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Volumn 188, Issue 9, 2006, Pages 3290-3298

Characterization of the transcriptional activators SalA and SyrF, which are required for syringomycin and syringopeptin production by Pseudomonas syringae pv. syringae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA GLUCURONIDASE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; PLANT TOXIN; PROTEIN SALA; PROTEIN SYRF; SYRINGOMYCIN; SYRINGOPEPTIN; UNCLASSIFIED DRUG;

EID: 33646266044     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.9.3290-3298.2006     Document Type: Article
Times cited : (32)

References (78)
  • 2
    • 1642567934 scopus 로고    scopus 로고
    • Functional analysis of genes involved in the synthesis of syringolin a by Pseudomonas syringae pv. syringae B301D-R
    • Amrein, H., S. Makart, J. Granado, R. Shakya, J. Schneider-Pokorny, and R. Dudler. 2004. Functional analysis of genes involved in the synthesis of syringolin A by Pseudomonas syringae pv. syringae B301D-R. Mol. Plant-Microbe Interact. 17:90-97.
    • (2004) Mol. Plant-Microbe Interact. , vol.17 , pp. 90-97
    • Amrein, H.1    Makart, S.2    Granado, J.3    Shakya, R.4    Schneider-Pokorny, J.5    Dudler, R.6
  • 3
    • 0025969319 scopus 로고
    • The regulatory status of the fixL-like and fixJ-like genes in Bradyrhizobium japonicum may be different from that in Rhizobium meliloti
    • Anthamatten, D., and H. Hennecke. 1991. The regulatory status of the fixL-like and fixJ-like genes in Bradyrhizobium japonicum may be different from that in Rhizobium meliloti. Mol. Gen. Genet. 225:38-48.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 38-48
    • Anthamatten, D.1    Hennecke, H.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0032838287 scopus 로고    scopus 로고
    • Influence of a putative ECF sigma factor on expression of the major outer membrane protein, OprF, in Pseudomonas aeruginosa and Pseudomonas fluorescens
    • Brinkman, F. S. L., G. Schoofs, R. E. W. Hancock, and R. De Mot. 1999. Influence of a putative ECF sigma factor on expression of the major outer membrane protein, OprF, in Pseudomonas aeruginosa and Pseudomonas fluorescens. J. Bacteriol. 181:4746-4754.
    • (1999) J. Bacteriol. , vol.181 , pp. 4746-4754
    • Brinkman, F.S.L.1    Schoofs, G.2    Hancock, R.E.W.3    De Mot, R.4
  • 6
    • 0032211618 scopus 로고    scopus 로고
    • Production of acyl-homoserine lactone quorum-sensing signals by gram-negative plant-associated bacteria
    • Cha, C., P. Gao, Y. C. Chen, P. D. Shaw, and S. K. Farrand. 1998. Production of acyl-homoserine lactone quorum-sensing signals by gram-negative plant-associated bacteria. Mol. Plant-Microbe Interact. 11:1119-1129.
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 1119-1129
    • Cha, C.1    Gao, P.2    Chen, Y.C.3    Shaw, P.D.4    Farrand, S.K.5
  • 7
    • 0026645260 scopus 로고
    • Genetic dissection of DNA-binding and luminescence gene activation by the Vibrio fischeri LuxR protein
    • Choi, S. H., and E. P. Greenberg. 1992. Genetic dissection of DNA-binding and luminescence gene activation by the Vibrio fischeri LuxR protein. J. Bacteriol. 174:4064-4069.
    • (1992) J. Bacteriol. , vol.174 , pp. 4064-4069
    • Choi, S.H.1    Greenberg, E.P.2
  • 9
    • 0023008724 scopus 로고
    • The nucleotide sequence and the transcription during sporulation of the gerE gene of Bacillus subtilis
    • Cutting, S., and J. Mandelstam. 1986. The nucleotide sequence and the transcription during sporulation of the gerE gene of Bacillus subtilis. J. Gen. Microbiol. 132:3013-3024.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 3013-3024
    • Cutting, S.1    Mandelstam, J.2
  • 11
    • 0029086289 scopus 로고
    • Nitrate and nitrite regulation of the Fnr-dependent aeg-46.5 promoter of Escherichia coli K-12 is mediated by competition between homologous response regulators (NarL and NarP) for a common DNA-binding site
    • Darwin, A. J., and V. Stewart. 1995. Nitrate and nitrite regulation of the Fnr-dependent aeg-46.5 promoter of Escherichia coli K-12 is mediated by competition between homologous response regulators (NarL and NarP) for a common DNA-binding site. J. Mol. Biol. 251:15-29.
