메뉴 건너뛰기




Volumn 157, Issue 9, 2011, Pages 2681-2693

The plant pathogen Streptomyces scabies 87-22 has a functional pyochelin biosynthetic pathway that is regulated by TetR- and AfsR-family proteins

Author keywords

[No Author keywords available]

Indexed keywords

DNA; IRON; PYOCHELIN; RNA; SIDEROPHORE; UNCLASSIFIED DRUG;

EID: 80052391212     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.047977-0     Document Type: Article
Times cited : (47)

References (72)
  • 1
    • 33645467335 scopus 로고    scopus 로고
    • Nur, a nickel-responsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor
    • Ahn, B.-E., Cha, J., Lee, E.-J., Han, A.-R., Thompson, C. J. & Roe, J.-H. (2006). Nur, a nickel-responsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor. Mol Microbiol 59, 1848-1858.
    • (2006) Mol Microbiol , vol.59 , pp. 1848-1858
    • Ahn, B.-E.1    Cha, J.2    Lee, E.-J.3    Han, A.-R.4    Thompson, C.J.5    Roe, J.-H.6
  • 2
    • 0021796364 scopus 로고
    • Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin
    • Ankenbauer, R., Sriyosachati, S. & Cox, C. D. (1985). Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin. Infect Immun 49, 132-140.
    • (1985) Infect Immun , vol.49 , pp. 132-140
    • Ankenbauer, R.1    Sriyosachati, S.2    Cox, C.D.3
  • 3
    • 11444260150 scopus 로고    scopus 로고
    • Identification of a cluster of genes that directs desferrioxamine biosynthesis in Streptomyces coelicolor M145
    • Barona-Gómez, F., Wong, U., Giannakopulos, A. E., Derrick, P. J. & Challis, G. L. (2004). Identification of a cluster of genes that directs desferrioxamine biosynthesis in Streptomyces coelicolor M145. J Am Chem Soc 126, 16282-16283.
    • (2004) J Am Chem Soc , vol.126 , pp. 16282-16283
    • Barona-Gómez, F.1    Wong, U.2    Giannakopulos, A.E.3    Derrick, P.J.4    Challis, G.L.5
  • 4
    • 33750963795 scopus 로고    scopus 로고
    • Multiple biosynthetic and uptake systems mediate siderophore-dependent iron acquisition in Streptomyces coelicolor A3(2) and Streptomyces ambofaciens ATCC 23877
    • Barona-Gómez, F., Lautru, S., Francou, F.-X., Leblond, P., Pernodet, J.-L. & Challis, G. L. (2006). Multiple biosynthetic and uptake systems mediate siderophore-dependent iron acquisition in Streptomyces coelicolor A3(2) and Streptomyces ambofaciens ATCC 23877. Microbiology 152, 3355-3366.
    • (2006) Microbiology , vol.152 , pp. 3355-3366
    • Barona-Gómez, F.1    Lautru, S.2    Francou, F.-X.3    Leblond, P.4    Pernodet, J.-L.5    Challis, G.L.6
  • 6
    • 0028079724 scopus 로고
    • The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site
    • Bibb, M. J., White, J., Ward, J. M. & Janssen, G. R. (1994). The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site. Mol Microbiol 14, 533-545.
    • (1994) Mol Microbiol , vol.14 , pp. 533-545
    • Bibb, M.J.1    White, J.2    Ward, J.M.3    Janssen, G.R.4
  • 8
    • 16244415184 scopus 로고    scopus 로고
    • Expression of ccaR, encoding the positive activator of cephamycin C and clavulanic acid production in Streptomyces clavuligerus, is dependent on bldG
    • Bignell, D. R. D., Tahlan, K., Colvin, K. R., Jensen, S. E. & Leskiw, B. K. (2005). Expression of ccaR, encoding the positive activator of cephamycin C and clavulanic acid production in Streptomyces clavuligerus, is dependent on bldG. Antimicrob Agents Chemother 49, 1529-1541.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1529-1541
    • Bignell, D.R.D.1    Tahlan, K.2    Colvin, K.R.3    Jensen, S.E.4    Leskiw, B.K.5
  • 10
    • 75749150917 scopus 로고    scopus 로고
    • Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic cluster that contributes to plantmicrobe interactions
    • Bignell, D. R. D., Seipke, R. F., Huguet-Tapia, J. C., Chambers, A. H., Parry, R. J. & Loria, R. (2010b). Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic cluster that contributes to plantmicrobe interactions. Mol Plant Microbe Interact 23, 161-175.
