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Volumn , Issue , 2009, Pages 13-1-13-26

Regulation of secondary metabolism in bacteria

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EID: 80052844919     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (157)
  • 1
    • 0027025041 scopus 로고
    • Microbial secondary metabolism: A new theoretical frontier for academia, a new opportunity for industry
    • discussion 16-23
    • Demain, A. L. Microbial secondary metabolism: a new theoretical frontier for academia, a new opportunity for industry. Ciba Found. Symp., 171, 3-16; discussion 16-23, 1992.
    • (1992) Ciba Found. Symp. , vol.171 , pp. 3-16
    • Demain, A.L.1
  • 2
    • 0024947834 scopus 로고
    • Why are secondary metabolites (natural products) biosynthesized?
    • Williams, D. H., Stone, M. J., Hauck, P. R., and Rahman, S. K. Why are secondary metabolites (natural products) biosynthesized? J. Nat. Prod., 52 (6), 1189-208, 1989.
    • (1989) J. Nat. Prod. , vol.52 , Issue.6 , pp. 1189-1208
    • Williams, D.H.1    Stone, M.J.2    Hauck, P.R.3    Rahman, S.K.4
  • 3
    • 0345492332 scopus 로고    scopus 로고
    • Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species
    • Challis, G. L. and Hopwood, D. A. Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species. Proc. Natl. Acad. Sci. USA, 100 Suppl 2, 14555-61, 2003.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14555-14561
    • Challis, G.L.1    Hopwood, D.A.2
  • 5
    • 15044342527 scopus 로고    scopus 로고
    • Doxorubicin productivity improvement by the recombinant Streptomyces peucetius with high-copy regulatory genes cultured in the optimized media composition
    • Park, H. S., Kang, S. H., Park, H. J., and Kim, E. S. Doxorubicin productivity improvement by the recombinant Streptomyces peucetius with high-copy regulatory genes cultured in the optimized media composition. J.Microbiol. Biotechnol., 15 (1), 66-71, 2005.
    • (2005) J.Microbiol. Biotechnol. , vol.15 , Issue.1 , pp. 66-71
    • Park, H.S.1    Kang, S.H.2    Park, H.J.3    Kim, E.S.4
  • 6
    • 0036126629 scopus 로고    scopus 로고
    • High-yield actinorhodin production in fed-batch culture by a Streptomyces lividans strain overexpressing the pathway-specific activator gene actll-ORF4
    • Bruheim, P., Sletta, H., Bibb, M. J., White, J., and Levine, D. W. High-yield actinorhodin production in fed-batch culture by a Streptomyces lividans strain overexpressing the pathway-specific activator gene actll-ORF4. J. Ind. Microbiol. Biotechnol., 28 (2), 103-11, 2002.
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.28 , Issue.2 , pp. 103-111
    • Bruheim, P.1    Sletta, H.2    Bibb, M.J.3    White, J.4    Levine, D.W.5
  • 7
    • 24944557992 scopus 로고    scopus 로고
    • Regulation of secondary metabolism in filamentous fungi
    • Yu, J. H. and Keller, N. Regulation of secondary metabolism in filamentous fungi. Annu. Rev. Phytopathol., 43, 437-58, 2005.
    • (2005) Annu. Rev. Phytopathol. , vol.43 , pp. 437-458
    • Yu, J.H.1    Keller, N.2
  • 8
    • 0002435032 scopus 로고
    • Regulation and integration of antibiotic production and morphological differentiation in Streptomyces spp
    • P. Piggot, C. Moran, and P. Youngman, eds, American Society for Microbiology, Washington, DC
    • Champness, W. C. and Chater, K. F. Regulation and integration of antibiotic production and morphological differentiation in Streptomyces spp. In P. Piggot, C. Moran, and P. Youngman, eds. Regulation of Bacterial Differentiation. American Society for Microbiology, Washington, DC, 61-94, 1994.
    • (1994) Regulation of Bacterial Differentiation. , pp. 61-94
    • Champness, W.C.1    Chater, K.F.2
  • 9
    • 0001830516 scopus 로고    scopus 로고
    • Regulation of bacterial antibiotic production
    • H. Kleinkauf and H. von Dohren, eds, Products of Secondary Metabolism. VCH, Weinheim, Germany
    • Chater, K. F. and Bibb, M. J. Regulation of bacterial antibiotic production. In H. Kleinkauf and H. von Dohren, eds. Biotechnology. Vol. 6. Products of Secondary Metabolism. VCH, Weinheim, Germany, 57-105, 1997.
    • (1997) Biotechnology , vol.6 , pp. 57-105
    • Chater, K.F.1    Bibb, M.J.2
  • 10
    • 15744383448 scopus 로고    scopus 로고
    • Regulation of secondary metabolism in streptomycetes
    • Bibb, M. J. Regulation of secondary metabolism in streptomycetes. Curr. Opin. Microbiol., 8 (2), 208-15, 2005.
    • (2005) Curr. Opin. Microbiol. , vol.8 , Issue.2 , pp. 208-215
    • Bibb, M.J.1
  • 13
    • 0038460070 scopus 로고    scopus 로고
    • Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes
    • Novotna, J., Vohradsky, J., Berndt, P., Gramajo, H., Langen, H., Li, X. M., Minas, W., Orsaria, L., Roeder, D., and Thompson, C. J. Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes. Mol. Microbiol., 48 (5), 1289-303, 2003.
    • (2003) Mol. Microbiol. , vol.48 , Issue.5 , pp. 1289-1303
    • Novotna, J.1    Vohradsky, J.2    Berndt, P.3    Gramajo, H.4    Langen, H.5    Li, X.M.6    Minas, W.7    Orsaria, L.8    Roeder, D.9    Thompson, C.J.10
  • 14
    • 20444397992 scopus 로고    scopus 로고
    • Genome-scale analysis of Streptomyces coelicolor A3(2) metabolism
    • Borodina, I., Krabben, P., and Nielsen, J. Genome-scale analysis of Streptomyces coelicolor A3(2) metabolism. Genome Res., 15 (6), 820-29, 2005.
    • (2005) Genome Res. , vol.15 , Issue.6 , pp. 820-829
    • Borodina, I.1    Krabben, P.2    Nielsen, J.3
  • 15
    • 2442715070 scopus 로고    scopus 로고
    • Systematic insertional mutagenesis of a streptomycete genome: A link between osmoadaptation and antibiotic production
    • Bishop, A., Fielding, S., Dyson, P., and Herron, P. Systematic insertional mutagenesis of a streptomycete genome: a link between osmoadaptation and antibiotic production. Genome Res., 14 (5), 893-900, 2004.
    • (2004) Genome Res. , vol.14 , Issue.5 , pp. 893-900
    • Bishop, A.1    Fielding, S.2    Dyson, P.3    Herron, P.4
  • 16
    • 0034662997 scopus 로고    scopus 로고
    • Genomewide insertional mutagenesis in Streptomyces coelicolor reveals additional genes involved in morphological differentiation
    • Gehring, A. M., Nodwell, J. R., Beverley, S. M., and Losick, R. Genomewide insertional mutagenesis in Streptomyces coelicolor reveals additional genes involved in morphological differentiation. Proc. Natl. Acad. Sci. USA, 97 (17), 9642-47, 2000.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.17 , pp. 9642-9647
    • Gehring, A.M.1    Nodwell, J.R.2    Beverley, S.M.3    Losick, R.4
  • 17
    • 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., Lih, C. J., Pan, K. H., and Cohen, S. N. Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways in Streptomyces coelicolor using DNA microarrays. Genes Dev., 15 (23), 3183-92, 2001.
    • (2001) Genes Dev. , vol.15 , Issue.23 , pp. 3183-3192
    • Huang, J.1    Lih, C.J.2    Pan, K.H.3    Cohen, S.N.4
  • 18
    • 22144470117 scopus 로고    scopus 로고
    • An unexpected role for the putative 4'-phosphopantetheinyl transferase-encoding gene nysF in the regulation of nystatin biosynthesis in Streptomyces noursei ATCC 11455
    • Volokhan, O., Sletta, H., Sekurova, O. N., Ellingsen, T. E., and Zotchev, S. B. An unexpected role for the putative 4'-phosphopantetheinyl transferase-encoding gene nysF in the regulation of nystatin biosynthesis in Streptomyces noursei ATCC 11455. FEMS Microbiol. Lett., 249 (1), 57-64, 2005.
    • (2005) FEMS Microbiol. Lett. , vol.249 , Issue.1 , pp. 57-64
    • Volokhan, O.1    Sletta, H.2    Sekurova, O.N.3    Ellingsen, T.E.4    Zotchev, S.B.5
  • 19
    • 0030929313 scopus 로고    scopus 로고
    • A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold
    • Wietzorrek, A. and Bibb, M. A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol. Microbiol., 25 (6), 1181-84, 1997.