    • (1995) J. Mol. Biol. , vol.251 , pp. 15-29
    • Darwin, A.J.1    Stewart, V.2
  • 12
    • 0033032594 scopus 로고    scopus 로고
    • Quorum sensing in Vibrio fischeri: Elements of the luxI promoter
    • Egland, K. A., and E. P. Greenberg. 1999. Quorum sensing in Vibrio fischeri: elements of the luxI promoter. Mol. Microbiol. 31:1197-1204.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1197-1204
    • Egland, K.A.1    Greenberg, E.P.2
  • 13
    • 0037168492 scopus 로고    scopus 로고
    • Effect of phosphorylation on the interdomain interaction of the response regulator, NarL
    • Eldridge, A. M., H. S. Kang, E. Johnson, R. Gunsalus, and F. W. Dahlquist. 2002. Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry 41:15173-15180.
    • (2002) Biochemistry , vol.41 , pp. 15173-15180
    • Eldridge, A.M.1    Kang, H.S.2    Johnson, E.3    Gunsalus, R.4    Dahlquist, F.W.5
  • 14
    • 0344483912 scopus 로고    scopus 로고
    • Regulation of alginate biosynthesis in Pseudomonas syringae pv. syringae
    • Fakhr, M. K., A. Peñaloza-Vázquez, A. M. Chakrabarty, and C. L. Bender. 1999. Regulation of alginate biosynthesis in Pseudomonas syringae pv. syringae. J. Bacteriol. 181:3478-3485.
    • (1999) J. Bacteriol. , vol.181 , pp. 3478-3485
    • Fakhr, M.K.1    Peñaloza-Vázquez, A.2    Chakrabarty, A.M.3    Bender, C.L.4
  • 15
    • 0036338424 scopus 로고    scopus 로고
    • Role of the C-terminal domain of the alpha subunit of RNA polymerase in LuxR-dependent transcriptional activation of the lux operon during quorum sensing
    • Finney, A. H., R. J. Blick, K. Murakami, A. Ishihama, and A. M. Stevens. 2002. Role of the C-terminal domain of the alpha subunit of RNA polymerase in LuxR-dependent transcriptional activation of the lux operon during quorum sensing. J. Bacteriol. 184:4520-4528.
    • (2002) J. Bacteriol. , vol.184 , pp. 4520-4528
    • Finney, A.H.1    Blick, R.J.2    Murakami, K.3    Ishihama, A.4    Stevens, A.M.5
  • 16
    • 12344310625 scopus 로고    scopus 로고
    • Erwinia chrysanthemi requires a second iron transport route dependent of the siderophore achromobactin for extracellular growth and plant infection
    • Franza, T., B. Mahé, and D. Expert. 2005. Erwinia chrysanthemi requires a second iron transport route dependent of the siderophore achromobactin for extracellular growth and plant infection. Mol. Microbiol. 55:261-275.
    • (2005) Mol. Microbiol. , vol.55 , pp. 261-275
    • Franza, T.1    Mahé, B.2    Expert, D.3
  • 17
    • 0036731699 scopus 로고    scopus 로고
    • Listening in on bacteria: Acyl-homoserine lactone signalling
    • Fuqua, C., and E. P. Greenberg. 2002. Listening in on bacteria: acyl-homoserine lactone signalling. Nat. Rev. Mol. Cell Biol. 3:685-695.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 685-695
    • Fuqua, C.1    Greenberg, E.P.2
  • 18
    • 0029818809 scopus 로고    scopus 로고
    • Census and consensus in bacterial ecosystems: The LuxR-LuxI family of quorum-sensing transcriptional regulators
    • Fuqua, C., S. C. Winans, and E. P. Greenberg. 1996. Census and consensus in bacterial ecosystems: the LuxR-LuxI family of quorum-sensing transcriptional regulators. Annu. Rev. Microbiol. 50:727-751.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 727-751
    • Fuqua, C.1    Winans, S.C.2    Greenberg, E.P.3
  • 19
    • 0025755803 scopus 로고
    • Cloning and characterization of the Pseudomonas aeruginosa lasR gene, a transcriptional activator of elastase expression
    • Gambello, M. J., and B. H. Iglewski. 1991. Cloning and characterization of the Pseudomonas aeruginosa lasR gene, a transcriptional activator of elastase expression. J. Bacteriol. 173:3000-3009.
    • (1991) J. Bacteriol. , vol.173 , pp. 3000-3009
    • Gambello, M.J.1    Iglewski, B.H.2
  • 20
    • 0026647311 scopus 로고
    • Transformation of Acidiphilium by electroporation and conjugation
    • Glenn, A. W., F. F. Roberto, and T. E. Ward. 1992. Transformation of Acidiphilium by electroporation and conjugation. Can. J. Microbiol. 38:387-393.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 387-393
    • Glenn, A.W.1    Roberto, F.F.2    Ward, T.E.3
  • 21
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S. G. N., J. Jessee, F. R. Bloom, and D. Hanahan. 1990. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc. Natl. Acad. Sci. USA 87:4645-4649.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4645-4649
    • Grant, S.G.N.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 22
    • 0000284384 scopus 로고
    • Molecular and genetic analysis of toxin production by pathovars of Pseudomonas syringae
    • Gross, D. C. 1991. Molecular and genetic analysis of toxin production by pathovars of Pseudomonas syringae. Annu. Rev. Phytopathol. 29:247-278.
