcam1349 is a c-di-GMP effector that regulates biofilm formation in the respiratory pathogen Burkholderia cenocepacia. Mol. Microbiol., 82, 327-341.
    • (2011) Mol. Microbiol. , vol.82 , pp. 327-341
    • Fazli, M.1    O'Connell, A.2    Nilsson, M.3    Niehaus, K.4    Dow, J.M.5    Givskov, M.6    Ryan, R.P.7    Tolker-Nielsen, T.8
  • 24
    • 76749083886 scopus 로고    scopus 로고
    • Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP
    • Krasteva, P. V., Fong, J. C., Shikuma, N. J., Beyhan, S., Navarro, M. V., Yildiz, F. H. and Sondermann, H. (2010) Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science, 327, 866-868.
    • (2010) Science , vol.327 , pp. 866-868
    • Krasteva, P.V.1    Fong, J.C.2    Shikuma, N.J.3    Beyhan, S.4    Navarro, M.V.5    Yildiz, F.H.6    Sondermann, H.7
  • 25
    • 75749117906 scopus 로고    scopus 로고
    • The cyclic nucleotide monophosphate domain of Xanthomonas campestris global regulator Clp defines a new class of cyclic di-GMP effectors
    • Tao, F., He, Y. W., Wu, D. H., Swarup, S. and Zhang, L. H. (2010) The cyclic nucleotide monophosphate domain of Xanthomonas campestris global regulator Clp defines a new class of cyclic di-GMP effectors. J. Bacteriol., 192, 1020-1029.
    • (2010) J. Bacteriol. , vol.192 , pp. 1020-1029
    • Tao, F.1    He, Y.W.2    Wu, D.H.3    Swarup, S.4    Zhang, L.H.5
  • 26
    • 80052315142 scopus 로고    scopus 로고
    • MrkH, a novel c-di-GMP-dependent transcriptional activator, controls Klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression
    • Wilksch, J. J., Yang, J., Clements, A., Gabbe, J. L., Short, K. R., Cao, H., Cavaliere, R., James, C. E., Whitchurch, C. B., Schembri, M. A. et al. (2011) MrkH, a novel c-di-GMP-dependent transcriptional activator, controls Klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression. PLoS Pathog., 7, e1002204.
    • (2011) PLoS Pathog. , vol.7
    • Wilksch, J.J.1    Yang, J.2    Clements, A.3    Gabbe, J.L.4    Short, K.R.5    Cao, H.6    Cavaliere, R.7    James, C.E.8    Whitchurch, C.B.9    Schembri, M.A.10
  • 27
    • 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
  • 28
    • 76449122382 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix
    • Borlee, B. R., Goldman, A. D., Murakami, K., Samudrala, R., Wozniak, D. J. and Parsek, M. R. (2010) Pseudomonas aeruginosa uses a cyclic-di-GMP- regulated adhesin to reinforce the biofilm extracellular matrix. Mol. Microbiol., 75, 827-842.
    • (2010) Mol. Microbiol. , vol.75 , pp. 827-842
    • Borlee, B.R.1    Goldman, A.D.2    Murakami, K.3    Samudrala, R.4    Wozniak, D.J.5    Parsek, M.R.6
  • 29
    • 0030924138 scopus 로고    scopus 로고
    • A transcriptional activator, FleQ, regulates mucin adhesion and flagellar gene expression in Pseudomonas aeruginosa in a cascade manner
    • Arora, S. K., Ritchings, B. W., Almira, E. C., Lory, S. and Ramphal, R. (1997) A transcriptional activator, FleQ, regulates mucin adhesion and flagellar gene expression in Pseudomonas aeruginosa in a cascade manner. J. Bacteriol., 179, 5574-5581.
    • (1997) J. Bacteriol. , vol.179 , pp. 5574-5581
    • Arora, S.K.1    Ritchings, B.W.2    Almira, E.C.3    Lory, S.4    Ramphal, R.5
  • 30
    • 0242521414 scopus 로고    scopus 로고
    • A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa
    • Dasgupta, N., Wolfgang, M. C., Goodman, A. L., Arora, S. K., Jyot, J., Lory, S. and Ramphal, R. (2003) A four-tiered transcriptional regulatory circuit controls flagellar biogenesis in Pseudomonas aeruginosa. Mol. Microbiol., 50, 809-824.
