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Volumn 192, Issue 24, 2010, Pages 6428-6438

Expression of the Streptomyces coelicolor SoxR regulon is intimately linked with actinorhodin production

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ACTINORHODINE; BACTERIAL PROTEIN; EPIMERASE; HYDROLYASE; IRON; OXIDOREDUCTASE; PROTEIN SOXR; SULFUR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 78649647804     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00916-10     Document Type: Article
Times cited : (38)

References (55)
  • 1
    • 0344146592 scopus 로고    scopus 로고
    • Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein
    • Arias, P., M. A. Fernandez-Moreno, and F. Malpartida. 1999. Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein. J. Bacteriol. 181:6958-6968.
    • (1999) J. Bacteriol. , vol.181 , pp. 6958-6968
    • Arias, P.1    Fernandez-Moreno, M.A.2    Malpartida, F.3
  • 2
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman, M., R. Logan, K. O'Brien, E. T. Seno, R. N. Rao, and B. E. Schoner. 1992. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116:43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 3
    • 0030844766 scopus 로고    scopus 로고
    • Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation
    • Bradley, T. M., E. Hidalgo, V. Leautaud, H. Ding, and B. Demple. 1997. Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. Nucleic Acids Res. 25:1469-1475.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1469-1475
    • Bradley, T.M.1    Hidalgo, E.2    Leautaud, V.3    Ding, H.4    Demple, B.5
  • 6
    • 0345492332 scopus 로고    scopus 로고
    • Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species
    • Challis, D. L., and D. A. Hopwood. 2003. Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species. Proc. Natl. Acad. Sci. U. S. A. 105:14555-14561.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14555-14561
    • Challis, D.L.1    Hopwood, D.A.2
  • 7
    • 4744353201 scopus 로고    scopus 로고
    • Functional analysis of SoxR residues affecting transduction of oxidative stress signals into gene expression
    • Chander, M., and B. Demple. 2004. Functional analysis of SoxR residues affecting transduction of oxidative stress signals into gene expression. J. Biol. Chem. 279:41603-41610.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41603-41610
    • Chander, M.1    Demple, B.2
  • 8
    • 0037385285 scopus 로고    scopus 로고
    • Transcription-defective soxR mutants of Escherichia coli: Isolation and in vivo characterization
    • Chander, M., L. Raducha-Grace, and B. Demple. 2003. Transcription- defective soxR mutants of Escherichia coli: isolation and in vivo characterization. J. Bacteriol. 185:2441-2450.
    • (2003) J. Bacteriol. , vol.185 , pp. 2441-2450
    • Chander, M.1    Raducha-Grace, L.2    Demple, B.3
  • 9
    • 0029065955 scopus 로고
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 10
    • 0027026475 scopus 로고
    • Self-protection mechanisms in antibiotic producers
    • Cundliffe, E. 1992. Self-protection mechanisms in antibiotic producers. Ciba Found. Symp. 171:199-214.
    • (1992) Ciba Found. Symp. , vol.171 , pp. 199-214
    • Cundliffe, E.1
  • 11
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 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
  • 12
    • 50649098819 scopus 로고    scopus 로고
    • Redox-active antibiotics control gene expression and community behavior in divergent bacteria
    • Dietrich, L. E. P., T. K. Teal, A. Price-Whelan, and D. K. Newman. 2008. Redox-active antibiotics control gene expression and community behavior in divergent bacteria. Science 321:1203-1206.