    • (1997) Mol. Microbiol. , vol.25 , Issue.6 , pp. 1181-1184
    • Wietzorrek, A.1    Bibb, M.2
  • 20
    • 0035031304 scopus 로고    scopus 로고
    • Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae
    • Wilson, D. J., Xue, Y., Reynolds, K. A., and Sherman, D. H. Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae. J. Bacteriol., 183 (11), 3468-75, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.11 , pp. 3468-3475
    • Wilson, D.J.1    Xue, Y.2    Reynolds, K.A.3    Sherman, D.H.4
  • 21
    • 0029440560 scopus 로고
    • Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete
    • Hopwood, D. A., Chater, K. F., and Bibb, M. J. Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete. Biotechnology, 28, 65-102, 1995.
    • (1995) Biotechnology , vol.28 , pp. 65-102
    • Hopwood, D.A.1    Chater, K.F.2    Bibb, M.J.3
  • 22
    • 0036229192 scopus 로고    scopus 로고
    • Mapping the DNA-binding domain and target sequences of the Streptomyces peucetius daunorubicin biosynthesis regulatory protein, DnrI
    • Sheldon, P. J., Busarow, S. B., and Hutchinson, C. R. Mapping the DNA-binding domain and target sequences of the Streptomyces peucetius daunorubicin biosynthesis regulatory protein, DnrI. Mol. Microbiol., 44 (2), 449-60, 2002.
    • (2002) Mol. Microbiol. , vol.44 , Issue.2 , pp. 449-460
    • Sheldon, P.J.1    Busarow, S.B.2    Hutchinson, C.R.3
  • 23
    • 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 Bibb, M. afsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2). Mol. Microbiol., 21 (2), 385-96, 1996.
    • (1996) Mol. Microbiol. , vol.21 , Issue.2 , pp. 385-396
    • Floriano, B.1    Bibb, M.2
  • 24
    • 0141594679 scopus 로고    scopus 로고
    • AfsR as an integrator of signals that are sensed by multiple serine/threonine kinases in Streptomyces coelicolor A3(2)
    • Horinouchi, S. AfsR as an integrator of signals that are sensed by multiple serine/threonine kinases in Streptomyces coelicolor A3(2). J. Ind. Microbiol. Biotechnol., 30 (8), 462-67, 2003.
    • (2003) J. Ind. Microbiol. Biotechnol. , vol.30 , Issue.8 , pp. 462-467
    • Horinouchi, S.1
  • 25
    • 0029945534 scopus 로고
    • Colworth Prize Lecture. The regulation of antibiotic production in Streptomyces coelicolor A3(2)
    • Bibb, M. 1995. Colworth Prize Lecture. The regulation of antibiotic production in Streptomyces coelicolor A3(2). Microbiology, 142 (Pt 6), 1335-44, 1996.
    • (1995) Microbiology , vol.142 , pp. 1335-1344
    • Bibb, M.1
  • 26
    • 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., Fernandez-Moreno, M. A., and Malpartida, F. Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein. J. Bacteriol., 181 (22), 6958-68, 1999.
    • (1999) J. Bacteriol. , vol.181 , Issue.22 , pp. 6958-6968
    • Arias, P.1    Fernandez-Moreno, M.A.2    Malpartida, F.3
  • 27
    • 0028874933 scopus 로고
    • Regulator of streptomycin gene expression, StrR, of Streptomyces griseus is a DNA binding activator protein with multiple recognition sites
    • Retzlaff, L. and Distler, J. The regulator of streptomycin gene expression, StrR, of Streptomyces griseus is a DNA binding activator protein with multiple recognition sites. Mol. Microbiol., 18 (1), 151-62, 1995.
    • (1995) Mol. Microbiol. , vol.18 , Issue.1 , pp. 151-162
    • Retzlaff, L.1    Distler, J.2
  • 28
    • 0029818342 scopus 로고    scopus 로고
    • Purification and characterization of the DNA-binding protein DnrI, a transcriptional factor of daunorubicin biosynthesis in Streptomyces peucetius
    • Tang, L., Grimm, A., Zhang, Y. X., and Hutchinson, C. R. Purification and characterization of the DNA-binding protein DnrI, a transcriptional factor of daunorubicin biosynthesis in Streptomyces peucetius. Mol. Microbiol., 22 (5), 801-13, 1996.
    • (1996) Mol. Microbiol. , vol.22 , Issue.5 , pp. 801-813
    • Tang, L.1    Grimm, A.2    Zhang, Y.X.3    Hutchinson, C.R.4
  • 29
    • 0026784840 scopus 로고
    • Transcriptional regulation of the redD transcriptional activator gene accounts for growth-phase-dependent production of the antibiotic undecylprodigiosin in Streptomyces coelicolor A3(2)
    • Takano, E., Gramajo, H. C., Strauch, E., Andres, N., White, J., and Bibb, M. J. Transcriptional regulation of the redD transcriptional activator gene accounts for growth-phase-dependent production of the antibiotic undecylprodigiosin in Streptomyces coelicolor A3(2). Mol. Microbiol., 6 (19), 2797-804, 1992.
    • (1992) Mol. Microbiol. , vol.6 , Issue.19 , pp. 2797-2804
    • Takano, E.1    Gramajo, H.C.2    Strauch, E.3    Andres, N.4    White, J.5    Bibb, M.J.6
  • 30
    • 0025117571 scopus 로고
    • Nucleotide sequence and transcriptional analysis of the redD locus of Streptomyces coelicolor A3(2)
    • Narva, K. E. and Feitelson, J. S. Nucleotide sequence and transcriptional analysis of the redD locus of Streptomyces coelicolor A3(2). J. Bacteriol., 172 (1), 326-33, 1990.
    • (1990) J. Bacteriol. , vol.172 , Issue.1 , pp. 326-333
    • Narva, K.E.1    Feitelson, J.S.2
  • 31
    • 0029937535 scopus 로고    scopus 로고
    • A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: Sequence analysis and complementation of early-block mutations in the anthracycline pathway
    • Ylihonko, K., Tuikkanen, J., Jussila, S., Cong, L., and Mantsala, P. A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway. Mol. Gen. Genet., 251 (2), 113-20, 1996.
    • (1996) Mol. Gen. Genet. , vol.251 , Issue.2 , pp. 113-120
    • Ylihonko, K.1    Tuikkanen, J.2    Jussila, S.3    Cong, L.4    Mantsala, P.5
  • 32
    • 0030954966 scopus 로고    scopus 로고
    • A regulatory gene (ccaR) required for cephamycin and clavulanic acid production in Streptomyces clavuligerus: Amplification results in overproduction of both beta-lactam compounds
    • Perez-Llarena, F. J., Liras, P., Rodriguez-Garcia, A., and Martin, J. F. A regulatory gene (ccaR) required for cephamycin and clavulanic acid production in Streptomyces clavuligerus: amplification results in overproduction of both beta-lactam compounds. J. Bacteriol., 179 (6), 2053-59, 1997.
    • (1997) J. Bacteriol. , vol.179 , Issue.6 , pp. 2053-2059
    • Perez-Llarena, F.J.1    Liras, P.2    Rodriguez-Garcia, A.3    Martin, J.F.4
  • 33
    • 0036097237 scopus 로고    scopus 로고
    • CcaR is an autoregulatory protein that binds to the ccaR and cefD-cmcI promoters of the cephamycin C-clavulanic acid cluster in Streptomyces clavuligerus
    • Santamarta, I., Rodriguez-Garcia, A., Perez-Redondo, R., Martin, J. F., and Liras, P. CcaR is an autoregulatory protein that binds to the ccaR and cefD-cmcI promoters of the cephamycin C-clavulanic acid cluster in Streptomyces clavuligerus. J. Bacteriol., 184 (11), 3106-13, 2002.
    • (2002) J. Bacteriol. , vol.184 , Issue.11 , pp. 3106-3113
    • Santamarta, I.1    Rodriguez-Garcia, A.2    Perez-Redondo, R.3    Martin, J.F.4    Liras, P.5
  • 34
    • 0032902411 scopus 로고    scopus 로고
    • Mithramycin gene cluster of Streptomyces argillaceus contains a positive regulatory gene and two repeated DNA sequences that are located at both ends of the cluster
    • Lombo, F., Brana, A. F., Mendez, C., and Salas, J. A. The mithramycin gene cluster of Streptomyces argillaceus contains a positive regulatory gene and two repeated DNA sequences that are located at both ends of the cluster. J. Bacteriol., 181 (2), 642-7, 1999.
    • (1999) J. Bacteriol. , vol.181 , Issue.2 , pp. 642-647
    • Lombo, F.1    Brana, A.F.2    Mendez, C.3    Salas, J.A.4
  • 35
    • 15244341383 scopus 로고    scopus 로고
    • Involvement of AlpV, a new member of the Streptomyces antibiotic regulatory protein family, in regulation of the duplicated type II polyketide synthase alp gene cluster in Streptomyces ambofaciens
    • Aigle, B., Pang, X., Decaris, B., and Leblond, P. Involvement of AlpV, a new member of the Streptomyces antibiotic regulatory protein family, in regulation of the duplicated type II polyketide synthase alp gene cluster in Streptomyces ambofaciens. J. Bacteriol., 187 (7), 2491-500, 2005.
