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Volumn 7, Issue 12, 2012, Pages 2036-2045

An ABC transporter with two periplasmic binding proteins involved in iron acquisition in pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; FPVC PROTEIN; FPVF PROTEIN; IRON; PERIPLASMIC BINDING PROTEIN; PYOVERDINE; SIDEROPHORE; UNCLASSIFIED DRUG;

EID: 84871564039     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300330v     Document Type: Article
Times cited : (49)

References (52)
  • 2
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • Hider, R. C. and Kong, X. (2011) Chemistry and biology of siderophores Nat. Prod. Rep. 27, 637-657
    • (2011) Nat. Prod. Rep. , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 3
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. and Dover, L. G. (2000) Iron metabolism in pathogenic bacteria Annu. Rev. Microbiol. 54, 881-941
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 4
    • 42549136915 scopus 로고    scopus 로고
    • Siderotyping of fluorescent Pseudomonas: Molecular mass determination by mass spectrometry as a powerful pyoverdine siderotyping method
    • Meyer, J. M., Gruffaz, C., Raharinosy, V., Bezverbnaya, I., Schafer, M., and Budzikiewicz, H. (2008) Siderotyping of fluorescent Pseudomonas: molecular mass determination by mass spectrometry as a powerful pyoverdine siderotyping method Biometals 21, 259-271
    • (2008) Biometals , vol.21 , pp. 259-271
    • Meyer, J.M.1    Gruffaz, C.2    Raharinosy, V.3    Bezverbnaya, I.4    Schafer, M.5    Budzikiewicz, H.6
  • 5
    • 0000933886 scopus 로고
    • Bacterial siderophores: Structure and NMR assigment of pyoverdins PaA, siderophores of Pseudomonas aeruginosa ATCC 15692
    • Demange, P., Wendenbaum, S., Linget, C., Mertz, C., Cung, M. T., Dell, A., and Abdallah, M. A. (1990) Bacterial siderophores: structure and NMR assigment of pyoverdins PaA, siderophores of Pseudomonas aeruginosa ATCC 15692 Biol. Metals 3, 155-170
    • (1990) Biol. Metals , vol.3 , pp. 155-170
    • Demange, P.1    Wendenbaum, S.2    Linget, C.3    Mertz, C.4    Cung, M.T.5    Dell, A.6    Abdallah, M.A.7
  • 6
    • 0346636767 scopus 로고    scopus 로고
    • Iron acquisition and its control in Pseudomonas aeruginosa: Many roads lead to Rome
    • Poole, K. and McKay, G. A. (2003) Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome Front. Biosci. 8, d661-686
    • (2003) Front. Biosci. , vol.8 , pp. 661-686
    • Poole, K.1    McKay, G.A.2
  • 7
    • 35948949060 scopus 로고    scopus 로고
    • A β-strand lock-exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif
    • Brillet, K., Journet, L., Celia, H., Paulus, L., Stahl, A., Pattus, F., and Cobessi, D. (2007) A β-strand lock-exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif Structure 15, 1383-1391
    • (2007) Structure , vol.15 , pp. 1383-1391
    • Brillet, K.1    Journet, L.2    Celia, H.3    Paulus, L.4    Stahl, A.5    Pattus, F.6    Cobessi, D.7
  • 8
    • 33947600827 scopus 로고    scopus 로고
    • From the periplasmic signaling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: Crystal structure of the ferric pyoverdine outer membrane receptor
    • Wirth, C., Meyer-Klaucke, W., Pattus, F., and Cobessi, D. (2007) From the periplasmic signaling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: crystal structure of the ferric pyoverdine outer membrane receptor J. Mol. Biol. 68, 398-406
    • (2007) J. Mol. Biol. , vol.68 , pp. 398-406
    • Wirth, C.1    Meyer-Klaucke, W.2    Pattus, F.3    Cobessi, D.4
  • 9
    • 67651247345 scopus 로고    scopus 로고
    • Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa
    • Schalk, I. J., Lamont, I. L., and Cobessi, D. (2009) Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa Biometals 22, 671-678
    • (2009) Biometals , vol.22 , pp. 671-678
    • Schalk, I.J.1    Lamont, I.L.2    Cobessi, D.3
  • 10
    • 33748657558 scopus 로고    scopus 로고
    • Interaction of TonB with outer membrane receptor FpvA of Pseudomonas aeruginosa