    • (2003) Mol. Microbiol. , vol.50 , pp. 809-824
    • Dasgupta, N.1    Wolfgang, M.C.2    Goodman, A.L.3    Arora, S.K.4    Jyot, J.5    Lory, S.6    Ramphal, R.7
  • 31
    • 0036777449 scopus 로고    scopus 로고
    • FleQ, the major flagellar gene regulator in Pseudomonas aeruginosa, binds to enhancer sites located either upstream or atypically downstream of the RpoN binding site
    • Jyot, J., Dasgupta, N. and Ramphal, R. (2002) FleQ, the major flagellar gene regulator in Pseudomonas aeruginosa, binds to enhancer sites located either upstream or atypically downstream of the RpoN binding site. J. Bacteriol., 184, 5251-5260.
    • (2002) J. Bacteriol. , vol.184 , pp. 5251-5260
    • Jyot, J.1    Dasgupta, N.2    Ramphal, R.3
  • 32
    • 66149084428 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa rugose small-colony variants have adaptations that likely promote persistence in the cystic fibrosis lung
    • Starkey, M., Hickman, J. H., Ma, L., Zhang, N., De Long, S., Hinz, A., Palacios, S., Manoil, C., Kirisits, M. J., Starner, T. D. et al. (2009) Pseudomonas aeruginosa rugose small-colony variants have adaptations that likely promote persistence in the cystic fibrosis lung. J. Bacteriol., 191, 3492-3503.
    • (2009) J. Bacteriol. , vol.191 , pp. 3492-3503
    • Starkey, M.1    Hickman, J.H.2    Ma, L.3    Zhang, N.4    De Long, S.5    Hinz, A.6    Palacios, S.7    Manoil, C.8    Kirisits, M.J.9    Starner, T.D.10
  • 33
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin, E. V. (1993) A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J. Mol. Biol., 229, 1165-1174.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 34
    • 0033987999 scopus 로고    scopus 로고
    • Flen, a gene that regulates flagellar number in Pseudomonas aeruginosa
    • Dasgupta, N., Arora, S. K. and Ramphal, R. (2000) fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa. J. Bacteriol., 182, 357-364.
    • (2000) J. Bacteriol. , vol.182 , pp. 357-364
    • Dasgupta, N.1    Arora, S.K.2    Ramphal, R.3
  • 35
    • 0034748979 scopus 로고    scopus 로고
    • Interaction of the antiactivator FleN with the transcriptional activator FleQ regulates flagellar number in Pseudomonas aeruginosa
    • Dasgupta, N. and Ramphal, R. (2001) Interaction of the antiactivator FleN with the transcriptional activator FleQ regulates flagellar number in Pseudomonas aeruginosa. J. Bacteriol., 183, 6636-6644.
    • (2001) J. Bacteriol. , vol.183 , pp. 6636-6644
    • Dasgupta, N.1    Ramphal, R.2
  • 36
    • 23744479941 scopus 로고    scopus 로고
    • Characterization of colony morphology variants isolated from Pseudomonas aeruginosa biofilms
    • Kirisits, M. J., Prost, L., Starkey, M. and Parsek, M. R. (2005) Characterization of colony morphology variants isolated from Pseudomonas aeruginosa biofilms. Appl. Environ. Microbiol., 71, 4809-4821.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4809-4821
    • Kirisits, M.J.1    Prost, L.2    Starkey, M.3    Parsek, M.R.4
  • 37
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: Application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang, T. T., Karkhoff-Schweizer, R. R., Kutchma, A. J. and Schweizer, H. P. (1998) A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene, 212, 77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 38
    • 32244448730 scopus 로고    scopus 로고
    • A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: Application for DNA fragment transfer between chromosomes and plasmid transformation
    • Choi, K. H., Kumar, A. and Schweizer, H. P. (2006) A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation. J. Microbiol. Methods, 64, 391-397.
    • (2006) J. Microbiol. Methods , vol.64 , pp. 391-397
    • Choi, K.H.1    Kumar, A.2    Schweizer, H.P.3
  • 39
    • 0033580277 scopus 로고    scopus 로고
    • Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator
    • Newman, J. R. and Fuqua, C. (1999) Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator. Gene, 227, 197-203.
    • (1999) Gene , vol.227 , pp. 197-203
    • Newman, J.R.1    Fuqua, C.2
  • 40
    • 0034935287 scopus 로고    scopus 로고
    • Nonradiochemical DNase I footprinting by capillary electrophoresis
    • Wilson, D. O., Johnson, P. and McCord, B. R. (2001) Nonradiochemical DNase I footprinting by capillary electrophoresis. Electrophoresis, 22, 1979-1986.