    • (2010) Mol Plant Microbe Interact , vol.23 , pp. 161-175
    • Bignell, D.R.D.1    Seipke, R.F.2    Huguet-Tapia, J.C.3    Chambers, A.H.4    Parry, R.J.5    Loria, R.6
  • 11
    • 0030933283 scopus 로고    scopus 로고
    • Probing of Pseudomonas aeruginosa, Pseudomonas aureofaciens, Burkholderia (Pseudomonas) cepacia, Pseudomonas fluorescens, and Pseudomonas putida with the ferripyochelin receptor A gene and the synthesis of pyochelin in Pseudomonas aureofaciens, Pseudomonas fluorescens, and Pseudomonas putida
    • Castignetti, D. (1997). Probing of Pseudomonas aeruginosa, Pseudomonas aureofaciens, Burkholderia (Pseudomonas) cepacia, Pseudomonas fluorescens, and Pseudomonas putida with the ferripyochelin receptor A gene and the synthesis of pyochelin in Pseudomonas aureofaciens, Pseudomonas fluorescens, and Pseudomonas putida. Curr Microbiol 34, 250-257.
    • (1997) Curr Microbiol , vol.34 , pp. 250-257
    • Castignetti, D.1
  • 12
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • Challis, G. L., Ravel, J. & Townsend, C. A. (2000). Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem Biol 7, 211-224.
    • (2000) Chem Biol , vol.7 , pp. 211-224
    • Challis, G.L.1    Ravel, J.2    Townsend, C.A.3
  • 13
    • 0020081797 scopus 로고
    • Effect of pyochelin on the virulence of Pseudomonas aeruginosa
    • Cox, C. D. (1982). Effect of pyochelin on the virulence of Pseudomonas aeruginosa. Infect Immun 36, 17-23.
    • (1982) Infect Immun , vol.36 , pp. 17-23
    • Cox, C.D.1
  • 14
    • 0019588236 scopus 로고
    • Pyochelin: Novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa
    • Cox, C. D., Rinehart, K. L., Jr, Moore, M. L. & Cook, J. C., Jr (1981). Pyochelin: novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa. Proc Natl Acad Sci U S A 78, 4256-4260.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4256-4260
    • Cox, C.D.1    Rinehart Jr., K.L.2    Moore, M.L.3    Cook Jr., J.C.4
  • 15
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97, 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 17
    • 0024026561 scopus 로고
    • Systemic virulence of Erwinia chrysanthemi 3937 requires a functional iron assimilation system
    • Enard, C., Diolez, A. & Expert, D. (1988). Systemic virulence of Erwinia chrysanthemi 3937 requires a functional iron assimilation system. J Bacteriol 170, 2419-2426.
    • (1988) J Bacteriol , vol.170 , pp. 2419-2426
    • Enard, C.1    Diolez, A.2    Expert, D.3
  • 18
    • 0035868495 scopus 로고    scopus 로고
    • Enterobactin: The characteristic catecholate siderophore of Enterobacteriaceae is produced by Streptomyces species.(1)
    • Fiedler, H.-P., Krastel, P., Müller, J., Gebhardt, K. & Zeeck, A. (2001). Enterobactin: the characteristic catecholate siderophore of Enterobacteriaceae is produced by Streptomyces species.(1). FEMS Microbiol Lett 196, 147-151.