    • Adams, H., Zeder-Lutz, G., Greenwald, J., Schalk, I. J., Célia, H., and Pattus, F. (2006) Interaction of TonB with outer membrane receptor FpvA of Pseudomonas aeruginosa J. Bacteriol. 188, 5752-5761
    • (2006) J. Bacteriol. , vol.188 , pp. 5752-5761
    • Adams, H.1    Zeder-Lutz, G.2    Greenwald, J.3    Schalk, I.J.4    Célia, H.5    Pattus, F.6
  • 11
    • 0036185882 scopus 로고    scopus 로고
    • Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa
    • Zhao, Q. and Poole, K. (2002) Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa J. Bacteriol. 184, 1503-1513
    • (2002) J. Bacteriol. , vol.184 , pp. 1503-1513
    • Zhao, Q.1    Poole, K.2
  • 12
    • 0343395846 scopus 로고    scopus 로고
    • ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
    • Koster, W. (2001) ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12 Res. Microbiol. 152, 291-301
    • (2001) Res. Microbiol. , vol.152 , pp. 291-301
    • Koster, W.1
  • 13
    • 2442485987 scopus 로고    scopus 로고
    • Identification of rhtX and fptX, novel genes encoding proteins that show homology and function in the utilization of the siderophores rhizobactin 1021 by Sinorhizobium meliloti and pyochelin by Pseudomonas aeruginosa, respectively
    • Cuiv, P. O., Clarke, P., Lynch, D., and O'Connell, M. (2004) Identification of rhtX and fptX, novel genes encoding proteins that show homology and function in the utilization of the siderophores rhizobactin 1021 by Sinorhizobium meliloti and pyochelin by Pseudomonas aeruginosa, respectively J. Bacteriol. 186, 2996-3005
    • (2004) J. Bacteriol. , vol.186 , pp. 2996-3005
    • Cuiv, P.O.1    Clarke, P.2    Lynch, D.3    O'Connell, M.4
  • 14
    • 77749270483 scopus 로고    scopus 로고
    • The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechansim with acylation of the siderophore and a recycling of the modified desferrichrome
    • Hannauer, M., Barda, Y., Mislin, G. L., Shanzer, A., and Schalk, I. J. (2010) The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechansim with acylation of the siderophore and a recycling of the modified desferrichrome J. Bacteriol. 192, 1212-1220
    • (2010) J. Bacteriol. , vol.192 , pp. 1212-1220
    • Hannauer, M.1    Barda, Y.2    Mislin, G.L.3    Shanzer, A.4    Schalk, I.J.5
  • 15
    • 0022998008 scopus 로고
    • Iron hydroxamate transport of Escherichia coli: Nucleotide sequence of the fhuB gene and identification of the protein
    • Koster, W. and Braun, V. (1986) Iron hydroxamate transport of Escherichia coli: nucleotide sequence of the fhuB gene and identification of the protein Mol. Gen. Genet. 204, 435-442
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 435-442
    • Koster, W.1    Braun, V.2
  • 16
    • 0024675811 scopus 로고
    • Iron-hydroxamate transport into Escherichia coli K12: Localization of FhuD in the periplasm and of FhuB in the cytoplasmic membrane
    • Koster, W. and Braun, V. (1989) Iron-hydroxamate transport into Escherichia coli K12: localization of FhuD in the periplasm and of FhuB in the cytoplasmic membrane Mol. Gen. Genet. 217, 233-239
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 233-239
    • Koster, W.1    Braun, V.2
  • 17
    • 34948822308 scopus 로고    scopus 로고
    • Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli
    • Braun, V. and Herrmann, C. (2007) Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli J. Bacteriol. 189, 6913-6918
    • (2007) J. Bacteriol. , vol.189 , pp. 6913-6918
    • Braun, V.1    Herrmann, C.2
  • 18
    • 0024549156 scopus 로고
    • Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli
    • Staudenmaier, H., Van Hove, B., Yaraghi, Z., and Braun, V. (1989) Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli J. Bacteriol. 171, 2626-2633
    • (1989) J. Bacteriol. , vol.171 , pp. 2626-2633
    • Staudenmaier, H.1    Van Hove, B.2    Yaraghi, Z.3    Braun, V.4
  • 19
    • 0025770263 scopus 로고
    • Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease
    • Chenault, S. S. and Earhart, C. F. (1991) Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease Mol. Microbiol. 5, 1405-1413