    • (2001) Electrophoresis , vol.22 , pp. 1979-1986
    • Wilson, D.O.1    Johnson, P.2    McCord, B.R.3
  • 41
    • 0033729216 scopus 로고    scopus 로고
    • Integration-proficient Pseudomonas aeruginosa vectors for isolation of single-copy chromosomal lacZ and lux gene fusions
    • 952
    • Becher, A. and Schweizer, H. P. (2000) Integration-proficient Pseudomonas aeruginosa vectors for isolation of single-copy chromosomal lacZ and lux gene fusions. BioTechniques, 29, 948-950, 952.
    • (2000) BioTechniques , vol.29 , pp. 948-950
    • Becher, A.1    Schweizer, H.P.2
  • 42
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 43
    • 3042735895 scopus 로고    scopus 로고
    • Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix
    • Friedman, L. and Kolter, R. (2004) Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix. J. Bacteriol., 186, 4457-4465.
    • (2004) J. Bacteriol. , vol.186 , pp. 4457-4465
    • Friedman, L.1    Kolter, R.2
  • 45
    • 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, 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
    • Guvener, Z.T.1    Harwood, C.S.2
  • 46
    • 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, pii:e00183-10.
    • (2010) MBio , vol.1
    • 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
  • 47
    • 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
  • 49
    • 0024564064 scopus 로고
    • Regulation of transcription in Escherichia coli from the mer and merR promoters in the transposon Tn501
    • Lund, P. A. and Brown, N. L. (1989) Regulation of transcription in Escherichia coli from the mer and merR promoters in the transposon Tn501. J. Mol. Biol., 205, 343-353.
    • (1989) J. Mol. Biol. , vol.205 , pp. 343-353
    • Lund, P.A.1    Brown, N.L.2
  • 50
    • 0022636264 scopus 로고
    • Transcriptional regulation of the mercury-resistance genes of transposon Tn501
    • Lund, P. A., Ford, S. J. and Brown, N. L. (1986) Transcriptional regulation of the mercury-resistance genes of transposon Tn501. J. Gen. Microbiol., 132, 465-480.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 465-480
    • Lund, P.A.1    Ford, S.J.2    Brown, N.L.3
  • 51
    • 0037189573 scopus 로고    scopus 로고
    • The central domain of Escherichia coli TyrR is responsible for hexamerization associated with tyrosine-mediated repression of gene expression
    • Dixon, M. P., Pau, R. N., Howlett, G. J., Dunstan, D. E., Sawyer, W. H. and Davidson, B. E. (2002) The central domain of Escherichia coli TyrR is responsible for hexamerization associated with tyrosine-mediated repression of gene expression. J. Biol. Chem., 277, 23186-23192.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23186-23192
    • Dixon, M.P.1    Pau, R.N.2    Howlett, G.J.3    Dunstan, D.E.4    Sawyer, W.H.5    Davidson, B.E.6
  • 52
    • 0025740385 scopus 로고
    • TyrR protein of Escherichia coli and its role as repressor and activator
    • Pittard, A. J. and Davidson, B. E. (1991) TyrR protein of Escherichia coli and its role as repressor and activator. Mol. Microbiol., 5, 1585-1592.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1585-1592
    • Pittard, A.J.1    Davidson, B.E.2
  • 53
    • 1942519889 scopus 로고    scopus 로고
    • Mode of action of the TyrR protein: Repression and activation of the tyrP promoter of Escherichia coli
    • Yang, J., Hwang, J. S., Camakaris, H., Irawaty, W., Ishihama, A. and Pittard, J. (2004) Mode of action of the TyrR protein: repression and activation of the tyrP promoter of Escherichia coli. Mol. Microbiol., 52, 243-256.
    • (2004) Mol. Microbiol. , vol.52 , pp. 243-256
    • Yang, J.1    Hwang, J.S.2    Camakaris, H.3    Irawaty, W.4    Ishihama, A.5    Pittard, J.6
  • 55
    • 0026317737 scopus 로고
    • Mutational analysis of repression and activation of the tyrP gene in Escherichia coli
    • Andrews, A. E., Lawley, B. and Pittard, A. J. (1991) Mutational analysis of repression and activation of the tyrP gene in Escherichia coli. J. Bacteriol., 173, 5068-5078.