    • (1991) Annu. Rev. Phytopathol. , vol.29 , pp. 247-278
    • Gross, D.C.1
  • 23
    • 0002351805 scopus 로고
    • Production and purification of syringomycin, a phytotoxin produced by Pseudomonas syringae
    • Gross, D. C., and J. E. DeVay. 1977. Production and purification of syringomycin, a phytotoxin produced by Pseudomonas syringae. Physiol. Plant Pathol. 11:13-28.
    • (1977) Physiol. Plant Pathol. , vol.11 , pp. 13-28
    • Gross, D.C.1    Devay, J.E.2
  • 24
    • 0032484013 scopus 로고    scopus 로고
    • Characterization of the syringomycin synthetase gene cluster: A link between prokaryotic and eukaryotic peptide synthetases
    • Guenzi, E., G. Galli, I. Grgurina, D. C. Gross, and G. Grandi. 1998. Characterization of the syringomycin synthetase gene cluster: a link between prokaryotic and eukaryotic peptide synthetases. J. Biol. Chem. 273:32857-32863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32857-32863
    • Guenzi, E.1    Galli, G.2    Grgurina, I.3    Gross, D.C.4    Grandi, G.5
  • 25
    • 0029898120 scopus 로고    scopus 로고
    • Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities
    • Hassett, D. J., P. A. Sokol, M. L. Howell, J. F. Ma, H. T. Schweizer, U. Ochsner, and M. L. Vasil. 1996. Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities. J. Bacteriol. 178:3996-4003.
    • (1996) J. Bacteriol. , vol.178 , pp. 3996-4003
    • Hassett, D.J.1    Sokol, P.A.2    Howell, M.L.3    Ma, J.F.4    Schweizer, H.T.5    Ochsner, U.6    Vasil, M.L.7
  • 26
    • 0027482770 scopus 로고
    • Cloning and characterization of the Pseudomonas aeruginosa sodA and sodB genes encoding manganese- and iron-cofactored superoxide dismutase: Demonstration of increased manganese superoxide dismutase activity in alginate-producing bacteria
    • Hassett, D. J., W. A. Woodruff, D. J. Wozniak, M. L. Vasil, M. S. Cohen, and D. E. Ohman. 1993. Cloning and characterization of the Pseudomonas aeruginosa sodA and sodB genes encoding manganese- and iron-cofactored superoxide dismutase: demonstration of increased manganese superoxide dismutase activity in alginate-producing bacteria. J. Bacteriol. 175:7658-7665.
    • (1993) J. Bacteriol. , vol.175 , pp. 7658-7665
    • Hassett, D.J.1    Woodruff, W.A.2    Wozniak, D.J.3    Vasil, M.L.4    Cohen, M.S.5    Ohman, D.E.6
  • 27
    • 0035543152 scopus 로고    scopus 로고
    • Regulatory roles of the GacS/GacA two-component system in plant-associated and other Gram-negative bacteria
    • Heeb, S., and D. Haas. 2001. Regulatory roles of the GacS/GacA two-component system in plant-associated and other Gram-negative bacteria. Mol. Plant-Microbe Interact. 14:1351-1363.
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 1351-1363
    • Heeb, S.1    Haas, D.2
  • 28
    • 0027509821 scopus 로고
    • Survival of hunger and stress-the role of rpoS in early stationary phase gene regulation in Escherichia coli
    • Hengge-Aronis, R. 1993. Survival of hunger and stress-the role of rpoS in early stationary phase gene regulation in Escherichia coli. Cell 72:165-168.
    • (1993) Cell , vol.72 , pp. 165-168
    • Hengge-Aronis, R.1
  • 29
    • 0026680588 scopus 로고
    • The lemA gene required for pathogenicity of Pseudomonas syringae pv. syringae on bean is a member of a family of two-component regulators
    • Hrabak, E. M., and D. K. Willis. 1992. The lemA gene required for pathogenicity of Pseudomonas syringae pv. syringae on bean is a member of a family of two-component regulators. J. Bacteriol. 174:3011-3020.