    • (2008) Science , vol.321 , pp. 1203-1206
    • Dietrich, L.E.P.1    Teal, T.K.2    Price-Whelan, A.3    Newman, D.K.4
  • 13
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signaling factor in the quorum sensing network of Pseudomonas aeruginosa
    • Dietrich, L. E. P., A. Price-Whelan, A. Petersen, M. Whitely, and D. K. Newman. 2006. The phenazine pyocyanin is a terminal signaling factor in the quorum sensing network of Pseudomonas aeruginosa. Mol. Microbiol. 61: 1308-1321.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1308-1321
    • Dietrich, L.E.P.1    Price-Whelan, A.2    Petersen, A.3    Whitely, M.4    Newman, D.K.5
  • 14
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding, H., and B. Demple. 1997. In vivo kinetics of a redox-regulated transcriptional switch. Proc. Natl. Acad. Sci. U. S. A. 94:8445-8449.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 15
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • Ding, H., E. Hidalgo, and B. Demple. 1996. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J. Biol. Chem. 271:33173-33175.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 16
    • 33845411514 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens soxR is involved in superoxide stress protection and also directly regulates superoxide-inducible expression of itself and a target gene
    • Eiamphungporn, W., N. Charoenlap, P. Vattanaviboon, and S. Mongkolsuk. 2006. Agrobacterium tumefaciens soxR is involved in superoxide stress protection and also directly regulates superoxide-inducible expression of itself and a target gene. J. Bacteriol. 188:8669-8673.
    • (2006) J. Bacteriol. , vol.188 , pp. 8669-8673
    • Eiamphungporn, W.1    Charoenlap, N.2    Vattanaviboon, P.3    Mongkolsuk, S.4
  • 17
    • 0033977621 scopus 로고    scopus 로고
    • Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin a in Streptomyces fradiae Tu2717
    • Faust, B., D. Hoffmeister, G. Weitnauer, L. Westrich, S. Haag, P. Schneider, H. Decker, E. Kunzel, J. Rohr, and A. Bechthold. 2000. Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717. Microbiology 146:147-154.
    • (2000) Microbiology , vol.146 , pp. 147-154
    • Faust, B.1    Hoffmeister, D.2    Weitnauer, G.3    Westrich, L.4    Haag, S.5    Schneider, P.6    Decker, H.7    Kunzel, E.8    Rohr, J.9    Bechthold, A.10
  • 18
    • 70350708933 scopus 로고    scopus 로고
    • Microbial responses to xenobiotic compounds. Identification of genes that allow Pseudomonas putida KT2440 to cope with 2,4,6-trinitrotoluene
    • Fernandez, M., E. Duque, P. Pizarro-Tobias, P. van Dillewijn, R. M. Wittich, and J. L. Ramos. 2009. Microbial responses to xenobiotic compounds. Identification of genes that allow Pseudomonas putida KT2440 to cope with 2,4,6-trinitrotoluene. Microb. Biotechnol. 2:287-294.
    • (2009) Microb. Biotechnol. , vol.2 , pp. 287-294
    • Fernandez, M.1    Duque, E.2    Pizarro-Tobias, P.3    Van Dillewijn, P.4    Wittich, R.M.5    Ramos, J.L.6
  • 19
    • 0025899144 scopus 로고
    • The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces
    • Fernandez-Moreno, M. A., J. L. Caballero, D. A. Hopwood, and F. Malpartida. 1991. The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces. Cell 66:769-780.
    • (1991) Cell , vol.66 , pp. 769-780
    • Fernandez-Moreno, M.A.1    Caballero, J.L.2    Hopwood, D.A.3    Malpartida, F.4
  • 20
    • 0029762312 scopus 로고    scopus 로고
    • AfsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2)
    • Floriano, B., and M. Bibb. 1996. afsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2). Mol. Microbiol. 21:385-396.
    • (1996) Mol. Microbiol. , vol.21 , pp. 385-396
    • Floriano, B.1    Bibb, M.2
  • 21
    • 0031048106 scopus 로고    scopus 로고
    • Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo
    • Gaudu, P., N. Moon, and B. Weiss. 1997. Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo. J. Biol. Chem. 272:5082-5086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5082-5086
    • Gaudu, P.1    Moon, N.2    Weiss, B.3
  • 22
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu, P., and B. Weiss. 1996. SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. U. S. A. 93:10094-10098.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 23
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by super-oxide- Generating agents in Escherichia coli
    • Greenberg, J. T., P. Monach, J. J. Chou, P. D. Josephy, and B. Demple. 1990. Positive control of a global antioxidant defense regulon activated by super-oxide- generating agents in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 87:6181-6185.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.J.3    Josephy, P.D.4    Demple, B.5
  • 24
    • 0037452723 scopus 로고    scopus 로고
    • Gene replacement by PCR targeting in Streptomyces and its use to identify a protein domain involved in the biosynthesis of the sesquiterpene odour geosmin
    • Gust, B., G. L. Challis, K. Fowler, T. Kieser, and K. F. Chater. 2003. Gene replacement by PCR targeting in Streptomyces and its use to identify a protein domain involved in the biosynthesis of the sesquiterpene odour 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
  • 25
    • 0035905808 scopus 로고    scopus 로고
    • Crystal structure of the transcription factor BmrR bound to DNA and a drug
    • Heldwein, E. E., and R. G. Brennan. 2001. Crystal structure of the transcription factor BmrR bound to DNA and a drug. Nature 409:378-382.