    • (2005) J. Bacteriol. , vol.187 , Issue.7 , pp. 2491-2500
    • Aigle, B.1    Pang, X.2    Decaris, B.3    Leblond, P.4
  • 36
    • 21344473915 scopus 로고    scopus 로고
    • NovG, a DNA-binding protein acting as a positive regulator of novobiocin biosynthesis
    • Eustaquio, A. S., Li, S. M., and Heide, L. NovG, a DNA-binding protein acting as a positive regulator of novobiocin biosynthesis. Microbiology, 151 (Pt 6), 1949-61, 2005.
    • (2005) Microbiology , vol.151 , pp. 1949-1961
    • Eustaquio, A.S.1    Li, S.M.2    Heide, L.3
  • 37
    • 0038325632 scopus 로고    scopus 로고
    • Production of landomycins in Streptomyces globisporus 1912 and S cyanogenus S136 is regulated by genes encoding putative transcriptional activators
    • Rebets, Y., Ostash, B., Luzhetskyy, A., Hoffmeister, D., Brana, A., Mendez, C., Salas, J. A., Bechthold, A., and Fedorenko, V. Production of landomycins in Streptomyces globisporus 1912 and S cyanogenus S136 is regulated by genes encoding putative transcriptional activators. FEMS Microbiol. Lett., 222 (1), 149-53, 2003.
    • (2003) FEMS Microbiol. Lett. , vol.222 , Issue.1 , pp. 149-153
    • Rebets, Y.1    Ostash, B.2    Luzhetskyy, A.3    Hoffmeister, D.4    Brana, A.5    Mendez, C.6    Salas, J.A.7    Bechthold, A.8    Fedorenko, V.9
  • 38
    • 13444292553 scopus 로고    scopus 로고
    • DNA-binding activity of LndI protein and temporal expression of the gene that upregulates landomycin E production in Streptomyces globisporus 1912
    • Rebets, Y., Ostash, B., Luzhetskyy, A., Kushnir, S., Fukuhara, M., Bechthold, A., Nashimoto, M., Nakamura, T., and Fedorenko, V. DNA-binding activity of LndI protein and temporal expression of the gene that upregulates landomycin E production in Streptomyces globisporus 1912. Microbiology, 151 (Pt 1), 281-90, 2005.
    • (2005) Microbiology , vol.151 , pp. 281-290
    • Rebets, Y.1    Ostash, B.2    Luzhetskyy, A.3    Kushnir, S.4    Fukuhara, M.5    Bechthold, A.6    Nashimoto, M.7    Nakamura, T.8    Fedorenko, V.9
  • 39
    • 1342304165 scopus 로고    scopus 로고
    • In vivo analysis of the regulatory genes in the nystatin biosynthetic gene cluster of Streptomyces noursei ATCC 11455 reveals their differential control over antibiotic biosynthesis
    • Sekurova, O. N., Brautaset, T., Sletta, H., Borgos, S. E., Jakobsen, M. O., Ellingsen, T. E., Strom, A. R., Valla, S., and Zotchev, S. B. In vivo analysis of the regulatory genes in the nystatin biosynthetic gene cluster of Streptomyces noursei ATCC 11455 reveals their differential control over antibiotic biosynthesis. J. Bacteriol., 186 (5), 1345-54, 2004.
    • (2004) J. Bacteriol. , vol.186 , Issue.5 , pp. 1345-1354
    • Sekurova, O.N.1    Brautaset, T.2    Sletta, H.3    Borgos, S.E.4    Jakobsen, M.O.5    Ellingsen, T.E.6    Strom, A.R.7    Valla, S.8    Zotchev, S.B.9
  • 40
    • 0029872079 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of the enzymatic domains in the modular polyketide synthase
    • Aparicio, J. F., Molnar, I., Schwecke, T., Konig, A., Haydock, S. F., Khaw, L. E., Staunton, J., and Leadlay, P. F. Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase. Gene, 169 (1), 9-16, 1996.
    • (1996) Gene , vol.169 , Issue.1 , pp. 9-16
    • Aparicio, J.F.1    Molnar, I.2    Schwecke, T.3    Konig, A.4    Haydock, S.F.5    Khaw, L.E.6    Staunton, J.7    Leadlay, P.F.8
  • 41
    • 1942539982 scopus 로고    scopus 로고
    • Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis
    • Anton, N., Mendes, M. V., Martin, J. F., and Aparicio, J. F. Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis. J. Bacteriol., 186 (9), 2567-75, 2004.
    • (2004) J. Bacteriol. , vol.186 , Issue.9 , pp. 2567-2575
    • Anton, N.1    Mendes, M.V.2    Martin, J.F.3    Aparicio, J.F.4
  • 43
    • 0029891143 scopus 로고    scopus 로고
    • Global negative regulation of Streptomyces coelicolor antibiotic synthesis mediated by an absA-encoded putative signal transduction system
    • Brian, P., Riggle, P. J., Santos, R. A., and Champness, W. C. Global negative regulation of Streptomyces coelicolor antibiotic synthesis mediated by an absA-encoded putative signal transduction system. J. Bacteriol., 178 (11), 3221-31, 1996.
    • (1996) J. Bacteriol. , vol.178 , Issue.11 , pp. 3221-3231
    • Brian, P.1    Riggle, P.J.2    Santos, R.A.3    Champness, W.C.4
  • 44
    • 0029821306 scopus 로고    scopus 로고
    • Cutrs signal transduction system of Streptomyces lividans represses the biosynthesis of the polyketide antibiotic actinorhodin
    • Chang, H. M., Chen, M. Y., Shieh, Y. T., Bibb, M. J., and Chen, C. W. The cutRS signal transduction system of Streptomyces lividans represses the biosynthesis of the polyketide antibiotic actinorhodin. Mol. Microbiol., 21 (5), 1075-85, 1996.
    • (1996) Mol. Microbiol. , vol.21 , Issue.5 , pp. 1075-1085
    • Chang, H.M.1    Chen, M.Y.2    Shieh, Y.T.3    Bibb, M.J.4    Chen, C.W.5
  • 45
    • 23844502988 scopus 로고    scopus 로고
    • Characterization of a regulatory gene essential for the production of the angucycline-like polyketide antibiotic auricin in Streptomyces aureofaciens CCM 3239
    • Novakova, R., Homerova, D., Feckova, L., and Kormanec, J. Characterization of a regulatory gene essential for the production of the angucycline-like polyketide antibiotic auricin in Streptomyces aureofaciens CCM 3239. Microbiology, 151 (Pt 8), 2693-706, 2005.
    • (2005) Microbiology , vol.151 , pp. 2693-2706
    • Novakova, R.1    Homerova, D.2    Feckova, L.3    Kormanec, J.4
  • 46
    • 0031906193 scopus 로고    scopus 로고
    • A responseregulator-like activator of antibiotic synthesis from Streptomyces coelicolor A3(2) with an aminoterminal domain that lacks a phosphorylation pocket
    • Guthrie, E. P., Flaxman, C. S., White, J., Hodgson, D. A., Bibb, M. J., and Chater, K. F., A responseregulator-like activator of antibiotic synthesis from Streptomyces coelicolor A3(2) with an aminoterminal domain that lacks a phosphorylation pocket. Microbiology, 144 (Pt 3), 727-38, 1998.
    • (1998) Microbiology , vol.144 , pp. 727-738
    • Guthrie, E.P.1    Flaxman, C.S.2    White, J.3    Hodgson, D.A.4    Bibb, M.J.5    Chater, K.F.6
  • 47
    • 10344221578 scopus 로고    scopus 로고
    • DnrN protein of Streptomyces peucetius, a pseudo-response regulator, is a DNA-binding protein involved in the regulation of daunorubicin biosynthesis
    • Furuya, K. and Hutchinson, C. R. The DnrN protein of Streptomyces peucetius, a pseudo-response regulator, is a DNA-binding protein involved in the regulation of daunorubicin biosynthesis. J. Bacteriol., 178 (21), 6310-8, 1996.
    • (1996) J. Bacteriol. , vol.178 , Issue.21 , pp. 6310-6318
    • Furuya, K.1    Hutchinson, C.R.2
  • 48
    • 26244432061 scopus 로고    scopus 로고
    • Transcriptional activation of the pathway-specific regulator of the actinorhodin biosynthetic genes in Streptomyces coelicolor
    • Uguru, G. C., Stephens, K. E., Stead, J. A., Towle, J. E., Baumberg, S., and McDowall, K. J., Transcriptional activation of the pathway-specific regulator of the actinorhodin biosynthetic genes in Streptomyces coelicolor. Mol. Microbiol., 58 (1), 131-50, 2005.