    • (2001) FEMS Microbiol Lett , vol.196 , pp. 147-151
    • Fiedler, H.-P.1    Krastel, P.2    Müller, J.3    Gebhardt, K.4    Zeeck, A.5
  • 19
    • 2942707687 scopus 로고    scopus 로고
    • Iron-regulatory proteins DmdR1 and DmdR2 of Streptomyces coelicolor form two different DNA-protein complexes with iron boxes
    • Flores, F. J. & Martín, J. F. (2004). Iron-regulatory proteins DmdR1 and DmdR2 of Streptomyces coelicolor form two different DNA-protein complexes with iron boxes. Biochem J 380, 497-503.
    • (2004) Biochem J , vol.380 , pp. 497-503
    • Flores, F.J.1    Martín, J.F.2
  • 20
    • 2942525902 scopus 로고    scopus 로고
    • Characterization of the iron-regulated desA promoter of Streptomyces pilosus as a system for controlled gene expression in actinomycetes
    • Flores, F. J., Rincón, J. & Martín, J. F. (2003). Characterization of the iron-regulated desA promoter of Streptomyces pilosus as a system for controlled gene expression in actinomycetes. Microb Cell Fact 2, 5.
    • (2003) Microb Cell Fact , vol.2 , pp. 5
    • Flores, F.J.1    Rincón, J.2    Martín, J.F.3
  • 21
    • 13444293049 scopus 로고    scopus 로고
    • Functional analysis of two divalent metal-dependent regulatory genes dmdR1 and dmdR2 in Streptomyces coelicolor and proteome changes in deletion mutants
    • Flores, F. J., Barreiro, C., Coque, J. J. R. & Martín, J. F. (2005). Functional analysis of two divalent metal-dependent regulatory genes dmdR1 and dmdR2 in Streptomyces coelicolor and proteome changes in deletion mutants. FEBS J 272, 725-735.
    • (2005) FEBS J , vol.272 , pp. 725-735
    • Flores, F.J.1    Barreiro, C.2    Coque, J.J.R.3    Martín, J.F.4
  • 22
    • 0036831751 scopus 로고    scopus 로고
    • Coupling of iron assimilation and pectinolysis in Erwinia chrysanthemi 3937
    • Franza, T., Michaud-Soret, I., Piquerel, P. & Expert, D. (2002). Coupling of iron assimilation and pectinolysis in Erwinia chrysanthemi 3937. Mol Plant Microbe Interact 15, 1181-1191.
    • (2002) Mol Plant Microbe Interact , vol.15 , pp. 1181-1191
    • Franza, T.1    Michaud-Soret, I.2    Piquerel, P.3    Expert, D.4
  • 23
    • 0041888245 scopus 로고    scopus 로고
    • Integration site for Streptomyces phage phiBT1 and development of site-specific integrating vectors
    • Gregory, M. A., Till, R. & Smith, M. C. M. (2003). Integration site for Streptomyces phage phiBT1 and development of site-specific integrating vectors. J Bacteriol 185, 5320-5323.
    • (2003) J Bacteriol , vol.185 , pp. 5320-5323
    • Gregory, M.A.1    Till, R.2    Smith, M.C.M.3
  • 24
    • 0027945605 scopus 로고
    • Microbial iron transport
    • Guerinot, M. L. (1994). Microbial iron transport. Annu Rev Microbiol 48, 743-772.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 743-772
    • Guerinot, M.L.1
  • 25
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust, B., Challis, G. L., Fowler, K., Kieser, T. & Chater, K. F. (2003a). PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc Natl Acad Sci U S A 100, 1541-1546.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 27
    • 0034130524 scopus 로고    scopus 로고
    • Regulation of the furA and catC operon, encoding a ferric uptake regulator homologue and catalase-peroxidase, respectively, in Streptomyces coelicolor A3(2)
    • Hahn, J.-S., Oh, S.-Y. & Roe, J.-H. (2000a). Regulation of the furA and catC operon, encoding a ferric uptake regulator homologue and catalase-peroxidase, respectively, in Streptomyces coelicolor A3(2). J Bacteriol 182, 3767-3774.