    • (2001) Nature , vol.409 , pp. 378-382
    • Heldwein, E.E.1    Brennan, R.G.2
  • 26
    • 0025036667 scopus 로고
    • Activator-dependent preinduction binding of sigma-70 RNA polymerase at the metal-regulated mer promoter
    • Heltzel, A., I. W. Lee, P. A. Totis, and A. O. Summers. 1990. Activator-dependent preinduction binding of sigma-70 RNA polymerase at the metal-regulated mer promoter. Biochemistry 29:9572-9584.
    • (1990) Biochemistry , vol.29 , pp. 9572-9584
    • Heltzel, A.1    Lee, I.W.2    Totis, P.A.3    Summers, A.O.4
  • 27
    • 0031041391 scopus 로고    scopus 로고
    • Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor
    • Hidalgo, E., and B. Demple. 1997. Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor. EMBO J. 16:1056-1065.
    • (1997) EMBO J. , vol.16 , pp. 1056-1065
    • Hidalgo, E.1    Demple, B.2
  • 28
    • 0029152251 scopus 로고
    • Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • Hidalgo, E., J. M. Bollinger, Jr., T. M. Bradley, C. T. Walsh, and B. Demple. 1995. Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270:20908-20914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger Jr., J.M.2    Bradley, T.M.3    Walsh, C.T.4    Demple, B.5
  • 29
    • 0028049068 scopus 로고
    • An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
    • Hidalgo, E., and B. Demple. 1994. An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J. 13:138-146.
    • (1994) EMBO J. , vol.13 , pp. 138-146
    • Hidalgo, E.1    Demple, B.2
  • 30
    • 0036299643 scopus 로고    scopus 로고
    • Activation of antibiotic biosynthesis by specified mutations in the rpoB gene (encoding the RNA polymerase β subunit) of Streptomyces lividans
    • Hu, H., Q. Zhang, and K. Ochi. 2002. Activation of antibiotic biosynthesis by specified mutations in the rpoB gene (encoding the RNA polymerase β subunit) of Streptomyces lividans. J. Bacteriol. 184:3984-3991.
    • (2002) J. Bacteriol. , vol.184 , pp. 3984-3991
    • Hu, H.1    Zhang, Q.2    Ochi, K.3
  • 32
    • 0035576880 scopus 로고    scopus 로고
    • Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA microarrays
    • Huang, J., C. J. Lih, K. H. Pan, and S. N. Cohen. 2001. Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA microarrays. Genes Dev. 15:3183-3192.