    • (2005) Mol. Microbiol. , vol.58 , Issue.1 , pp. 131-150
    • Uguru, G.C.1    Stephens, K.E.2    Stead, J.A.3    Towle, J.E.4    Baumberg, S.5    McDowall, K.J.6
  • 49
    • 8844259757 scopus 로고    scopus 로고
    • Building filaments in the air: Aerial morphogenesis in bacteria and fungi
    • Elliot, M. A. and Talbot, N. J. Building filaments in the air: aerial morphogenesis in bacteria and fungi. Curr. Opin. Microbiol., 7 (6), 594-601, 2004.
    • (2004) Curr. Opin. Microbiol. , vol.7 , Issue.6 , pp. 594-601
    • Elliot, M.A.1    Talbot, N.J.2
  • 50
    • 0024149321 scopus 로고
    • Protein phosphorylation in prokaryotes
    • Cozzone, A. J. Protein phosphorylation in prokaryotes. Annu. Rev. Microbiol., 42, 97-125, 1988.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 97-125
    • Cozzone, A.J.1
  • 51
    • 0035133737 scopus 로고    scopus 로고
    • Genetic and transcriptional analysis of absA, an antibiotic gene cluster-linked two-component system that regulates multiple antibiotics in Streptomyces coelicolor
    • Anderson, T. B., Brian, P., and Champness, W. C. Genetic and transcriptional analysis of absA, an antibiotic gene cluster-linked two-component system that regulates multiple antibiotics in Streptomyces coelicolor. Mol. Microbiol., 39 (3), 553-66, 2001.
    • (2001) Mol. Microbiol. , vol.39 , Issue.3 , pp. 553-566
    • Anderson, T.B.1    Brian, P.2    Champness, W.C.3
  • 52
    • 0031800852 scopus 로고    scopus 로고
    • Transcriptional regulation of Streptomyces coelicolor pathwayspecific antibiotic regulators by the absA and absB loci
    • Aceti, D. J. and Champness, W. C. Transcriptional regulation of Streptomyces coelicolor pathwayspecific antibiotic regulators by the absA and absB loci. J. Bacteriol., 180 (12), 3100-6, 1998.
    • (1998) J. Bacteriol. , vol.180 , Issue.12 , pp. 3100-3106
    • Aceti, D.J.1    Champness, W.C.2
  • 53
    • 3843050181 scopus 로고    scopus 로고
    • Phosphate control of the biosynthesis of antibiotics and other secondary metabolites is mediated by the PhoR-PhoP system: An unfinished story
    • Martin, J. F. Phosphate control of the biosynthesis of antibiotics and other secondary metabolites is mediated by the PhoR-PhoP system: an unfinished story. J. Bacteriol., 186 (16), 5197-201, 2004.
    • (2004) J. Bacteriol. , vol.186 , Issue.16 , pp. 5197-5201
    • Martin, J.F.1
  • 54
    • 0026490160 scopus 로고
    • A putative two-component regulatory system involved in secondary metabolism in Streptomyces spp
    • Ishizuka, H., Horinouchi, S., Kieser, H. M., Hopwood, D. A., and Beppu, T. A putative two-component regulatory system involved in secondary metabolism in Streptomyces spp. J. Bacteriol., 174 (23), 7585-94, 1992.
    • (1992) J. Bacteriol. , vol.174 , Issue.23 , pp. 7585-7594
    • Ishizuka, H.1    Horinouchi, S.2    Kieser, H.M.3    Hopwood, D.A.4    Beppu, T.5
  • 55
    • 0038284769 scopus 로고    scopus 로고
    • Two-component PhoR-PhoP system controls both primary metabolism and secondary metabolite biosynthesis in Streptomyces lividans
    • Sola-Landa, A., Moura, R. S., and Martin, J. F. The two-component PhoR-PhoP system controls both primary metabolism and secondary metabolite biosynthesis in Streptomyces lividans. Proc. Natl. Acad. Sci. USA, 100 (10), 6133-38, 2003.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.10 , pp. 6133-6138
    • Sola-Landa, A.1    Moura, R.S.2    Martin, J.F.3
  • 56
    • 0035019043 scopus 로고    scopus 로고
    • Genomic analysis of the histidine kinase family in bacteria and archaea
    • Kim, D. and Forst, S. Genomic analysis of the histidine kinase family in bacteria and archaea. Microbiology, 147 (Pt 5), 1197-212, 2001.
    • (2001) Microbiology , vol.147 , pp. 1197-1212
    • Kim, D.1    Forst, S.2
  • 57
    • 4844230017 scopus 로고    scopus 로고
    • Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2)
    • Hutchings, M. I., Hoskisson, P. A., Chandra, G., and Buttner, M. J. Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2). Microbiology, 150 (Pt 9), 2795-806, 2004.
    • (2004) Microbiology , vol.150 , pp. 2795-2806
    • Hutchings, M.I.1    Hoskisson, P.A.2    Chandra, G.3    Buttner, M.J.4
  • 58
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • Kennelly, P. J. Protein kinases and protein phosphatases in prokaryotes: a genomic perspective. FEMS Microbiol. Lett., 206 (1), 1-8, 2002.
    • (2002) FEMS Microbiol. Lett. , vol.206 , Issue.1 , pp. 1-8
    • Kennelly, P.J.1
  • 59
    • 0038039713 scopus 로고    scopus 로고
    • Eukaryotic-type protein kinases in Streptomyces coelicolor: Variations on a common theme
    • Petrickova, K. and Petricek, M. Eukaryotic-type protein kinases in Streptomyces coelicolor: variations on a common theme. Microbiology, 149 (Pt 7), 1609-21, 2003.
    • (2003) Microbiology , vol.149 , pp. 1609-1621
    • Petrickova, K.1    Petricek, M.2
  • 60
    • 0034837644 scopus 로고    scopus 로고
    • Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein
    • Umeyama, T. and Horinouchi, S. Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein. J. Bacteriol., 183 (19), 5506-12, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.19 , pp. 5506-5512
    • Umeyama, T.1    Horinouchi, S.2
  • 61
    • 0036268103 scopus 로고    scopus 로고
    • Afss is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2)
    • Lee, P. C., Umeyama, T., and Horinouchi, S. afsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2). Mol. Microbiol., 43 (6), 1413-30, 2002.
    • (2002) Mol. Microbiol. , vol.43 , Issue.6 , pp. 1413-1430
    • Lee, P.C.1    Umeyama, T.2    Horinouchi, S.3
  • 62
    • 0036040203 scopus 로고    scopus 로고
    • Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces
    • Umeyama, T., Lee, P. C., and Horinouchi, S. Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces. Appl. Microbiol. Biotechnol., 59 (4-5), 419-25, 2002.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , Issue.4-5 , pp. 419-425
    • Umeyama, T.1    Lee, P.C.2    Horinouchi, S.3
  • 63
    • 4344568532 scopus 로고    scopus 로고
    • Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes
    • Shi, L. and Zhang, W. Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes. Microbiology, 150 (Pt 7), 2247-56, 2004.
    • (2004) Microbiology , vol.150 , pp. 2247-2256
    • Shi, L.1    Zhang, W.2
  • 64
    • 0030045016 scopus 로고    scopus 로고
    • Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2)
    • Li, Y. and Strohl, W. R. Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2). J. Bacteriol., 178 (1), 136-42, 1996.
    • (1996) J. Bacteriol. , vol.178 , Issue.1 , pp. 136-142
    • Li, Y.1    Strohl, W.R.2
  • 65
    • 0030273880 scopus 로고    scopus 로고
    • Expression of the Streptomyces coelicolor A3(2) ptpA gene encoding a phosphotyrosine protein phosphatase leads to overproduction of secondary metabolites in S. lividans
    • Umeyama, T., Tanabe, Y., Aigle, B. D., and Horinouchi, S. Expression of the Streptomyces coelicolor A3(2) ptpA gene encoding a phosphotyrosine protein phosphatase leads to overproduction of secondary metabolites in S. lividans. FEMS Microbiol. Lett., 144 (2-3), 177-84, 1996.
    • (1996) FEMS Microbiol. Lett. , vol.144 , Issue.2-3 , pp. 177-184
    • Umeyama, T.1    Tanabe, Y.2    Aigle, B.D.3    Horinouchi, S.4
  • 66
    • 11844296791 scopus 로고    scopus 로고
    • Biochemical activities of the absA two-component system of Streptomyces coelicolor
    • Sheeler, N. L., MacMillan, S. V., and Nodwell, J. R. Biochemical activities of the absA two-component system of Streptomyces coelicolor. J. Bacteriol., 187 (2), 687-96, 2005.