    • (2000) J Bacteriol , vol.182 , pp. 3767-3774
    • Hahn, J.-S.1    Oh, S.-Y.2    Roe, J.-H.3
  • 28
    • 0034623713 scopus 로고    scopus 로고
    • 2-sensitive Fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor
    • 2-sensitive Fur-like repressor CatR regulating the major catalase gene in Streptomyces coelicolor. J Biol Chem 275, 38254-38260.
    • (2000) J Biol Chem , vol.275 , pp. 38254-38260
    • Hahn, J.-S.1    Oh, S.-Y.2    Chater, K.F.3    Cho, Y.-H.4    Roe, J.-H.5
  • 29
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke, K. (2001). Iron and metal regulation in bacteria. Curr Opin Microbiol 4, 172-177.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 172-177
    • Hantke, K.1
  • 30
    • 33749033361 scopus 로고    scopus 로고
    • The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase
    • Harrison, A. J., Yu, M., Gårdenborg, T., Middleditch, M., Ramsay, R. J., Baker, E. N. & Lott, J. S. (2006). The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J Bacteriol 188, 6081-6091.
    • (2006) J Bacteriol , vol.188 , pp. 6081-6091
    • Harrison, A.J.1    Yu, M.2    Gårdenborg, T.3    Middleditch, M.4    Ramsay, R.J.5    Baker, E.N.6    Lott, J.S.7
  • 31
    • 0027326482 scopus 로고
    • Cloning and sequence analysis of a gene (pchR) encoding an AraC family activator of pyochelin and ferripyochelin receptor synthesis in Pseudomonas aeruginosa
    • Heinrichs, D. E. & Poole, K. (1993). Cloning and sequence analysis of a gene (pchR) encoding an AraC family activator of pyochelin and ferripyochelin receptor synthesis in Pseudomonas aeruginosa. J Bacteriol 175, 5882-5889.
    • (1993) J Bacteriol , vol.175 , pp. 5882-5889
    • Heinrichs, D.E.1    Poole, K.2
  • 32
    • 0029914952 scopus 로고    scopus 로고
    • PchR, a regulator of ferripyochelin receptor gene (fptA) expression in Pseudomonas aeruginosa, functions both as an activator and as a repressor
    • Heinrichs, D. E. & Poole, K. (1996). PchR, a regulator of ferripyochelin receptor gene (fptA) expression in Pseudomonas aeruginosa, functions both as an activator and as a repressor. J Bacteriol 178, 2586-2592.
    • (1996) J Bacteriol , vol.178 , pp. 2586-2592
    • Heinrichs, D.E.1    Poole, K.2
  • 33
    • 16844374518 scopus 로고    scopus 로고
    • The role of the novel Fem protein VanK in vancomycin resistance in Streptomyces coelicolor
    • Hong, H.-J., Hutchings, M. I., Hill, L. M. & Buttner, M. J. (2005). The role of the novel Fem protein VanK in vancomycin resistance in Streptomyces coelicolor. J Biol Chem 280, 13055-13061.
    • (2005) J Biol Chem , vol.280 , pp. 13055-13061
    • Hong, H.-J.1    Hutchings, M.I.2    Hill, L.M.3    Buttner, M.J.4
  • 34
    • 0029013429 scopus 로고
    • Comparison of the main siderophores produced by some species of Streptomyces
    • Imbert, M., Bechet, M. & Blondeau, R. (1995). Comparison of the main siderophores produced by some species of Streptomyces. Curr Microbiol 31, 129-133.
    • (1995) Curr Microbiol , vol.31 , pp. 129-133
    • Imbert, M.1    Bechet, M.2    Blondeau, R.3
  • 35
    • 0035799154 scopus 로고    scopus 로고
    • Synthetic studies of thiazoline and thiazolidine-containing natural products. Part 3: Total synthesis and absolute configuration of the siderophore yersiniabactin
    • Ino, A. & Murabayashi, A. (2001). Synthetic studies of thiazoline and thiazolidine-containing natural products. Part 3: Total synthesis and absolute configuration of the siderophore yersiniabactin. Tetrahedron 57, 1897-1902.