    • (1992) J. Bacteriol. , vol.174 , pp. 3011-3020
    • Hrabak, E.M.1    Willis, D.K.2
  • 30
    • 0001197879 scopus 로고
    • Involvement of the lemA gene in production of syringomycin and protease by Pseudomonas syringae pv. syringae
    • Hrabak, E. M., and D. K. Willis. 1993. Involvement of the lemA gene in production of syringomycin and protease by Pseudomonas syringae pv. syringae. Mol. Plant-Microbe Interact. 6:368-375.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 368-375
    • Hrabak, E.M.1    Willis, D.K.2
  • 31
    • 0026643236 scopus 로고
    • Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium
    • Island, M. D., B. Y. Wei, and R. J. Kadner. 1992. Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 174:2754-2762.
    • (1992) J. Bacteriol. , vol.174 , pp. 2754-2762
    • Island, M.D.1    Wei, B.Y.2    Kadner, R.J.3
  • 32
    • 25144523330 scopus 로고    scopus 로고
    • Characterization of a resistance-nodulation-cell division transporter system associated with the syr-syp genomic island of Pseudomonas syringae pv. syringae
    • Kang, H., and D. C. Gross. 2005. Characterization of a resistance-nodulation-cell division transporter system associated with the syr-syp genomic island of Pseudomonas syringae pv. syringae. Appl. Environ. Microbiol. 71:5056-5065.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5056-5065
    • Kang, H.1    Gross, D.C.2
  • 33
    • 0000862655 scopus 로고
    • Overproduction and purification of the luxR gene product: Transcriptional activator of the Vibrio fischeri luminescence system
    • Kaplan, H. B., and E. P. Greenberg. 1987. Overproduction and purification of the luxR gene product: transcriptional activator of the Vibrio fischeri luminescence system. Proc. Natl. Acad. Sci. USA 84:6639-6643.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6639-6643
    • Kaplan, H.B.1    Greenberg, E.P.2
  • 34
    • 0032586070 scopus 로고    scopus 로고
    • 22) controls alginate production and tolerance to environmental stress in Pseudomonas syringae
    • 22) controls alginate production and tolerance to environmental stress in Pseudomonas syringae. J. Bacteriol. 181:7176-7184.
    • (1999) J. Bacteriol. , vol.181 , pp. 7176-7184
    • Keith, L.M.W.1    Bender, C.L.2
  • 35
    • 0033034448 scopus 로고    scopus 로고
    • Swarming by Pseudomonas syringae B728a requires gacS (lemA) and gacA but not the acyl-homoserine lactone biosynthetic gene ahlI
    • Kinscherf, T. G., and D. K. Willis. 1999. Swarming by Pseudomonas syringae B728a requires gacS (lemA) and gacA but not the acyl-homoserine lactone biosynthetic gene ahlI. J. Bacteriol. 181:4133-4136.
    • (1999) J. Bacteriol. , vol.181 , pp. 4133-4136
    • Kinscherf, T.G.1    Willis, D.K.2
  • 36
    • 0031807594 scopus 로고    scopus 로고
    • A newly identified regulator is required for virulence and toxin production in Pseudomonas syringae
    • Kitten, T., T. G. Kinscherf, J. L. McEvoy, and D. K. Willis. 1998. A newly identified regulator is required for virulence and toxin production in Pseudomonas syringae. Mol. Microbiol. 28:917-929.
    • (1998) Mol. Microbiol. , vol.28 , pp. 917-929
    • Kitten, T.1    Kinscherf, T.G.2    McEvoy, J.L.3    Willis, D.K.4
  • 37
    • 0034799844 scopus 로고    scopus 로고
    • Isolation and characterization of the algD gene of Pseudomonas syringae pv. phaseolicola and its distribution among other pseudomonads and related organisms
    • Koopmann, B., H. Rollwage, M. Nollenburg, and K. Rudolph. 2001. Isolation and characterization of the algD gene of Pseudomonas syringae pv. phaseolicola and its distribution among other pseudomonads and related organisms. J. Phytopathol. 149:511-519.
    • (2001) J. Phytopathol. , vol.149 , pp. 511-519
    • Koopmann, B.1    Rollwage, H.2    Nollenburg, M.3    Rudolph, K.4
  • 38
    • 0028023092 scopus 로고
    • In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12
    • Li, J., S. Kustu, and V. Stewart. 1994. In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12. J. Mol. Biol. 241:150-165.
    • (1994) J. Mol. Biol. , vol.241 , pp. 150-165
    • Li, J.1    Kustu, S.2    Stewart, V.3
  • 39
    • 0942297855 scopus 로고    scopus 로고
    • Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein
    • Li, L., D. G. Kang, and H. J. Cha. 2004. Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein. Biotechnol. Bioeng. 85:214-221.