    • (2005) J. Bacteriol. , vol.187 , Issue.2 , pp. 687-696
    • Sheeler, N.L.1    MacMillan, S.V.2    Nodwell, J.R.3
  • 67
    • 0000934764 scopus 로고    scopus 로고
    • Autoregulatory factors and regulation of antibiotic production in Streptomyces
    • England, R. R., Hobbs, G., Bainton, N. J., and Roberts, D. McL., eds, Cambridge University Press, Cambridge, U.K
    • Yamada, Y. Autoregulatory factors and regulation of antibiotic production in Streptomyces. In England, R. R., Hobbs, G., Bainton, N. J., and Roberts, D. McL., eds. Microbial Signalling and Communication. Cambridge University Press, Cambridge, U.K., 177-196, 1999.
    • (1999) Microbial Signalling and Communication. , pp. 177-196
    • Yamada, Y.1
  • 68
    • 0141921879 scopus 로고    scopus 로고
    • Gamma-butyrolactone autoregulators and receptor proteins in non-Streptomyces actinomycetes producing commercially important secondary metabolites
    • Choi, S. U., Lee, C. K., Hwang, Y. I., Kinosita, H., and Nihira, T. Gamma-butyrolactone autoregulators and receptor proteins in non-Streptomyces actinomycetes producing commercially important secondary metabolites. Arch. Microbiol., 180 (4), 303-7, 2003.
    • (2003) Arch. Microbiol. , vol.180 , Issue.4 , pp. 303-307
    • Choi, S.U.1    Lee, C.K.2    Hwang, Y.I.3    Kinosita, H.4    Nihira, T.5
  • 69
    • 0036731699 scopus 로고    scopus 로고
    • Listening in on bacteria: Acyl-homoserine lactone signaling
    • Fuqua, C. and Greenberg, E. P., Listening in on bacteria: acyl-homoserine lactone signaling. Nat. Rev. Mol. Cell. Biol., 3 (9), 685-95, 2002.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , Issue.9 , pp. 685-695
    • Fuqua, C.1    Greenberg, E.P.2
  • 70
    • 0028245937 scopus 로고
    • A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus
    • Horinouchi, S. and Beppu, T. A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus. Mol. Microbiol., 12 (6), 859-64, 1994.
    • (1994) Mol. Microbiol. , vol.12 , Issue.6 , pp. 859-864
    • Horinouchi, S.1    Beppu, T.2
  • 71
    • 17844392892 scopus 로고    scopus 로고
    • AdpA, a central transcriptional regulator in the A-factor regulatory cascade that leads to morphological development and secondary metabolism in Streptomyces griseus
    • Ohnishi, Y., Yamazaki, H., Kato, J. Y., Tomono, A., and Horinouchi, S. AdpA, a central transcriptional regulator in the A-factor regulatory cascade that leads to morphological development and secondary metabolism in Streptomyces griseus. Biosci. Biotechnol. Biochem., 69 (3), 431-39, 2005.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , Issue.3 , pp. 431-439
    • Ohnishi, Y.1    Yamazaki, H.2    Kato, J.Y.3    Tomono, A.4    Horinouchi, S.5
  • 72
    • 23644431543 scopus 로고    scopus 로고
    • Transcriptional control by A-factor of strR, the pathway-specific transcriptional activator for streptomycin biosynthesis in Streptomyces griseus
    • Tomono, A., Tsai, Y., Yamazaki, H., Ohnishi, Y., and Horinouchi, S. Transcriptional control by A-factor of strR, the pathway-specific transcriptional activator for streptomycin biosynthesis in Streptomyces griseus. J. Bacteriol., 187 (16), 5595-604, 2005.
    • (2005) J. Bacteriol. , vol.187 , Issue.16 , pp. 5595-5604
    • Tomono, A.1    Tsai, Y.2    Yamazaki, H.3    Ohnishi, Y.4    Horinouchi, S.5
  • 73
    • 1642367161 scopus 로고    scopus 로고
    • A single target is sufficient to account for the biological effects of the A-factor receptor protein of Streptomyces griseus
    • Kato, J. Y., Miyahisa, I., Mashiko, M., Ohnishi, Y., and Horinouchi, S. A single target is sufficient to account for the biological effects of the A-factor receptor protein of Streptomyces griseus. J. Bacteriol., 186 (7), 2206-11, 2004.
    • (2004) J. Bacteriol. , vol.186 , Issue.7 , pp. 2206-2211
    • Kato, J.Y.1    Miyahisa, I.2    Mashiko, M.3    Ohnishi, Y.4    Horinouchi, S.5
  • 74
    • 3242891579 scopus 로고    scopus 로고
    • DNA-binding specificity of AdpA, a transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus
    • Yamazaki, H., Tomono, A., Ohnishi, Y., and Horinouchi, S. DNA-binding specificity of AdpA, a transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus. Mol. Microbiol., 53 (2), 555-72, 2004.
    • (2004) Mol. Microbiol. , vol.53 , Issue.2 , pp. 555-572
    • Yamazaki, H.1    Tomono, A.2    Ohnishi, Y.3    Horinouchi, S.4
  • 75
    • 20444379644 scopus 로고    scopus 로고
    • Autorepression of AdpA of the AraC/XylS family, a key transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus
    • Kato, J. Y., Ohnishi, Y., and Horinouchi, S. Autorepression of AdpA of the AraC/XylS family, a key transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus. J. Mol. Biol., 350 (1), 12-26, 2005.
    • (2005) J. Mol. Biol. , vol.350 , Issue.1 , pp. 12-26
    • Kato, J.Y.1    Ohnishi, Y.2    Horinouchi, S.3
  • 76
    • 0030836620 scopus 로고    scopus 로고
    • DNA-binding activity of the A-factor receptor protein and its recognition DNA sequences
    • Onaka, H. and Horinouchi, S. DNA-binding activity of the A-factor receptor protein and its recognition DNA sequences. Mol. Microbiol., 24 (5), 991-1000, 1997.
    • (1997) Mol. Microbiol. , vol.24 , Issue.5 , pp. 991-1000
    • Onaka, H.1    Horinouchi, S.2
  • 77
    • 17644368157 scopus 로고    scopus 로고
    • Different proteins bind to the butyrolactone receptor protein ARE sequence located upstream of the regulatory ccaR gene of Streptomyces clavuligerus
    • Santamarta, I., Perez-Redondo, R., Lorenzana, L. M., Martin, J. F., and Liras, P. Different proteins bind to the butyrolactone receptor protein ARE sequence located upstream of the regulatory ccaR gene of Streptomyces clavuligerus. Mol. Microbiol., 56 (3), 824-35, 2005.
    • (2005) Mol. Microbiol. , vol.56 , Issue.3 , pp. 824-835
    • Santamarta, I.1    Perez-Redondo, R.2    Lorenzana, L.M.3    Martin, J.F.4    Liras, P.5
  • 78
    • 0023192121 scopus 로고
    • Structure of inducing factors for virginiamycin production in Streptomyces virginiae
    • Yamada, Y., Sugamura, K., Kondo, K., Yanagimoto, M., and Okada, H. The structure of inducing factors for virginiamycin production in Streptomyces virginiae. J. Antibiot. (Tokyo), 40 (4), 496-504, 1987.
    • (1987) J. Antibiot. (Tokyo) , vol.40 , Issue.4 , pp. 496-504
    • Yamada, Y.1    Sugamura, K.2    Kondo, K.3    Yanagimoto, M.4    Okada, H.5
  • 79
    • 0034972542 scopus 로고    scopus 로고
    • Gene replacement analysis of the butyrolactone autoregulator receptor (FarA) reveals that FarA acts as a Novel regulator in secondary metabolism of Streptomyces lavendulae FRI-5
    • Kitani, S., Yamada, Y., and Nihira, T. Gene replacement analysis of the butyrolactone autoregulator receptor (FarA) reveals that FarA acts as a Novel regulator in secondary metabolism of Streptomyces lavendulae FRI-5. J. Bacteriol., 183 (14), 4357-63, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.14 , pp. 4357-4363
    • Kitani, S.1    Yamada, Y.2    Nihira, T.3
  • 80
    • 0035788803 scopus 로고    scopus 로고
    • A complex role for the gamma-butyrolactone SCB1 in regulating antibiotic production in Streptomyces coelicolor A3(2)
    • Takano, E., Chakraburtty, R., Nihira, T., Yamada, Y., and Bibb, M. J. A complex role for the gamma-butyrolactone SCB1 in regulating antibiotic production in Streptomyces coelicolor A3(2). Mol. Microbiol., 41 (5), 1015-28, 2001.
    • (2001) Mol. Microbiol. , vol.41 , Issue.5 , pp. 1015-1028
    • Takano, E.1    Chakraburtty, R.2    Nihira, T.3    Yamada, Y.4    Bibb, M.J.5
  • 81
    • 20244388405 scopus 로고    scopus 로고
    • A bacterial hormone (the SCB1) directly controls the expression of a pathway-specific regulatory gene in the cryptic type I polyketide biosynthetic gene cluster of Streptomyces coelicolor
    • Takano, E., Kinoshita, H., Mersinias, V., Bucca, G., Hotchkiss, G., Nihira, T., Smith, C. P., Bibb, M., Wohlleben, W., and Chater, K. A bacterial hormone (the SCB1) directly controls the expression of a pathway-specific regulatory gene in the cryptic type I polyketide biosynthetic gene cluster of Streptomyces coelicolor. Mol. Microbiol., 56 (2), 465-79, 2005.