    • (2001) Tetrahedron , vol.57 , pp. 1897-1902
    • Ino, A.1    Murabayashi, A.2
  • 36
    • 35448942799 scopus 로고    scopus 로고
    • The AraC/XylS regulator TxtR modulates thaxtomin biosynthesis and virulence in Streptomyces scabies
    • Joshi, M. V., Bignell, D. R. D., Johnson, E. G., Sparks, J. P., Gibson, D. M. & Loria, R. (2007). The AraC/XylS regulator TxtR modulates thaxtomin biosynthesis and virulence in Streptomyces scabies. Mol Microbiol 66, 633-642.
    • (2007) Mol Microbiol , vol.66 , pp. 633-642
    • Joshi, M.V.1    Bignell, D.R.D.2    Johnson, E.G.3    Sparks, J.P.4    Gibson, D.M.5    Loria, R.6
  • 37
    • 64249172679 scopus 로고    scopus 로고
    • Chapter 17. Siderophore biosynthesis a substrate specificity assay for nonribosomal peptide synthetase-independent siderophore synthetases involving trapping of acyl-adenylate intermediates with hydroxylamine
    • Kadi, N. & Challis, G. L. (2009). Chapter 17. Siderophore biosynthesis a substrate specificity assay for nonribosomal peptide synthetase-independent siderophore synthetases involving trapping of acyl-adenylate intermediates with hydroxylamine. Methods Enzymol 458, 431-457.
    • (2009) Methods Enzymol , vol.458 , pp. 431-457
    • Kadi, N.1    Challis, G.L.2
  • 38
    • 33344476803 scopus 로고    scopus 로고
    • Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate
    • Kerbarh, O., Chirgadze, D. Y., Blundell, T. L. & Abell, C. (2006). Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate. J Mol Biol 357, 524-534.
    • (2006) J Mol Biol , vol.357 , pp. 524-534
    • Kerbarh, O.1    Chirgadze, D.Y.2    Blundell, T.L.3    Abell, C.4
  • 41
    • 65549110653 scopus 로고    scopus 로고
    • Effect of iron concentration on the growth rate of Pseudomonas syringae and the expression of virulence factors in hrp-inducing minimal medium
    • Kim, B. J., Park, J. H., Park, T. H., Bronstein, P. A., Schneider, D. J., Cartinhour, S. W. & Shuler, M. L. (2009). Effect of iron concentration on the growth rate of Pseudomonas syringae and the expression of virulence factors in hrp-inducing minimal medium. Appl Environ Microbiol 75, 2720-2726.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2720-2726
    • Kim, B.J.1    Park, J.H.2    Park, T.H.3    Bronstein, P.A.4    Schneider, D.J.5    Cartinhour, S.W.6    Shuler, M.L.7
  • 42
    • 27544477567 scopus 로고    scopus 로고
    • Discovery of a new peptide natural product by Streptomyces coelicolor genome mining
    • Lautru, S., Deeth, R. J., Bailey, L. M. & Challis, G. L. (2005). Discovery of a new peptide natural product by Streptomyces coelicolor genome mining. Nat Chem Biol 1, 265-269.
    • (2005) Nat Chem Biol , vol.1 , pp. 265-269
    • Lautru, S.1    Deeth, R.J.2    Bailey, L.M.3    Challis, G.L.4
  • 43
    • 0026344181 scopus 로고
    • The use of a rare codon specifically during development?
    • Leskiw, B. K., Bibb, M. J. & Chater, K. F. (1991). The use of a rare codon specifically during development? Mol Microbiol 5, 2861-2867.
    • (1991) Mol Microbiol , vol.5 , pp. 2861-2867
    • Leskiw, B.K.1    Bibb, M.J.2    Chater, K.F.3
  • 44
    • 0028815845 scopus 로고
    • Differential production of thaxtomins by pathogenic Streptomyces species in vitro
    • Loria, R., Bukhalid, R. A., Creath, R. A., Leiner, R. H. & Oliver, M. (1995). Differential production of thaxtomins by pathogenic Streptomyces species in vitro. Phytopathology 85, 537-541.