    • (1991) J. Bacteriol. , vol.173 , pp. 5068-5078
    • Andrews, A.E.1    Lawley, B.2    Pittard, A.J.3
  • 56
    • 41949098532 scopus 로고    scopus 로고
    • Dual role of LldR in regulation of the lldPRD operon, involved in L-lactate metabolism in Escherichia coli
    • Aguilera, L., Campos, E., Gimenez, R., Badia, J., Aguilar, J. and Baldoma, L. (2008) Dual role of LldR in regulation of the lldPRD operon, involved in L-lactate metabolism in Escherichia coli. J. Bacteriol., 190, 2997-3005.
    • (2008) J. Bacteriol. , vol.190 , pp. 2997-3005
    • Aguilera, L.1    Campos, E.2    Gimenez, R.3    Badia, J.4    Aguilar, J.5    Baldoma, L.6
  • 57
    • 33846829718 scopus 로고    scopus 로고
    • Catabolism of phenylalanine by Pseudomonas putida: The NtrC-family PhhR regulator binds to two sites upstream from the phhA gene and stimulates transcription with sigma70
    • Herrera, M. C. and Ramos, J. L. (2007) Catabolism of phenylalanine by Pseudomonas putida: the NtrC-family PhhR regulator binds to two sites upstream from the phhA gene and stimulates transcription with sigma70. J. Mol. Biol., 366, 1374-1386.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1374-1386
    • Herrera, M.C.1    Ramos, J.L.2
  • 58
    • 0032525980 scopus 로고    scopus 로고
    • A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase
    • Bowman, W. C. and Kranz, R. G. (1998) A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase. Genes. Dev., 12, 1884-1893.
    • (1998) Genes. Dev. , vol.12 , pp. 1884-1893
    • Bowman, W.C.1    Kranz, R.G.2
  • 59
    • 0033456155 scopus 로고    scopus 로고
    • The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system
    • Dischert, W., Vignais, P. M. and Colbeau, A. (1999) The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system. Mol. Microbiol., 34, 995-1006.
    • (1999) Mol. Microbiol. , vol.34 , pp. 995-1006
    • Dischert, W.1    Vignais, P.M.2    Colbeau, A.3
  • 60
    • 33646181238 scopus 로고    scopus 로고
    • Structural and functional studies of the response regulator HupR
    • Davies, K. M., Skamnaki, V., Johnson, L. N. and Venien-Bryan, C. (2006) Structural and functional studies of the response regulator HupR. J. Mol. Biol., 359, 276-288.
    • (2006) J. Mol. Biol. , vol.359 , pp. 276-288
    • Davies, K.M.1    Skamnaki, V.2    Johnson, L.N.3    Venien-Bryan, C.4
  • 61
    • 77949325119 scopus 로고    scopus 로고
    • The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris
    • Chin, K. H., Lee, Y. C., Tu, Z. L., Chen, C. H., Tseng, Y. H., Yang, J. M., Ryan, R. P., McCarthy, Y., Dow, J. M., Wang, A. H. et al. (2010) The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris. J. Mol. Biol., 396, 646-662.
    • (2010) J. Mol. Biol. , vol.396 , pp. 646-662
    • Chin, K.H.1    Lee, Y.C.2    Tu, Z.L.3    Chen, C.H.4    Tseng, Y.H.5    Yang, J.M.6    Ryan, R.P.7    McCarthy, Y.8    Dow, J.M.9    Wang, A.H.10
  • 62
    • 70350436270 scopus 로고    scopus 로고
    • Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv
    • Leduc, J. L. and Roberts, G. P. (2009) Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri. J. Bacteriol., 191, 7121-7122.
    • (2009) Citri. J. Bacteriol. , vol.191 , pp. 7121-7122
    • Leduc, J.L.1    Roberts, G.P.2
  • 63
    • 0030798605 scopus 로고    scopus 로고
    • Clues and consequences of DNA bending in transcription
    • Perez-Martin, J. and de Lorenzo, V. (1997) Clues and consequences of DNA bending in transcription. Annu. Rev. Microbiol., 51, 593-628.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 593-628
    • Perez-Martin, J.1    De Lorenzo, V.2
  • 64
    • 0028918916 scopus 로고
    • DNA-bend modulation in a repressor-to-activator switching mechanism
    • Ansari, A. Z., Bradner, J. E. and O'Halloran, T. V. (1995) DNA-bend modulation in a repressor-to-activator switching mechanism. Nature, 374, 371-375.
    • (1995) Nature , vol.374 , pp. 371-375
    • Ansari, A.Z.1    Bradner, J.E.2    O'Halloran, T.V.3
  • 65
    • 0026530492 scopus 로고
    • Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR
    • Ansari, A. Z., Chael, M. L. and O'Halloran, T. V. (1992) Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR. Nature, 355, 87-89.