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 214-221
    • Li, L.1    Kang, D.G.2    Cha, H.J.3
  • 40
    • 0036007225 scopus 로고    scopus 로고
    • Characterization of the salA, syrF, and syrG regulatory genes located at the right border of the syringomycin gene cluster of Pseudomonas syringae pv. syringae
    • Lu, S. E., B. K. Scholz-Schroeder, and D. C. Gross. 2002. Characterization of the salA, syrF, and syrG regulatory genes located at the right border of the syringomycin gene cluster of Pseudomonas syringae pv. syringae. Mol. Plant-Microbe Interact. 15:43-53.
    • (2002) Mol. Plant-Microbe Interact. , vol.15 , pp. 43-53
    • Lu, S.E.1    Scholz-Schroeder, B.K.2    Gross, D.C.3
  • 41
    • 0037161202 scopus 로고    scopus 로고
    • Construction of pMEKm12, an expression vector for protein production in Pseudomonas syringae
    • Lu, S. E., B. K. Scholz-Schroeder, and D. C. Gross. 2002. Construction of pMEKm12, an expression vector for protein production in Pseudomonas syringae. FEMS Microbiol. Lett. 210:115-121.
    • (2002) FEMS Microbiol. Lett. , vol.210 , pp. 115-121
    • Lu, S.E.1    Scholz-Schroeder, B.K.2    Gross, D.C.3
  • 42
    • 15244338839 scopus 로고    scopus 로고
    • Oligonucleotide microarray analysis of the salA regulon controlling phytotoxin production by Pseudomonas syringae pv. syringae
    • Lu, S. E., N. Wang, J. L. Wang, Z. J. Chen, and D. C. Gross. 2005. Oligonucleotide microarray analysis of the salA regulon controlling phytotoxin production by Pseudomonas syringae pv. syringae. Mol. Plant-Microbe Interact. 18:324-333.
    • (2005) Mol. Plant-Microbe Interact. , vol.18 , pp. 324-333
    • Lu, S.E.1    Wang, N.2    Wang, J.L.3    Chen, Z.J.4    Gross, D.C.5
  • 43
    • 0037630396 scopus 로고    scopus 로고
    • Mutational analysis of TraR. Correlating function with molecular structure of a quorum-sensing transcriptional activator
    • Luo, Z. Q., A. J. Smyth, P. Gao, Y. P. Qin, and S. K. Farrand. 2003. Mutational analysis of TraR. Correlating function with molecular structure of a quorum-sensing transcriptional activator. J. Biol. Chem. 278:13173-13182.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13173-13182
    • Luo, Z.Q.1    Smyth, A.J.2    Gao, P.3    Qin, Y.P.4    Farrand, S.K.5
  • 44
    • 0028826326 scopus 로고
    • Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: Characterization of a novel ferrisiderophore permease of the ABC transporter family
    • Mahé, B., C. Masclaux, L. Rauscher, C. Enard, and D. Expert. 1995. Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family. Mol. Microbiol. 18:33-43.
    • (1995) Mol. Microbiol. , vol.18 , pp. 33-43
    • Mahé, B.1    Masclaux, C.2    Rauscher, L.3    Enard, C.4    Expert, D.5
  • 46
    • 0028343505 scopus 로고
    • A mutation in the indole-3-acetic acid biosynthesis pathway of Pseudomonas syringae pv. syringae affects growth in Phaseolus vulgaris and syringomycin production
    • Mazzola, M., and F. F. White. 1994. A mutation in the indole-3-acetic acid biosynthesis pathway of Pseudomonas syringae pv. syringae affects growth in Phaseolus vulgaris and syringomycin production. J. Bacteriol. 176:1374-1382.
    • (1994) J. Bacteriol. , vol.176 , pp. 1374-1382
    • Mazzola, M.1    White, F.F.2
  • 47
    • 0030591786 scopus 로고    scopus 로고
    • Characterization of the pvdE gene which is required for pyoverdine synthesis in Pseudomonas aeruginosa
    • McMorran, B. J., M. E. Merriman, I. T. Rombel, and I. L. Lamont. 1996. Characterization of the pvdE gene which is required for pyoverdine synthesis in Pseudomonas aeruginosa. Gene 176:55-59.
    • (1996) Gene , vol.176 , pp. 55-59
    • McMorran, B.J.1    Merriman, M.E.2    Rombel, I.T.3    Lamont, I.L.4
  • 48
    • 0025940781 scopus 로고
    • Plant signal molecules activate the syrB gene, which is required for syringomycin production by Pseudomonas syringae pv. syringae
    • Mo, Y. Y., and D. C. Gross. 1991. Plant signal molecules activate the syrB gene, which is required for syringomycin production by Pseudomonas syringae pv. syringae. J. Bacteriol. 173:5784-5792.
    • (1991) J. Bacteriol. , vol.173 , pp. 5784-5792
    • Mo, Y.Y.1    Gross, D.C.2
  • 52
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 53
    • 0027412028 scopus 로고
    • Conjugation factor of Agrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction
    • Piper, K. R., S. B. von Bodman, and S. K. Farrand. 1993. Conjugation factor of Agrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction. Nature 362:448-450.