    • (1995) Phytopathology , vol.85 , pp. 537-541
    • Loria, R.1    Bukhalid, R.A.2    Creath, R.A.3    Leiner, R.H.4    Oliver, M.5
  • 45
  • 46
    • 33748951425 scopus 로고    scopus 로고
    • Evolution of plant pathogenicity in Streptomyces
    • Loria, R., Kers, J. & Joshi, M. (2006). Evolution of plant pathogenicity in Streptomyces. Annu Rev Phytopathol 44, 469-487.
    • (2006) Annu Rev Phytopathol , vol.44 , pp. 469-487
    • Loria, R.1    Kers, J.2    Joshi, M.3
  • 48
    • 0026575735 scopus 로고
    • Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector
    • MacNeil, D. J., Gewain, K. M., Ruby, C. L., Dezeny, G., Gibbons, P. H. & MacNeil, T. (1992). Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector. Gene 111, 61-68.
    • (1992) Gene , vol.111 , pp. 61-68
    • McNeil, D.J.1    Gewain, K.M.2    Ruby, C.L.3    Dezeny, G.4    Gibbons, P.H.5    McNeil, T.6
  • 49
    • 26944468295 scopus 로고    scopus 로고
    • PchR-box recognition by the AraC-type regulator PchR of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector
    • Michel, L., González, N., Jagdeep, S., Nguyen-Ngoc, T. & Reimmann, C. (2005). PchR-box recognition by the AraC-type regulator PchR of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector. Mol Microbiol 58, 495-509.
    • (2005) Mol Microbiol , vol.58 , pp. 495-509
    • Michel, L.1    González, N.2    Jagdeep, S.3    Nguyen-Ngoc, T.4    Reimmann, C.5
  • 50
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke, M. & Marahiel, M. A. (2007). Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 71, 413-451.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 51
    • 0033764027 scopus 로고    scopus 로고
    • The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues
    • Ortiz de OruéLucana, D. & Schrempf, H. (2000). The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues. Mol Gen Genet 264, 341-353.
    • (2000) Mol Gen Genet , vol.264 , pp. 341-353
    • de Oruélucana Ortiz, D.1    Schrempf, H.2
  • 52
    • 0035979338 scopus 로고    scopus 로고
    • In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: Characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities
    • Patel, H. M. & Walsh, C. T. (2001). In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities. Biochemistry 40, 9023-9031.
    • (2001) Biochemistry , vol.40 , pp. 9023-9031
    • Patel, H.M.1    Walsh, C.T.2
  • 53
    • 73649110250 scopus 로고    scopus 로고
    • Gene cluster involved in the biosynthesis of griseobactin, a catechol-peptide siderophore of Streptomyces sp. ATCC 700974
    • Patzer, S. I. & Braun, V. (2010). Gene cluster involved in the biosynthesis of griseobactin, a catechol-peptide siderophore of Streptomyces sp. ATCC 700974. J Bacteriol 192, 426-435.
    • (2010) J Bacteriol , vol.192 , pp. 426-435
    • Patzer, S.I.1    Braun, V.2
  • 54
    • 0027251630 scopus 로고
    • Coordinate regulation of siderophore and exotoxin A production: Molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene
    • Prince, R. W., Cox, C. D. & Vasil, M. L. (1993). Coordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene. J Bacteriol 175, 2589-2598.
    • (1993) J Bacteriol , vol.175 , pp. 2589-2598
    • Prince, R.W.1    Cox, C.D.2    Vasil, M.L.3
  • 55
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulenceconferring siderophore mycobactin
    • Quadri, L. E. N., Sello, J., Keating, T. A., Weinreb, P. H. & Walsh, C. T. (1998). Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulenceconferring siderophore mycobactin. Chem Biol 5, 631-645.