    • (1992) Nature , vol.355 , pp. 87-89
    • Ansari, A.Z.1    Chael, M.L.2    O'Halloran, T.V.3
  • 66
    • 18244389706 scopus 로고    scopus 로고
    • Modulating DNA bending affects NodD-mediated transcriptional control in Rhizobium leguminosarum
    • Chen, X. C., Feng, J., Hou, B. H., Li, F. Q., Li, Q. and Hong, G. F. (2005) Modulating DNA bending affects NodD-mediated transcriptional control in Rhizobium leguminosarum. Nucleic Acids Res., 33, 2540-2548.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2540-2548
    • Chen, X.C.1    Feng, J.2    Hou, B.H.3    Li, F.Q.4    Li, Q.5    Hong, G.F.6
  • 67
    • 34248587997 scopus 로고    scopus 로고
    • The transcriptional repressor TtgV recognizes a complex operator as a tetramer and induces convex DNA bending
    • Guazzaroni, M. E., Krell, T., Gutierrez del Arroyo, P., Velez, M., Jimenez, M., Rivas, G. and Ramos, J. L. (2007) The transcriptional repressor TtgV recognizes a complex operator as a tetramer and induces convex DNA bending. J. Mol. Biol., 369, 927-939.
    • (2007) J. Mol. Biol. , vol.369 , pp. 927-939
    • Guazzaroni, M.E.1    Krell, T.2    Gutierrez Del Arroyo, P.3    Velez, M.4    Jimenez, M.5    Rivas, G.6    Ramos, J.L.7
  • 68
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks, S. E. and Oyston, P. C. (2008) Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology, 154, 3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 69
    • 0024968107 scopus 로고
    • The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex
    • O'Halloran, T. V., Frantz, B., Shin, M. K., Ralston, D. M. and Wright, J. G. (1989) The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex. Cell, 56, 119-129.
    • (1989) Cell , vol.56 , pp. 119-129
    • O'Halloran, T.V.1    Frantz, B.2    Shin, M.K.3    Ralston, D.M.4    Wright, J.G.5
  • 70
    • 0028969228 scopus 로고
    • Differential DNA bending introduced by the Pseudomonas putida LysR-type regulator, CatR, at the plasmid-borne pheBA and chromosomal catBC promoters
    • Parsek, M. R., Kivisaar, M. and Chakrabarty, A. M. (1995) Differential DNA bending introduced by the Pseudomonas putida LysR-type regulator, CatR, at the plasmid-borne pheBA and chromosomal catBC promoters. Mol. Microbiol., 15, 819-828.
    • (1995) Mol. Microbiol. , vol.15 , pp. 819-828
    • Parsek, M.R.1    Kivisaar, M.2    Chakrabarty, A.M.3
  • 71
    • 0038349270 scopus 로고    scopus 로고
    • MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation
    • Lutkenhaus, J. and Sundaramoorthy, M. (2003) MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Mol. Microbiol., 48, 295-303.
    • (2003) Mol. Microbiol. , vol.48 , pp. 295-303
    • Lutkenhaus, J.1    Sundaramoorthy, M.2
  • 72
    • 0037241005 scopus 로고    scopus 로고
    • A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum
    • Hu, Z. and Lutkenhaus, J. (2003) A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum. Mol. Microbiol., 47, 345-355.
    • (2003) Mol. Microbiol. , vol.47 , pp. 345-355
    • Hu, Z.1    Lutkenhaus, J.2
  • 73
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer-a conserved biological switch
    • Leonard, T. A., Butler, P. J. and Lowe, J. (2005) Bacterial chromosome segregation: structure and DNA binding of the Soj dimer-a conserved biological switch. EMBO J., 24, 270-282.
    • (2005) EMBO J. , vol.24 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 74
    • 79551521160 scopus 로고    scopus 로고
    • The Pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa
    • Colvin, K. M., Gordon, V. D., Murakami, K., Borlee, B. R., Wozniak, D. J., Wong, G. C. and Parsek, M. R. (2011) The Pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa. PLoS Pathog., 7, e1001264.
    • (2011) PLoS Pathog. , vol.7
    • Colvin, K.M.1    Gordon, V.D.2    Murakami, K.3    Borlee, B.R.4    Wozniak, D.J.5    Wong, G.C.6    Parsek, M.R.7


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