    • (1993) Nature , vol.362 , pp. 448-450
    • Piper, K.R.1    Von Bodman, S.B.2    Farrand, S.K.3
  • 54
    • 0019841516 scopus 로고
    • The plasmid cloning vector pBR325 contains a 482 base-pair-long inverted duplication
    • Prentki, P., F. Karch, S. Iida, and J. Meyer. 1981. The plasmid cloning vector pBR325 contains a 482 base-pair-long inverted duplication. Gene 14:289-299.
    • (1981) Gene , vol.14 , pp. 289-299
    • Prentki, P.1    Karch, F.2    Iida, S.3    Meyer, J.4
  • 55
    • 0030671073 scopus 로고    scopus 로고
    • A quorum-sensing system in the free-living photosynthetic bacterium Rhodobacter sphaeroides
    • Puskas, A., E. P. Greenberg, S. Kaplan, and A. L. Schaeffer. 1997. A quorum-sensing system in the free-living photosynthetic bacterium Rhodobacter sphaeroides. J. Bacteriol. 179:7530-7537.
    • (1997) J. Bacteriol. , vol.179 , pp. 7530-7537
    • Puskas, A.1    Greenberg, E.P.2    Kaplan, S.3    Schaeffer, A.L.4
  • 56
    • 0034596996 scopus 로고    scopus 로고
    • Quorum-sensing signal binding results in dimerization of TraR and its release from membranes into the cytoplasm
    • Qin, Y. P., Z. Q. Luo, A. J. Smyth, P. Gao, S. B. von Bodman, and S. K. Farrand. 2000. Quorum-sensing signal binding results in dimerization of TraR and its release from membranes into the cytoplasm. EMBO J. 19:5212-5221.
    • (2000) EMBO J. , vol.19 , pp. 5212-5221
    • Qin, Y.P.1    Luo, Z.Q.2    Smyth, A.J.3    Gao, P.4    Von Bodman, S.B.5    Farrand, S.K.6
  • 57
    • 0027209206 scopus 로고
    • SyrD is required for syringomycin production by Pseudomonas syringae pathovar syringae and is related to a family of ATP-binding secretion proteins
    • Quigley, N. B., Y. Y. Mo, and D. C. Gross. 1993. SyrD is required for syringomycin production by Pseudomonas syringae pathovar syringae and is related to a family of ATP-binding secretion proteins. Mol. Microbiol. 9:787-801.
    • (1993) Mol. Microbiol. , vol.9 , pp. 787-801
    • Quigley, N.B.1    Mo, Y.Y.2    Gross, D.C.3
  • 58
    • 0043062687 scopus 로고    scopus 로고
    • In vivo and in vitro evidence that TtgV is the specific regulator of the TtgGHI multidrug and solvent efflux pump of Pseudomonas putida
    • Rojas, A., A. Segura, M. E. Guazzaroni, W. Teran, A. Hurtado, M. T. Gallegos, and J. L. Ramos. 2003. In vivo and in vitro evidence that TtgV is the specific regulator of the TtgGHI multidrug and solvent efflux pump of Pseudomonas putida. J. Bacteriol. 185:4755-4763.
    • (2003) J. Bacteriol. , vol.185 , pp. 4755-4763
    • Rojas, A.1    Segura, A.2    Guazzaroni, M.E.3    Teran, W.4    Hurtado, A.5    Gallegos, M.T.6    Ramos, J.L.7
  • 59
    • 0028058238 scopus 로고
    • Extracellular protease and phospholipase C are controlled by the global regulatory gene gacA in the biocontrol strain Pseudomonas fluorescens CHA0
    • Sacherer, P., G. Défago, and D. Haas. 1994. Extracellular protease and phospholipase C are controlled by the global regulatory gene gacA in the biocontrol strain Pseudomonas fluorescens CHA0. FEMS Microbiol. Lett. 116:155-160.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 155-160
    • Sacherer, P.1    Défago, G.2    Haas, D.3
  • 61
    • 0035114743 scopus 로고    scopus 로고
    • The contribution of syringopeptin and syringomycin to virulence of Pseudomonas syringae pv. syringae strain B301D on the basis of sypA and syrB1 biosynthesis mutant analysis
    • Scholz-Schroeder, B. K., M. L. Hutchison, I. Grgurina, and D. C. Gross. 2001. The contribution of syringopeptin and syringomycin to virulence of Pseudomonas syringae pv. syringae strain B301D on the basis of sypA and syrB1 biosynthesis mutant analysis. Mol. Plant-Microbe Interact. 14:336-348.