    • (1998) Chem Biol , vol.5 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 56
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF
    • Quadri, L. E. N., Keating, T. A., Patel, H. M. & Walsh, C. T. (1999). Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF. Biochemistry 38, 14941-14954.
    • (1999) Biochemistry , vol.38 , pp. 14941-14954
    • Quadri, L.E.N.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 57
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • Rausch, C., Weber, T., Kohlbacher, O., Wohlleben, W. & Huson, D. H. (2005). Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). Nucleic Acids Res 33, 5799-5808.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3    Wohlleben, W.4    Huson, D.H.5
  • 58
    • 0035151726 scopus 로고    scopus 로고
    • Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa
    • Reimmann, C., Patel, H. M., Serino, L., Barone, M., Walsh, C. T. & Haas, D. (2001). Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa. J Bacteriol 183, 813-820.
    • (2001) J Bacteriol , vol.183 , pp. 813-820
    • Reimmann, C.1    Patel, H.M.2    Serino, L.3    Barone, M.4    Walsh, C.T.5    Haas, D.6
  • 59
    • 4544326782 scopus 로고    scopus 로고
    • PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa
    • Reimmann, C., Patel, H. M., Walsh, C. T. & Haas, D. (2004). PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa. J Bacteriol 186, 6367-6373.
    • (2004) J Bacteriol , vol.186 , pp. 6367-6373
    • Reimmann, C.1    Patel, H.M.2    Walsh, C.T.3    Haas, D.4
  • 61
    • 3042801972 scopus 로고    scopus 로고
    • The stereoisomers of pyochelin, a siderophore of Pseudomonas aeruginosa
    • Schlegel, K., Taraz, K. & Budzikiewicz, H. (2004). The stereoisomers of pyochelin, a siderophore of Pseudomonas aeruginosa. Biometals 17, 409-414.
    • (2004) Biometals , vol.17 , pp. 409-414
    • Schlegel, K.1    Taraz, K.2    Budzikiewicz, H.3
  • 62
    • 0023905712 scopus 로고
    • Cloning and expression of two genes of Streptomyces pilosus involved in the biosynthesis of the siderophore desferrioxamine B
    • Schupp, T., Toupet, C. & Divers, M. (1988). Cloning and expression of two genes of Streptomyces pilosus involved in the biosynthesis of the siderophore desferrioxamine B. Gene 64, 179-188.
    • (1988) Gene , vol.64 , pp. 179-188
    • Schupp, T.1    Toupet, C.2    Divers, M.3
  • 63
    • 57349180498 scopus 로고    scopus 로고
    • Streptomyces scabies 87-22 possesses a functional tomatinase
    • Seipke, R. F. & Loria, R. (2008). Streptomyces scabies 87-22 possesses a functional tomatinase. J Bacteriol 190, 7684-7692.
    • (2008) J Bacteriol , vol.190 , pp. 7684-7692
    • Seipke, R.F.1    Loria, R.2
  • 64
    • 0028882959 scopus 로고
    • Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa
    • Serino, L., Reimmann, C., Baur, H., Beyeler, M., Visca, P. & Haas, D. (1995). Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. Mol Gen Genet 249, 217-228.
    • (1995) Mol Gen Genet , vol.249 , pp. 217-228
    • Serino, L.1    Reimmann, C.2    Baur, H.3    Beyeler, M.4    Visca, P.5    Haas, D.6
  • 65
    • 0031020825 scopus 로고    scopus 로고
    • Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron-regulated pchDCBA operon in Pseudomonas aeruginosa
    • Serino, L., Reimmann, C., Visca, P., Beyeler, M., Chiesa, V. D. & Haas, D. (1997). Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron-regulated pchDCBA operon in Pseudomonas aeruginosa. J Bacteriol 179, 248-257.
    • (1997) J Bacteriol , vol.179 , pp. 248-257
    • Serino, L.1    Reimmann, C.2    Visca, P.3    Beyeler, M.4    Chiesa, V.D.5    Haas, D.6
  • 66
    • 34249806024 scopus 로고    scopus 로고
    • The zincresponsive regulator Zur controls a zinc uptake system and some ribosomal proteins in Streptomyces coelicolor A3(2)
    • Shin, J.-H., Oh, S.-Y., Kim, S.-J. & Roe, J.-H. (2007). The zincresponsive regulator Zur controls a zinc uptake system and some ribosomal proteins in Streptomyces coelicolor A3(2). J Bacteriol 189, 4070-4077.