    • (2005) Mol. Microbiol. , vol.56 , Issue.2 , pp. 465-479
    • Takano, E.1    Kinoshita, H.2    Mersinias, V.3    Bucca, G.4    Hotchkiss, G.5    Nihira, T.6    Smith, C.P.7    Bibb, M.8    Wohlleben, W.9    Chater, K.10
  • 82
    • 0036365252 scopus 로고    scopus 로고
    • Regulation of tylosin production and morphological differentiation in Streptomyces fradiae by TylP, a deduced gamma-butyrolactone receptor
    • Stratigopoulos, G., Gandecha, A. R., and Cundliffe, E. Regulation of tylosin production and morphological differentiation in Streptomyces fradiae by TylP, a deduced gamma-butyrolactone receptor. Mol. Microbiol., 45 (3), 735-44, 2002.
    • (2002) Mol. Microbiol. , vol.45 , Issue.3 , pp. 735-744
    • Stratigopoulos, G.1    Gandecha, A.R.2    Cundliffe, E.3
  • 83
    • 4544242286 scopus 로고    scopus 로고
    • Cloning and characterization of a gene encoding the gamma-butyrolactone autoregulator receptor from Streptomyces clavuligerus
    • Kim, H. S., Lee, Y. J., Lee, C. K., Choi, S. U., Yeo, S. H., Hwang, Y. I., Yu, T. S., Kinoshita, H., and Nihira, T. Cloning and characterization of a gene encoding the gamma-butyrolactone autoregulator receptor from Streptomyces clavuligerus. Arch. Microbiol., 182 (1), 44-50, 2004.
    • (2004) Arch. Microbiol. , vol.182 , Issue.1 , pp. 44-50
    • Kim, H.S.1    Lee, Y.J.2    Lee, C.K.3    Choi, S.U.4    Yeo, S.H.5    Hwang, Y.I.6    Yu, T.S.7    Kinoshita, H.8    Nihira, T.9
  • 84
    • 27744469345 scopus 로고    scopus 로고
    • Cloning and in vivo functional analysis by disruption of a gene encoding the gamma-butyrolactone autoregulator receptor from Streptomyces natalensis
    • Lee, K. M., Lee, C. K., Choi, S. U., Park, H. R., Kitani, S., Nihira, T., and Hwang, Y. I. Cloning and in vivo functional analysis by disruption of a gene encoding the gamma-butyrolactone autoregulator receptor from Streptomyces natalensis. Arch. Microbiol., 184 (4), 249-57, 2005.
    • (2005) Arch. Microbiol. , vol.184 , Issue.4 , pp. 249-257
    • Lee, K.M.1    Lee, C.K.2    Choi, S.U.3    Park, H.R.4    Kitani, S.5    Nihira, T.6    Hwang, Y.I.7
  • 85
    • 2442687980 scopus 로고    scopus 로고
    • Cloning and functional analysis by gene disruption of a gene encoding a gamma-butyrolactone autoregulator receptor from Kitasatospora setae
    • Choi, S. U., Lee, C. K., Hwang, Y. I., Kinoshita, H., and Nihira, T. Cloning and functional analysis by gene disruption of a gene encoding a gamma-butyrolactone autoregulator receptor from Kitasatospora setae. J. Bacteriol., 186 (11), 3423-30, 2004.
    • (2004) J. Bacteriol. , vol.186 , Issue.11 , pp. 3423-3430
    • Choi, S.U.1    Lee, C.K.2    Hwang, Y.I.3    Kinoshita, H.4    Nihira, T.5
  • 86
    • 0035941202 scopus 로고    scopus 로고
    • Pleiotropic functions of a Streptomyces pristinaespiralis autoregulator receptor in development, antibiotic biosynthesis, and expression of a superoxide dismutase
    • Folcher, M., Gaillard, H., Nguyen, L. T., Nguyen, K. T., Lacroix, P., Bamas-Jacques, N., Rinkel, M., and Thompson, C. J. Pleiotropic functions of a Streptomyces pristinaespiralis autoregulator receptor in development, antibiotic biosynthesis, and expression of a superoxide dismutase. J. Biol. Chem., 276 (47), 44297-306, 2001.
    • (2001) J. Biol. Chem. , vol.276 , Issue.47 , pp. 44297-44306
    • Folcher, M.1    Gaillard, H.2    Nguyen, L.T.3    Nguyen, K.T.4    Lacroix, P.5    Bamas-Jacques, N.6    Rinkel, M.7    Thompson, C.J.8
  • 87
    • 0742269396 scopus 로고    scopus 로고
    • Identification by gene deletion analysis of barB as a negative regulator controlling an early process of virginiamycin biosynthesis in Streptomyces virginiae
    • Matsuno, K., Yamada, Y., Lee, C. K., and Nihira, T. Identification by gene deletion analysis of barB as a negative regulator controlling an early process of virginiamycin biosynthesis in Streptomyces virginiae. Arch. Microbiol., 181 (1), 52-9, 2004.
    • (2004) Arch. Microbiol. , vol.181 , Issue.1 , pp. 52-59
    • Matsuno, K.1    Yamada, Y.2    Lee, C.K.3    Nihira, T.4
  • 88
    • 0033200371 scopus 로고    scopus 로고
    • Multiple regulatory genes in the tylosin biosynthetic cluster of Streptomyces fradiae
    • Bate, N., Butler, A. R., Gandecha, A. R., and Cundliffe, E. Multiple regulatory genes in the tylosin biosynthetic cluster of Streptomyces fradiae. Chem. Biol., 6 (9), 617-24, 1999.
    • (1999) Chem. Biol. , vol.6 , Issue.9 , pp. 617-624
    • Bate, N.1    Butler, A.R.2    Gandecha, A.R.3    Cundliffe, E.4
  • 89
    • 9644257510 scopus 로고    scopus 로고
    • Positive control of tylosin biosynthesis: Pivotal role of TylR
    • Stratigopoulos, G., Bate, N., and Cundliffe, E. Positive control of tylosin biosynthesis: pivotal role of TylR. Mol. Microbiol., 54 (5), 1326-34, 2004.
    • (2004) Mol. Microbiol. , vol.54 , Issue.5 , pp. 1326-1334
    • Stratigopoulos, G.1    Bate, N.2    Cundliffe, E.3
  • 90
    • 0036008104 scopus 로고    scopus 로고
    • Expression analysis of the tylosin-biosynthetic gene cluster: Pivotal regulatory role of the tylQ product
    • Stratigopoulos, G. and Cundliffe, E. Expression analysis of the tylosin-biosynthetic gene cluster: pivotal regulatory role of the tylQ product. Chem. Biol., 9 (1), 71-8, 2002.
    • (2002) Chem. Biol. , vol.9 , Issue.1 , pp. 71-78
    • Stratigopoulos, G.1    Cundliffe, E.2
  • 91
    • 0036166719 scopus 로고    scopus 로고
    • Differential roles of two SARP-encoding regulatory genes during tylosin biosynthesis
    • Bate, N., Stratigopoulos, G., and Cundliffe, E. Differential roles of two SARP-encoding regulatory genes during tylosin biosynthesis. Mol. Microbiol., 43 (2), 449-58, 2002.
    • (2002) Mol. Microbiol. , vol.43 , Issue.2 , pp. 449-458
    • Bate, N.1    Stratigopoulos, G.2    Cundliffe, E.3
  • 92
    • 0034011484 scopus 로고    scopus 로고
    • Identification of an AfsA homologue (BarX) from Streptomyces virginiae as a pleiotropic regulator controlling autoregulator biosynthesis, virginiamycin biosynthesis and virginiamycin M1 resistance
    • Kawachi, R., Akashi, T., Kamitani, Y., Sy, A., Wangchaisoonthorn, U., Nihira, T., and Yamada, Y. Identification of an AfsA homologue (BarX) from Streptomyces virginiae as a pleiotropic regulator controlling autoregulator biosynthesis, virginiamycin biosynthesis and virginiamycin M1 resistance. Mol. Microbiol., 36 (2), 302-13, 2000.
    • (2000) Mol. Microbiol. , vol.36 , Issue.2 , pp. 302-313
    • Kawachi, R.1    Akashi, T.2    Kamitani, Y.3    Sy, A.4    Wangchaisoonthorn, U.5    Nihira, T.6    Yamada, Y.7
  • 93
    • 0036724816 scopus 로고    scopus 로고
    • Bars1, a gene for biosynthesis of a gamma-butyrolactone autoregulator, a microbial signaling molecule eliciting antibiotic production in Streptomyces species
    • Shikura, N., Yamamura, J., and Nihira, T. barS1, a gene for biosynthesis of a gamma-butyrolactone autoregulator, a microbial signaling molecule eliciting antibiotic production in Streptomyces species. J. Bacteriol., 184 (18), 5151-57, 2002.