    • (1991) Mol. Microbiol. , vol.5 , pp. 1405-1413
    • Chenault, S.S.1    Earhart, C.F.2
  • 21
    • 0019306798 scopus 로고
    • Iron transport in Escherichia coli: Uptake and modification of ferrichrome
    • Hartman, A. and Braun, V. (1980) Iron transport in Escherichia coli: uptake and modification of ferrichrome J. Bacteriol. 143, 246-255
    • (1980) J. Bacteriol. , vol.143 , pp. 246-255
    • Hartman, A.1    Braun, V.2
  • 22
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • Brickman, T. J. and McIntosh, M. A. (1992) Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex J. Biol. Chem. 267, 12350-12355
    • (1992) J. Biol. Chem. , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    McIntosh, M.A.2
  • 23
    • 34047268399 scopus 로고    scopus 로고
    • Real-time FRET visualization of ferric-pyoverdine uptake in Pseudomonas aeruginosa: A role for ferrous iron
    • Greenwald, J., Hoegy, F., Nader, M., Journet, L., Mislin, G. L. A., Graumann, P. L., and Schalk, I. J. (2007) Real-time FRET visualization of ferric-pyoverdine uptake in Pseudomonas aeruginosa: a role for ferrous iron J. Biol. Chem. 282, 2987-2995
    • (2007) J. Biol. Chem. , vol.282 , pp. 2987-2995
    • Greenwald, J.1    Hoegy, F.2    Nader, M.3    Journet, L.4    Mislin, G.L.A.5    Graumann, P.L.6    Schalk, I.J.7
  • 24
    • 78649645704 scopus 로고    scopus 로고
    • An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa
    • Yeterian, E., Martin, L. W., Lamont, I. L., and Schalk, I. J. (2010) An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa Environ Microbiol Report 2, 412-418
    • (2010) Environ Microbiol Report , vol.2 , pp. 412-418
    • Yeterian, E.1    Martin, L.W.2    Lamont, I.L.3    Schalk, I.J.4
  • 25
    • 73949146114 scopus 로고    scopus 로고
    • Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa
    • Imperi, F., Tiburzi, F., and Visca, P. (2009) Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa Proc. Natl. Acad. Sci. U. S. A. 106, 20440-20445
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20440-20445
    • Imperi, F.1    Tiburzi, F.2    Visca, P.3
  • 26
    • 0037022174 scopus 로고    scopus 로고
    • Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa
    • Schalk, I. J., Abdallah, M. A., and Pattus, F. (2002) Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa Biochemistry 41, 1663-1671
    • (2002) Biochemistry , vol.41 , pp. 1663-1671
    • Schalk, I.J.1    Abdallah, M.A.2    Pattus, F.3
  • 27
    • 0038689220 scopus 로고    scopus 로고
    • Genomics of pyoverdine-mediated iron uptake in pseudomonads
    • Ravel, J. and Cornelis, P. (2003) Genomics of pyoverdine-mediated iron uptake in pseudomonads Trends Microbiol. 11, 195-200
    • (2003) Trends Microbiol. , vol.11 , pp. 195-200
    • Ravel, J.1    Cornelis, P.2
  • 29
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner, U., Snyder, A., Vasil, A. I., and Vasil, M. L. (2002) Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis Proc. Natl. Acad. Sci. U.S.A. 99, 8312-8317
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8312-8317
    • Ochsner, U.1    Snyder, A.2    Vasil, A.I.3    Vasil, M.L.4
  • 30
    • 0035982906 scopus 로고    scopus 로고
    • GeneChip expression analysis of the iron starvation response in Pseudomonas aeruginosa: Identification of novel pyoverdine biosynthesis genes
    • Ochsner, U. A., Wilderman, P. J., Vasil, A. I., and Vasil, M. L. (2002) GeneChip expression analysis of the iron starvation response in Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis genes Mol. Microbiol. 45, 1277-1287
    • (2002) Mol. Microbiol. , vol.45 , pp. 1277-1287
    • Ochsner, U.A.1    Wilderman, P.J.2    Vasil, A.I.3    Vasil, M.L.4
  • 31
    • 33644777983 scopus 로고    scopus 로고
    • The heterologous siderophores ferrioxamine B and ferrichrome activate signaling pathways in Pseudomonas aeruginosa
    • Llamas, M. A., Sparrius, M., Kloet, R., Jimenez, C. R., Vandenbroucke-Grauls, C., and Bitter, W. (2006) The heterologous siderophores ferrioxamine B and ferrichrome activate signaling pathways in Pseudomonas aeruginosa J. Bacteriol. 188, 1882-1891