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 336-348
    • Scholz-Schroeder, B.K.1    Hutchison, M.L.2    Grgurina, I.3    Gross, D.C.4
  • 62
    • 0037384426 scopus 로고    scopus 로고
    • The sypA, sypB and sypC synthetase genes encode twenty-two modules involved in the non-ribosomal peptide synthesis of syringopeptin by Pseudomonas syringae pv. syringae B301D
    • Scholz-Schroeder, B. K., J. D. Soule, and D. C. Gross. 2003. The sypA, sypB and sypC synthetase genes encode twenty-two modules involved in the non-ribosomal peptide synthesis of syringopeptin by Pseudomonas syringae pv. syringae B301D. Mol. Plant-Microbe Interact. 16:271-280.
    • (2003) Mol. Plant-Microbe Interact. , vol.16 , pp. 271-280
    • Scholz-Schroeder, B.K.1    Soule, J.D.2    Gross, D.C.3
  • 63
    • 0032563288 scopus 로고    scopus 로고
    • LSF and NTF-1 share a conserved DNA recognition motif yet require different oligomerization states to form a stable protein-DNA complex
    • Shirra, M. K., and U. Hansen. 1998. LSF and NTF-1 share a conserved DNA recognition motif yet require different oligomerization states to form a stable protein-DNA complex. J. Biol. Chem. 273:19260-19268.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19260-19268
    • Shirra, M.K.1    Hansen, U.2
  • 64
    • 0025864712 scopus 로고
    • Cloning and analysis of the gene (rpoDA) for the principal sigma factor of Pseudomonas aeruginosa
    • Tanaka, K., and H. Takahashi. 1991. Cloning and analysis of the gene (rpoDA) for the principal sigma factor of Pseudomonas aeruginosa. Biochim. Biophys. Acta 1089:113-119.
    • (1991) Biochim. Biophys. Acta , vol.1089 , pp. 113-119
    • Tanaka, K.1    Takahashi, H.2
  • 65
    • 1642581508 scopus 로고    scopus 로고
    • Reversible acyl-homoserine lactone binding to purified Vibrio fischeri LuxR protein
    • Urbanowski, A. L., C. P. Lostroh, and E. P. Greenberg. 2004. Reversible acyl-homoserine lactone binding to purified Vibrio fischeri LuxR protein. J. Bacteriol. 186:631-637.
    • (2004) J. Bacteriol. , vol.186 , pp. 631-637
    • Urbanowski, A.L.1    Lostroh, C.P.2    Greenberg, E.P.3
  • 66
    • 0001191014 scopus 로고
    • Synthetic and complex media for rapid detection of fluorescence of phytopathogenic pseudomonads: Effect of carbon source
    • Vidaver, A. K. 1967. Synthetic and complex media for rapid detection of fluorescence of phytopathogenic pseudomonads: effect of carbon source. Appl. Microbiol. 15:1523-1524.
    • (1967) Appl. Microbiol. , vol.15 , pp. 1523-1524
    • Vidaver, A.K.1
  • 67
    • 0029154127 scopus 로고
    • Capsular polysaccharide biosynthesis and pathogenicity in Erwinia stewartii require induction by an N-acylhomoserine lactone autoinducer
    • von Bodman, S. B., and S. K. Farrand. 1995. Capsular polysaccharide biosynthesis and pathogenicity in Erwinia stewartii require induction by an N-acylhomoserine lactone autoinducer. J. Bacteriol. 177:5000-5008.
    • (1995) J. Bacteriol. , vol.177 , pp. 5000-5008
    • Von Bodman, S.B.1    Farrand, S.K.2
  • 68
    • 33144485226 scopus 로고    scopus 로고
    • The expression of genes encoding lipodepsipeptide phytotoxins by Pseudomonas syringae pv. syringae is coordinated in response to plant signal molecules
    • Wang, N., S.-E. Lu, J. L. Wang, Z. J. Chen, and D. C. Gross. 2006. The expression of genes encoding lipodepsipeptide phytotoxins by Pseudomonas syringae pv. syringae is coordinated in response to plant signal molecules. Mol. Plant-Microbe Interact. 19:257-269.
    • (2006) Mol. Plant-Microbe Interact. , vol.19 , pp. 257-269
    • Wang, N.1    Lu, S.-E.2    Wang, J.L.3    Chen, Z.J.4    Gross, D.C.5
  • 69
    • 33144484253 scopus 로고    scopus 로고
    • Identification of the syr-syp box in the promoter regions of genes dedicated to syringomycin and syringopeptin production by Pseudomonas syringae pv. syringae B301D
    • Wang, N., S.-E. Lu, Q. Yang, S.-H. Sze, and D. C. Gross. 2006. Identification of the syr-syp box in the promoter regions of genes dedicated to syringomycin and syringopeptin production by Pseudomonas syringae pv. syringae B301D. J. Bacteriol. 188:160-168.