    • (2002) J. Bacteriol. , vol.184 , Issue.18 , pp. 5151-5157
    • Shikura, N.1    Yamamura, J.2    Nihira, T.3
  • 94
    • 4744343551 scopus 로고    scopus 로고
    • PI factor, a novel type quorumsensing inducer elicits pimaricin production in Streptomyces natalensis
    • Recio, E., Colinas, A., Rumbero, A., Aparicio, J. F., and Martin, J. F. PI factor, a novel type quorumsensing inducer elicits pimaricin production in Streptomyces natalensis. J. Biol. Chem., 279 (40), 41586-93, 2004.
    • (2004) J. Biol. Chem. , vol.279 , Issue.40 , pp. 41586-41593
    • Recio, E.1    Colinas, A.2    Rumbero, A.3    Aparicio, J.F.4    Martin, J.F.5
  • 95
    • 0032875632 scopus 로고    scopus 로고
    • A Streptomyces coelicolor antibiotic regulatory gene, absB, encodes an RNase III homolog
    • Price, B., Adamidis, T., Kong, R., and Champness, W. A Streptomyces coelicolor antibiotic regulatory gene, absB, encodes an RNase III homolog. J. Bacteriol., 181 (19), 6142-51, 1999.
    • (1999) J. Bacteriol. , vol.181 , Issue.19 , pp. 6142-6151
    • Price, B.1    Adamidis, T.2    Kong, R.3    Champness, W.4
  • 96
    • 0033817023 scopus 로고    scopus 로고
    • A single amino acid substitution in region 1.2 of the principal sigma factor of Streptomyces coelicolor A3(2) results in pleiotropic loss of antibiotic production
    • Aigle, B., Wietzorrek, A., Takano, E., and Bibb, M. J. A single amino acid substitution in region 1.2 of the principal sigma factor of Streptomyces coelicolor A3(2) results in pleiotropic loss of antibiotic production. Mol. Microbiol., 37 (5), 995-1004, 2000.
    • (2000) Mol. Microbiol. , vol.37 , Issue.5 , pp. 995-1004
    • Aigle, B.1    Wietzorrek, A.2    Takano, E.3    Bibb, M.J.4
  • 97
    • 0142043311 scopus 로고    scopus 로고
    • Putative anti-anti-sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor
    • Bignell, D. R., Lau, L. H., Colvin, K. R., and Leskiw, B. K. The putative anti-anti-sigma factor BldG is post-translationally modified by phosphorylation in Streptomyces coelicolor. FEMS Microbiol. Lett., 225 (1), 93-9, 2003.
    • (2003) FEMS Microbiol. Lett. , vol.225 , Issue.1 , pp. 93-99
    • Bignell, D.R.1    Lau, L.H.2    Colvin, K.R.3    Leskiw, B.K.4
  • 98
    • 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., Tahlan, K., Colvin, K. R., Jensen, S. E., and Leskiw, B. K. 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 (4), 1529-41, 2005.
    • (2005) Antimicrob., Agents Chemother. , vol.49 , Issue.4 , pp. 1529-1541
    • Bignell, D.R.1    Tahlan, K.2    Colvin, K.R.3    Jensen, S.E.4    Leskiw, B.K.5
  • 99
    • 0026029699 scopus 로고
    • TTA codons in some genes prevent their expression in a class of developmental, antibiotic-negative, Streptomyces mutants
    • Leskiw, B. K., Lawlor, E. J., Fernandez-Abalos, J. M., and Chater, K. F. TTA codons in some genes prevent their expression in a class of developmental, antibiotic-negative, Streptomyces mutants. Proc. Natl. Acad. Sci. USA, 88 (6), 2461-5, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.6 , pp. 2461-2465
    • Leskiw, B.K.1    Lawlor, E.J.2    Fernandez-Abalos, J.M.3    Chater, K.F.4
  • 100
    • 0025899144 scopus 로고
    • Act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces
    • Fernandez-Moreno, M. A., Caballero, J. L., Hopwood, D. A., and Malpartida, F. The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces. Cell, 66 (4), 769-80, 1991.
    • (1991) Cell , vol.66 , Issue.4 , pp. 769-780
    • Fernandez-Moreno, M.A.1    Caballero, J.L.2    Hopwood, D.A.3    Malpartida, F.4
  • 101
    • 0027457408 scopus 로고
    • Accumulation of bldA-specified tRNA is temporally regulated in Streptomyces coelicolor A3(2)
    • Leskiw, B. K., Mah, R., Lawlor, E. J., and Chater, K. F. Accumulation of bldA-specified tRNA is temporally regulated in Streptomyces coelicolor A3(2). J. Bacteriol., 175 (7), 1995-2005, 1993.
    • (1993) J. Bacteriol. , vol.175 , Issue.7 , pp. 1995-2005
    • Leskiw, B.K.1    Mah, R.2    Lawlor, E.J.3    Chater, K.F.4
  • 102
    • 0026597059 scopus 로고
    • Codon usage in the G+C-rich Streptomyces genome
    • Wright, F. and Bibb, M. J. Codon usage in the G+C-rich Streptomyces genome. Gene, 113 (1), 55-65, 1992.
    • (1992) Gene , vol.113 , Issue.1 , pp. 55-65
    • Wright, F.1    Bibb, M.J.2
  • 103
    • 33645057187 scopus 로고    scopus 로고
    • Expression of the regulatory protein LndI for landomycin E production in Streptomyces globisporus 1912 is controlled by the availability of tRNA for the rare UUA codon
    • Rebets, Y. V., Ostash, B. O., Fukuhara, M., Nakamura, T., and Fedorenko, V. O. Expression of the regulatory protein LndI for landomycin E production in Streptomyces globisporus 1912 is controlled by the availability of tRNA for the rare UUA codon. FEMS Microbiol. Lett. 256 (1), 30-7, 2006.
    • (2006) FEMS Microbiol. Lett. , vol.256 , Issue.1 , pp. 30-37
    • Rebets, Y.V.1    Ostash, B.O.2    Fukuhara, M.3    Nakamura, T.4    Fedorenko, V.O.5
  • 104
    • 0036176756 scopus 로고    scopus 로고
    • Regulation of the Streptomyces coelicolor calcium-dependent antibiotic by absA, encoding a cluster-linked two-component system
    • Ryding, N. J., Anderson, T. B., and Champness, W. C. Regulation of the Streptomyces coelicolor calcium-dependent antibiotic by absA, encoding a cluster-linked two-component system. J. Bacteriol. 184 (3), 794-805, 2002.
    • (2002) J. Bacteriol. , vol.184 , Issue.3 , pp. 794-805
    • Ryding, N.J.1    Anderson, T.B.2    Champness, W.C.3
  • 106
    • 0033118267 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria
    • Stulke, J. and Hillen, W. Carbon catabolite repression in bacteria. Curr. Opin. Microbiol., 2 (2), 195-201, 1999.
    • (1999) Curr. Opin. Microbiol. , vol.2 , Issue.2 , pp. 195-201
    • Stulke, J.1    Hillen, W.2
  • 108
    • 0028870129 scopus 로고
    • Identification and characterization of phosphoenolpyruvate: Fructose phosphotransferase systems in three Streptomyces species
    • Titgemeyer, F., Walkenhorst, J., Reizer, J., Stuiver, M. H., Cui, X., and Saier, M. H., Jr. Identification and characterization of phosphoenolpyruvate: fructose phosphotransferase systems in three Streptomyces species. Microbiology, 141 (Pt 1), 51-8, 1995.
    • (1995) Microbiology , vol.141 , pp. 51-58
    • Titgemeyer, F.1    Walkenhorst, J.2    Reizer, J.3    Stuiver, M.H.4    Cui, X.5    Saier, M.H.6
  • 111
    • 2442435708 scopus 로고    scopus 로고
    • Glucose kinase alone cannot be responsible for carbon source regulation in Streptomyces peucetius var. caesius
    • Ramos, I., Guzman, S., Escalante, L., Imriskova, I., Rodriguez-Sanoja, R., Sanchez, S., and Langley, E. Glucose kinase alone cannot be responsible for carbon source regulation in Streptomyces peucetius var. caesius. Res. Microbiol., 155 (4), 267-74, 2004.
    • (2004) Res. Microbiol. , vol.155 , Issue.4 , pp. 267-274
    • Ramos, I.1    Guzman, S.2    Escalante, L.3    Imriskova, I.4    Rodriguez-Sanoja, R.5    Sanchez, S.6    Langley, E.7
  • 112
    • 33644517930 scopus 로고    scopus 로고
    • Bacterial small-molecule signaling pathways
    • Camilli, A. and Bassler, B. L. Bacterial small-molecule signaling pathways. Science, 311 (5764), 1113-36, 2006.