    • (2006) J. Bacteriol. , vol.188 , pp. 1882-1891
    • Llamas, M.A.1    Sparrius, M.2    Kloet, R.3    Jimenez, C.R.4    Vandenbroucke-Grauls, C.5    Bitter, W.6
  • 35
    • 78651359481 scopus 로고    scopus 로고
    • A structural and functional analysis of type III periplasmic and substrate binding proteins: Their role in bacterial siderophore and heme transport
    • Chu, B. C. and Vogel, H. J. (2011) A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport Biol. Chem. 392, 39-52
    • (2011) Biol. Chem. , vol.392 , pp. 39-52
    • Chu, B.C.1    Vogel, H.J.2
  • 36
    • 2942748428 scopus 로고    scopus 로고
    • The binding mechanism of pyoverdin with the outer membrane receptor FpvA in Pseudomonas aeruginosa is dependent on its iron-loaded status
    • Clément, E., Mesini, P. J., Pattus, F., Abdallah, M. A., and Schalk, I. J. (2004) The binding mechanism of pyoverdin with the outer membrane receptor FpvA in Pseudomonas aeruginosa is dependent on its iron-loaded status Biochemistry 43, 7954-7965
    • (2004) Biochemistry , vol.43 , pp. 7954-7965
    • Clément, E.1    Mesini, P.J.2    Pattus, F.3    Abdallah, M.A.4    Schalk, I.J.5
  • 37
    • 2242464843 scopus 로고    scopus 로고
    • The interaction between pyoverdin and its outer membrane receptor in Pseudomonas aeruginosa leads to different conformers: A time-resolved fluorescence study
    • Folschweiller, N., Gallay, J., Vincent, M., Abdallah, M. A., Pattus, F., and Schalk, I. J. (2002) The interaction between pyoverdin and its outer membrane receptor in Pseudomonas aeruginosa leads to different conformers: a time-resolved fluorescence study Biochemistry 41, 14591-14601
    • (2002) Biochemistry , vol.41 , pp. 14591-14601
    • Folschweiller, N.1    Gallay, J.2    Vincent, M.3    Abdallah, M.A.4    Pattus, F.5    Schalk, I.J.6
  • 38
    • 0033587572 scopus 로고    scopus 로고
    • Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: Implications for siderophore-mediated iron transport
    • Schalk, I. J., Kyslik, P., Prome, D., van Dorsselaer, A., Poole, K., Abdallah, M. A., and Pattus, F. (1999) Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: implications for siderophore-mediated iron transport Biochemistry 38, 9357-9365
    • (1999) Biochemistry , vol.38 , pp. 9357-9365
    • Schalk, I.J.1    Kyslik, P.2    Prome, D.3    Van Dorsselaer, A.4    Poole, K.5    Abdallah, M.A.6    Pattus, F.7
  • 39
    • 0031968794 scopus 로고    scopus 로고
    • Fluorescent pseudomonad pyoverdines bind and oxidize ferrous ion
    • Xiao, R. and Kisaalita, W. S. (1998) Fluorescent pseudomonad pyoverdines bind and oxidize ferrous ion Appl. Environ. Microbiol. 64, 1472-1476
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1472-1476
    • Xiao, R.1    Kisaalita, W.S.2
  • 40
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J. A. (1997) Studying noncovalent protein complexes by electrospray ionization mass spectrometry Mass Spectrom. Rev. 16, 1-23
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 41
    • 80055065227 scopus 로고    scopus 로고
    • New roles for bacterial siderophores in metal transport and tolerance
    • Schalk, I. J., Hannauer, M., and Braud, A. (2011) New roles for bacterial siderophores in metal transport and tolerance Environ. Microbiol. 13, 2844-2854
    • (2011) Environ. Microbiol. , vol.13 , pp. 2844-2854
    • Schalk, I.J.1    Hannauer, M.2    Braud, A.3
  • 42
    • 0017125955 scopus 로고
    • Mechanisms of siderophore iron transport in enteric bacteria
    • Leong, J. and Neilands, J. B. (1976) Mechanisms of siderophore iron transport in enteric bacteria J. Bacteriol. 126, 823-830
    • (1976) J. Bacteriol. , vol.126 , pp. 823-830
    • Leong, J.1    Neilands, J.B.2
  • 43
    • 0000052762 scopus 로고
    • Bacterial iron transport: Coordination properties of pyoverdin PaA, a peptidic siderophore of Pseudomonas aeruginosa
    • Albrecht-Gary, A. M., Blanc, S., Rochel, N., Ocacktan, A. Z., and Abdallah, M. A. (1994) Bacterial iron transport: coordination properties of pyoverdin PaA, a peptidic siderophore of Pseudomonas aeruginosa Inorg. Chem. 33, 6391-6402