    • (2006) J. Bacteriol. , vol.188 , pp. 160-168
    • Wang, N.1    Lu, S.-E.2    Yang, Q.3    Sze, S.-H.4    Gross, D.C.5
  • 70
    • 0034651527 scopus 로고    scopus 로고
    • N-acyl homoserine lactone binding to the CarR receptor determines quorum-sensing specificity in Erwinia
    • Welch, M., D. E. Todd, N. A. Whitehead, S. J. McGowan, B. W. Bycroft, and G. P. C. Salmond. 2000. N-acyl homoserine lactone binding to the CarR receptor determines quorum-sensing specificity in Erwinia. EMBO J. 19:631-641.
    • (2000) EMBO J. , vol.19 , pp. 631-641
    • Welch, M.1    Todd, D.E.2    Whitehead, N.A.3    McGowan, S.J.4    Bycroft, B.W.5    Salmond, G.P.C.6
  • 71
    • 0028172499 scopus 로고
    • Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa
    • West, S. E. H., H. P. Schweizer, C. Dall, A. K. Sample, and L. J. Runyen-Janecky. 1994. Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa. Gene 148:81-86.
    • (1994) Gene , vol.148 , pp. 81-86
    • West, S.E.H.1    Schweizer, H.P.2    Dall, C.3    Sample, A.K.4    Runyen-Janecky, L.J.5
  • 72
    • 0029047970 scopus 로고
    • Analysis of the syrB and syrC genes of Pseudomonas syringae pv. syringae indicates that syringomycin is synthesized by a thiotemplate mechanism
    • Zhang, J. H., N. B. Quigley, and D. C. Gross. 1995. Analysis of the syrB and syrC genes of Pseudomonas syringae pv. syringae indicates that syringomycin is synthesized by a thiotemplate mechanism. J. Bacteriol. 177:4009-4020.
    • (1995) J. Bacteriol. , vol.177 , pp. 4009-4020
    • Zhang, J.H.1    Quigley, N.B.2    Gross, D.C.3
  • 73
    • 0030796661 scopus 로고    scopus 로고
    • Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae
    • Zhang, J. H., N. B. Quigley, and D. C. Gross. 1997. Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae. Appl. Environ. Microbiol. 63:2771-2778.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2771-2778
    • Zhang, J.H.1    Quigley, N.B.2    Gross, D.C.3
  • 74
    • 0346034963 scopus 로고    scopus 로고
    • Phosphorylation triggers domain separation in the DNA binding response regulator NarL
    • Zhang, J. H., G. P. Xiao, R. P. Gunsalus, and W. L. Hubbell. 2003. Phosphorylation triggers domain separation in the DNA binding response regulator NarL. Biochemistry 42:2552-2559.
    • (2003) Biochemistry , vol.42 , pp. 2552-2559
    • Zhang, J.H.1    Xiao, G.P.2    Gunsalus, R.P.3    Hubbell, W.L.4
  • 75
    • 1942538336 scopus 로고    scopus 로고
    • Pc operon from the highly mutable strain Pseudomonas cichorii 302959
    • Pc operon from the highly mutable strain Pseudomonas cichorii 302959. Can. J. Microbiol. 50:29-39.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 29-39
    • Zhang, S.1    Sundin, G.W.2
  • 76
    • 0031963471 scopus 로고    scopus 로고
    • Activity of the quorum-sensing regulator TraR of Agrobacterium tumefaciens is inhibited by a truncated, dominant defective TraR-like protein
    • Zhu, J., and S. C. Winans. 1998. Activity of the quorum-sensing regulator TraR of Agrobacterium tumefaciens is inhibited by a truncated, dominant defective TraR-like protein. Mol. Microbiol. 27:289-297.
    • (1998) Mol. Microbiol. , vol.27 , pp. 289-297
    • Zhu, J.1    Winans, S.C.2
  • 77
    • 0033609151 scopus 로고    scopus 로고
    • Autoinducer binding by the quorum-sensing regulator TraR increases affinity for target promoters in vitro and decreases TraR turnover rates in whole cells
    • Zhu, J., and S. C. Winans. 1999. Autoinducer binding by the quorum-sensing regulator TraR increases affinity for target promoters in vitro and decreases TraR turnover rates in whole cells. Proc. Natl. Acad. Sci. USA 96:4832-4837.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4832-4837
    • Zhu, J.1    Winans, S.C.2
  • 78
    • 0035852714 scopus 로고    scopus 로고
    • The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization
    • Zhu, J., and S. C. Winans. 2001. The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization. Proc. Natl. Acad. Sci. USA 98:1507-1512.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1507-1512
    • Zhu, J.1    Winans, S.C.2


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