    • (2001) Genes Dev. , vol.15 , pp. 3183-3192
    • Huang, J.1    Lih, C.J.2    Pan, K.H.3    Cohen, S.N.4
  • 33
    • 0033535067 scopus 로고    scopus 로고
    • Proof that the ACTVI genetic region of Streptomyces coelicolor A3(2) is involved in stereospecific pyran ring formation in the biosynthesis of actinorhodin
    • Ichinose, K., C. Surti, T. Taguchi, F. Malpartida, K. I. Booker-Milburn, G. R. Stephenson, Y. Ebizuka, and D. A. Hopwood. 1999. Proof that the ACTVI genetic region of Streptomyces coelicolor A3(2) is involved in stereospecific pyran ring formation in the biosynthesis of actinorhodin. Bioorg. Med. Chem. Lett. 9:395-400.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 395-400
    • Ichinose, K.1    Surti, C.2    Taguchi, T.3    Malpartida, F.4    Booker-Milburn, K.I.5    Stephenson, G.R.6    Ebizuka, Y.7    Hopwood, D.A.8
  • 35
    • 34548484841 scopus 로고    scopus 로고
    • The virulence of Vibrio vulnificus is affected by the cellular level of superoxide dismutase activity
    • Kang, I. H., J. S. Kim, and J. K. Lee. 2007. The virulence of Vibrio vulnificus is affected by the cellular level of superoxide dismutase activity. J. Microbiol. Biotechnol. 17:1399-1402.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1399-1402
    • Kang, I.H.1    Kim, J.S.2    Lee, J.K.3
  • 37
    • 24344493445 scopus 로고    scopus 로고
    • Induction of manganese-containing superoxide dismutase is required for acid tolerance in Vibrio vulnificus
    • Kim, J. S., M. H. Sung, D. H. Kho, and J. K. Lee. 2005. Induction of manganese-containing superoxide dismutase is required for acid tolerance in Vibrio vulnificus. J. Bacteriol. 187:5984-5995.
    • (2005) J. Bacteriol. , vol.187 , pp. 5984-5995
    • Kim, J.S.1    Sung, M.H.2    Kho, D.H.3    Lee, J.K.4
  • 38
    • 0026667294 scopus 로고
    • Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase
    • MacNeil, D. J., J. L. Occi, K. M. Gewain, T. MacNeil, P. H. Gibbons, C. L. Ruby, and S. L. Danis. 1992. Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase. Gene 115: 119-125.
    • (1992) Gene , vol.115 , pp. 119-125
    • MacNeil, D.J.1    Occi, J.L.2    Gewain, K.M.3    MacNeil, T.4    Gibbons, P.H.5    Ruby, C.L.6    Danis, S.L.7
  • 39
    • 33748685016 scopus 로고    scopus 로고
    • Quorum sensing and phenazines are involved in biofilm formation by Pseudomonas chlororaphis (aureofaciens) strain 30-84
    • Maddula, V. S., Z. Zhang, E. A. Pierson, and L. S. Pierson. 2006. Quorum sensing and phenazines are involved in biofilm formation by Pseudomonas chlororaphis (aureofaciens) strain 30-84. Microb. Ecol. 52:289-301.
    • (2006) Microb. Ecol. , vol.52 , pp. 289-301
    • Maddula, V.S.1    Zhang, Z.2    Pierson, E.A.3    Pierson, L.S.4
  • 40
    • 0019292120 scopus 로고
    • Control of antibiotic biosynthesis
    • Martin, J. F., and A. L. Demain. 1980. Control of antibiotic biosynthesis. Microbiol. Rev. 44:230-251.
    • (1980) Microbiol. Rev. , vol.44 , pp. 230-251
    • Martin, J.F.1    Demain, A.L.2
  • 41
    • 60549093395 scopus 로고    scopus 로고
    • Biosynthesis of actinorhodin and related antibiotics: Discovery of alternative routes for quinone formation encoded in the act gene cluster
    • Okamoto, S., T. Taguchi, K. Ochi, and K. Ichinose. 2009. Biosynthesis of actinorhodin and related antibiotics: discovery of alternative routes for quinone formation encoded in the act gene cluster. Chem. Biol. 16:226-236.
    • (2009) Chem. Biol. , vol.16 , pp. 226-236
    • Okamoto, S.1    Taguchi, T.2    Ochi, K.3    Ichinose, K.4
  • 42
    • 0002266546 scopus 로고
    • Iron-sulfur proteins
    • T. G. Spiro (ed.), John Wiley and Sons, New York, NY
    • Orme-Johnson, W. H., and N. R. Orme-Johnson. 1982. Iron-sulfur proteins, p. 67-96. In T. G. Spiro (ed.), The enzymes, vol. 13. John Wiley and Sons, New York, NY.