    • (1994) Inorg. Chem. , vol.33 , pp. 6391-6402
    • Albrecht-Gary, A.M.1    Blanc, S.2    Rochel, N.3    Ocacktan, A.Z.4    Abdallah, M.A.5
  • 44
    • 0035151056 scopus 로고    scopus 로고
    • Iron-free pyoverdin binds to its outer membrane receptor FpvA in Pseudomonas aeruginosa: A new mechanism for membrane iron transport
    • Schalk, I. J., Hennard, C., Dugave, C., Poole, K., Abdallah, M. A., and Pattus, F. (2001) Iron-free pyoverdin binds to its outer membrane receptor FpvA in Pseudomonas aeruginosa: a new mechanism for membrane iron transport Mol. Microbiol. 39, 351-360
    • (2001) Mol. Microbiol. , vol.39 , pp. 351-360
    • Schalk, I.J.1    Hennard, C.2    Dugave, C.3    Poole, K.4    Abdallah, M.A.5    Pattus, F.6
  • 45
    • 79953183933 scopus 로고    scopus 로고
    • Mechanism of ferrisiderophore uptake by Pseudomonas aeruginosa outer membrane transporter FpvA: No diffusion channel formed at any time during ferrisiderophore uptake
    • Nader, M., Journet, L., Meksem, A., Guillon, L., and Schalk, I. J. (2011) Mechanism of ferrisiderophore uptake by Pseudomonas aeruginosa outer membrane transporter FpvA: no diffusion channel formed at any time during ferrisiderophore uptake Biochemistry 50, 2530-2540
    • (2011) Biochemistry , vol.50 , pp. 2530-2540
    • Nader, M.1    Journet, L.2    Meksem, A.3    Guillon, L.4    Schalk, I.J.5
  • 47
    • 67649304833 scopus 로고    scopus 로고
    • Stereospecificity of the siderophore pyochelin outer membrane transporters in fluorescent Pseudomonads
    • Hoegy, F., Lee, X., Noël, S., Mislin, G. L., Rognan, D., Reimmann, C., and Schalk, I. J. (2009) Stereospecificity of the siderophore pyochelin outer membrane transporters in fluorescent Pseudomonads J. Biol. Chem. 284, 14949-14957
    • (2009) J. Biol. Chem. , vol.284 , pp. 14949-14957
    • Hoegy, F.1    Lee, X.2    Noël, S.3    Mislin, G.L.4    Rognan, D.5    Reimmann, C.6    Schalk, I.J.7
  • 48
    • 69949105383 scopus 로고    scopus 로고
    • Role of TonB1 in pyoverdine-mediated signaling in Pseudomonas aeruginosa
    • Shirley, M. and Lamont, I. L. (2009) Role of TonB1 in pyoverdine-mediated signaling in Pseudomonas aeruginosa J. Bacteriol. 191, 5634-5640
    • (2009) J. Bacteriol. , vol.191 , pp. 5634-5640
    • Shirley, M.1    Lamont, I.L.2
  • 49
    • 0026019764 scopus 로고
    • A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants
    • Morales, V. M., Backman, A., and Bagdasarian, M. (1991) A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants Gene 97, 39-47
    • (1991) Gene , vol.97 , pp. 39-47
    • Morales, V.M.1    Backman, A.2    Bagdasarian, M.3
  • 50
    • 84950280872 scopus 로고
    • Biocontrol of root diseases by Pseudomonas fluorescens CHAO: Current concepts and experimental approaches
    • (O'Gara, F. Dowling, D. N. and Boesten, B. Eds.), pp, VCH, Weinheim, Germany. - 89
    • Voisard, C., Bull, C., Keel, C., Laville, J., Maurhofer, M., Schnider, U., Défago, G., and Haas, D. (1994) Biocontrol of root diseases by Pseudomonas fluorescens CHAO: current concepts and experimental approaches, in Molecular Ecology of Rhizosphere Microorganisms (O'Gara, F., Dowling, D. N., and Boesten, B., Eds.), pp 67-89, VCH, Weinheim, Germany.
    • (1994) Molecular Ecology of Rhizosphere Microorganisms , pp. 67
    • Voisard, C.1    Bull, C.2    Keel, C.3    Laville, J.4    Maurhofer, M.5    Schnider, U.6    Défago, G.7    Haas, D.8
  • 51
    • 0033598832 scopus 로고    scopus 로고
    • Global GacA-steered control of cyanide and exoprotease production in Pseudomonas fluorescens involves specific ribosome binding sites
    • Blumer, C., Heeb, S., Pessi, G., and Haas, D. (1999) Global GacA-steered control of cyanide and exoprotease production in Pseudomonas fluorescens involves specific ribosome binding sites Proc. Natl. Acad. Sci. U.S.A. 96, 14073-14078
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14073-14078
    • Blumer, C.1    Heeb, S.2    Pessi, G.3    Haas, D.4


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