    • (2007) J Bacteriol , vol.189 , pp. 4070-4077
    • Shin, J.-H.1    Oh, S.-Y.2    Kim, S.-J.3    Roe, J.-H.4
  • 67
    • 0022569671 scopus 로고
    • Siderophore-mediated iron acquisition from transferrin by Pseudomonas aeruginosa
    • Sriyosachati, S. & Cox, C. D. (1986). Siderophore-mediated iron acquisition from transferrin by Pseudomonas aeruginosa. Infect Immun 52, 885-891.
    • (1986) Infect Immun , vol.52 , pp. 885-891
    • Sriyosachati, S.1    Cox, C.D.2
  • 68
    • 73849100330 scopus 로고    scopus 로고
    • The siderophore pyoverdine of Pseudomonas syringae pv. tabaci 6605 is an intrinsic virulence factor in host tobacco infection
    • Taguchi, F., Suzuki, T., Inagaki, Y., Toyoda, K., Shiraishi, T. & Ichinose, Y. (2010). The siderophore pyoverdine of Pseudomonas syringae pv. tabaci 6605 is an intrinsic virulence factor in host tobacco infection. J Bacteriol 192, 117-126.
    • (2010) J Bacteriol , vol.192 , pp. 117-126
    • Taguchi, F.1    Suzuki, T.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 69
    • 0034104386 scopus 로고    scopus 로고
    • Impact of siderophore production on Pseudomonas aeruginosa infections in immunosuppressed mice
    • Takase, H., Nitanai, H., Hoshino, K. & Otani, T. (2000). Impact of siderophore production on Pseudomonas aeruginosa infections in immunosuppressed mice. Infect Immun 68, 1834-1839.
    • (2000) Infect Immun , vol.68 , pp. 1834-1839
    • Takase, H.1    Nitanai, H.2    Hoshino, K.3    Otani, T.4
  • 70
    • 34248636493 scopus 로고    scopus 로고
    • Iron acquisition mechanisms of the Burkholderia cepacia complex
    • Thomas, M. S. (2007). Iron acquisition mechanisms of the Burkholderia cepacia complex. Biometals 20, 431-452.
    • (2007) Biometals , vol.20 , pp. 431-452
    • Thomas, M.S.1
  • 71
    • 37249020818 scopus 로고    scopus 로고
    • Pseudomonas fluorescens CHA0 produces enantio-pyochelin, the optical antipode of the Pseudomonas aeruginosa siderophore pyochelin
    • Youard, Z. A., Mislin, G. L. A., Majcherczyk, P. A., Schalk, I. J. & Reimmann, C. (2007). Pseudomonas fluorescens CHA0 produces enantio-pyochelin, the optical antipode of the Pseudomonas aeruginosa siderophore pyochelin. J Biol Chem 282, 35546-35553.
    • (2007) J Biol Chem , vol.282 , pp. 35546-35553
    • Youard, Z.A.1    Mislin, G.L.A.2    Majcherczyk, P.A.3    Schalk, I.J.4    Reimmann, C.5
  • 72
    • 0033026250 scopus 로고    scopus 로고
    • The mycelium-associated Streptomyces reticuli catalaseperoxidase, its gene and regulation by FurS
    • Zou, P.-J., Borovok, I., Ortiz de Oruélucana, D., Müller, D. & Schrempf, H. (1999). The mycelium-associated Streptomyces reticuli catalaseperoxidase, its gene and regulation by FurS. Microbiology 145, 549-559.
    • (1999) Microbiology , vol.145 , pp. 549-559
    • Zou, P.-J.1    Borovok, I.2    de Oruélucana Ortiz, D.3    Müller, D.4    Schrempf, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.