    • (1982) The Enzymes , vol.13 , pp. 67-96
    • Orme-Johnson, W.H.1    Orme-Johnson, N.R.2
  • 43
    • 17644408447 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response
    • Palma, M., J. Zurita, J. A. Ferreras, S. Worgall, D. H. Larone, L. Shi, F. Campagne, and L. E. N. Quadri. 2005. Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response. Infect. Immun. 73:2958-2966.
    • (2005) Infect. Immun. , vol.73 , pp. 2958-2966
    • Palma, M.1    Zurita, J.2    Ferreras, J.A.3    Worgall, S.4    Larone, D.H.5    Shi, L.6    Campagne, F.7    Quadri, L.E.N.8
  • 44
    • 30944437009 scopus 로고    scopus 로고
    • Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli
    • Park, W., S. Pena-Llopis, Y. Lee, and B. Demple. 2006. Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli. Biochem. Biophys. Res. Commun. 341:51-56.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 51-56
    • Park, W.1    Pena-Llopis, S.2    Lee, Y.3    Demple, B.4
  • 45
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello, P. J., and B. Demple. 2001. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19:109-114.
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 46
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P. J., M. H. Bennik, and B. Demple. 2001. Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J. Bacteriol. 183:3890-3902.
    • (2001) J. Bacteriol. , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 47
    • 33644907519 scopus 로고    scopus 로고
    • Rethinking "secondary" metabolism: Physiological roles for phenazine antibiotics
    • Price-Whelan, A., L. E. P. Dietrich, and D. K. Newman. 2007. Rethinking "secondary" metabolism: physiological roles for phenazine antibiotics. Nat. Chem. Biol. 2:71-77.
    • (2007) Nat. Chem. Biol. , vol.2 , pp. 71-77
    • Price-Whelan, A.1    Dietrich, L.E.P.2    Newman, D.K.3
  • 48
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen, S., and H. Skaletsky. 2000. Primer3 on the WWW for general users and for biologist programmers. Methods Mol. Biol. 132:365-386.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 51
    • 0032906549 scopus 로고    scopus 로고
    • Mitomycin resistance in Streptomyces lavendulae includes a novel drug-binding-protein-dependent export system
    • Sheldon, P. J., Y. Mao, M. He, and D. H. Sherman. 1999. Mitomycin resistance in Streptomyces lavendulae includes a novel drug-binding-protein- dependent export system. J. Bacteriol. 181:2507-2512.
    • (1999) J. Bacteriol. , vol.181 , pp. 2507-2512
    • Sheldon, P.J.1    Mao, Y.2    He, M.3    Sherman, D.H.4
  • 52
    • 0031053670 scopus 로고    scopus 로고
    • Characterization of a mitomycin-binding drug resistance mechanism from the producing organism, Streptomyces lavendulae
    • Sheldon, P. J., D. A. Johnson, P. R. August, H. W. Liu, and D. H. Sherman. 1997. Characterization of a mitomycin-binding drug resistance mechanism from the producing organism, Streptomyces lavendulae. J. Bacteriol. 179: 1796-1804.
    • (1997) J. Bacteriol. , vol.179 , pp. 1796-1804
    • Sheldon, P.J.1    Johnson, D.A.2    August, P.R.3    Liu, H.W.4    Sherman, D.H.5
  • 54
    • 0027034756 scopus 로고
    • Roles of secondary metabolites from microbes
    • Vining, L. C. 1992. Roles of secondary metabolites from microbes. Ciba Found. Symp. 171:184-194.
    • (1992) Ciba Found. Symp. , vol.171 , pp. 184-194
    • Vining, L.C.1
  • 55
    • 0032946254 scopus 로고    scopus 로고
    • Cloning and characterization of a gene cluster from Streptomyces cyanogenus S136 probably involved in landomycin biosynthesis
    • Westrich, L., S. Domann, B. Faust, D. Bedford, D. A. Hopwood, and A. Bechthold. 1999. Cloning and characterization of a gene cluster from Streptomyces cyanogenus S136 probably involved in landomycin biosynthesis. FEMS Microbiol. Lett. 170:381-387.
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 381-387
    • Westrich, L.1    Domann, S.2    Faust, B.3    Bedford, D.4    Hopwood, D.A.5    Bechthold, A.6


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