    • (2006) Science , vol.311 , Issue.5764 , pp. 1113-1136
    • Camilli, A.1    Bassler, B.L.2
  • 113
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., Lengeler, J. W., and Jacobson, G. R. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev., 57 (3), 543-94, 1993.
    • (1993) Microbiol. Rev. , vol.57 , Issue.3 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 114
    • 0031719202 scopus 로고    scopus 로고
    • Pleiotropic effects of cAMP on germination, antibiotic biosynthesis and morphological development in Streptomyces coelicolor
    • Susstrunk, U., Pidoux, J., Taubert, S., Ullmann, A., and Thompson, C. J. Pleiotropic effects of cAMP on germination, antibiotic biosynthesis and morphological development in Streptomyces coelicolor. Mol. Microbiol., 30 (1), 33-46, 1998.
    • (1998) Mol. Microbiol. , vol.30 , Issue.1 , pp. 33-46
    • Susstrunk, U.1    Pidoux, J.2    Taubert, S.3    Ullmann, A.4    Thompson, C.J.5
  • 115
    • 0019992015 scopus 로고
    • Catabolite repression in Streptomyces venezuelae. Induction of betagalactosidase, chloramphenicol production, and intracellular cyclic adenosine 3',5'-monophosphate concentrations
    • Chatterjee, S. and Vining, L. C. Catabolite repression in Streptomyces venezuelae. Induction of betagalactosidase, chloramphenicol production, and intracellular cyclic adenosine 3',5'-monophosphate concentrations. Can. J. Microbiol., 28 (3), 311-7, 1982.
    • (1982) Can. J. Microbiol. , vol.28 , Issue.3 , pp. 311-317
    • Chatterjee, S.1    Vining, L.C.2
  • 116
    • 0030922782 scopus 로고    scopus 로고
    • Ppgpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation
    • Chakraburtty, R. and Bibb, M. The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation. J. Bacteriol., 179 (18), 5854-61, 1997.
    • (1997) J. Bacteriol. , vol.179 , Issue.18 , pp. 5854-5861
    • Chakraburtty, R.1    Bibb, M.2
  • 117
    • 0035036356 scopus 로고    scopus 로고
    • Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2)
    • Sun, J., Hesketh, A., and Bibb, M. Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2). J. Bacteriol., 183 (11), 3488-98, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.11 , pp. 3488-3498
    • Sun, J.1    Hesketh, A.2    Bibb, M.3
  • 118
    • 4644349000 scopus 로고    scopus 로고
    • Cephamycin C production is regulated by relA and rsh genes in Streptomyces clavuligerus ATCC27064
    • Jin, W., Kim, H. K., Kim, J. Y., Kang, S. G., Lee, S. H., and Lee, K. J. Cephamycin C production is regulated by relA and rsh genes in Streptomyces clavuligerus ATCC27064. J. Biotechnol., 114 (1-2), 81-7, 2004.
    • (2004) J. Biotechnol. , vol.114 , Issue.1-2 , pp. 81-87
    • Jin, W.1    Kim, H.K.2    Kim, J.Y.3    Kang, S.G.4    Lee, S.H.5    Lee, K.J.6
  • 119
    • 2942590392 scopus 로고    scopus 로고
    • Two relA/spoT homologous genes are involved in the morphological and physiological differentiation of Streptomyces clavuligerus
    • Jin, W., Ryu, Y. G., Kang, S. G., Kim, S. K., Saito, N., Ochi, K., Lee, S. H., and Lee, K. J. Two relA/spoT homologous genes are involved in the morphological and physiological differentiation of Streptomyces clavuligerus. Microbiology, 150 (Pt 5), 1485-93, 2004.
    • (2004) Microbiology , vol.150 , pp. 1485-1493
    • Jin, W.1    Ryu, Y.G.2    Kang, S.G.3    Kim, S.K.4    Saito, N.5    Ochi, K.6    Lee, S.H.7    Lee, K.J.8
  • 120
    • 0035181472 scopus 로고    scopus 로고
    • Induction of ppGpp synthesis in Streptomyces coelicolor A3(2) grown under conditions of nutritional sufficiency elicits actII-ORF4 transcription and actinorhodin biosynthesis
    • Hesketh, A., Sun, J., and Bibb, M. Induction of ppGpp synthesis in Streptomyces coelicolor A3(2) grown under conditions of nutritional sufficiency elicits actII-ORF4 transcription and actinorhodin biosynthesis. Mol. Microbiol., 39 (1), 136-44, 2001.
    • (2001) Mol. Microbiol. , vol.39 , Issue.1 , pp. 136-144
    • Hesketh, A.1    Sun, J.2    Bibb, M.3
  • 121
    • 0036460093 scopus 로고    scopus 로고
    • A rifampicin resistance mutation in the rpoB gene confers ppGpp-independent antibiotic production in Streptomyces coelicolor A3(2)
    • Xu, J., Tozawa, Y., Lai, C., Hayashi, H., and Ochi, K. A rifampicin resistance mutation in the rpoB gene confers ppGpp-independent antibiotic production in Streptomyces coelicolor A3(2). Mol. Genet. Genomics, 268 (2), 179-89, 2002.
    • (2002) Mol. Genet. Genomics , vol.268 , Issue.2 , pp. 179-189
    • Xu, J.1    Tozawa, Y.2    Lai, C.3    Hayashi, H.4    Ochi, K.5
  • 122
    • 0036299643 scopus 로고    scopus 로고
    • Activation of antibiotic biosynthesis by specified mutations in the rpoB gene (encoding the RNA polymerase beta subunit) of Streptomyces lividans
    • Hu, H., Zhang, Q., and Ochi, K. Activation of antibiotic biosynthesis by specified mutations in the rpoB gene (encoding the RNA polymerase beta subunit) of Streptomyces lividans. J. Bacteriol., 184 (14), 3984-91, 2002.
    • (2002) J. Bacteriol. , vol.184 , Issue.14 , pp. 3984-3991
    • Hu, H.1    Zhang, Q.2    Ochi, K.3
  • 123
    • 0032914702 scopus 로고    scopus 로고
    • Phosphate control of oxytetracycline production by Streptomyces rimosus is at the level of transcription from promoters overlapped by tandem repeats similar to those of the DNA-binding sites of the OmpR family
    • McDowall, K. J., Thamchaipenet, A., and Hunter, I. S. Phosphate control of oxytetracycline production by Streptomyces rimosus is at the level of transcription from promoters overlapped by tandem repeats similar to those of the DNA-binding sites of the OmpR family. J. Bacteriol., 181 (10), 3025-32, 1999.
    • (1999) J. Bacteriol. , vol.181 , Issue.10 , pp. 3025-3032
    • McDowall, K.J.1    Thamchaipenet, A.2    Hunter, I.S.3
  • 124
    • 0025465341 scopus 로고
    • Phosphate control sequences involved in transcriptional regulation of antibiotic biosynthesis
    • Liras, P., Asturias, J. A., and Martin, J. F. Phosphate control sequences involved in transcriptional regulation of antibiotic biosynthesis. Trends Biotechnol., 8 (7), 184-89, 1990.
    • (1990) Trends Biotechnol. , vol.8 , Issue.7 , pp. 184-189
    • Liras, P.1    Asturias, J.A.2    Martin, J.F.3
  • 125
    • 19944370498 scopus 로고    scopus 로고
    • Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: Identification of PHO boxes
    • Sola-Landa, A., Rodriguez-Garcia, A., Franco-Dominguez, E., and Martin, J. F. Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: identification of PHO boxes. Mol. Microbiol., 56 (5), 1373-85, 2005.
    • (2005) Mol. Microbiol. , vol.56 , Issue.5 , pp. 1373-1385
    • Sola-Landa, A.1    Rodriguez-Garcia, A.2    Franco-Dominguez, E.3    Martin, J.F.4
  • 126
    • 0036231769 scopus 로고    scopus 로고
    • Polyphosphate kinase plays a negative role in the control of antibiotic production in Streptomyces lividans
    • Chouayekh, H. and Virolle, M. J. The polyphosphate kinase plays a negative role in the control of antibiotic production in Streptomyces lividans. Mol. Microbiol., 43 (4), 919-30, 2002.
    • (2002) Mol. Microbiol. , vol.43 , Issue.4 , pp. 919-930
    • Chouayekh, H.1    Virolle, M.J.2
  • 128
    • 0037226133 scopus 로고    scopus 로고
    • Enhanced expression of S-adenosylmethionine synthetase causes overproduction of actinorhodin in Streptomyces coelicolor A3(2)
    • Okamoto, S., Lezhava, A., Hosaka, T., Okamoto-Hosoya, Y., and Ochi, K. Enhanced expression of S-adenosylmethionine synthetase causes overproduction of actinorhodin in Streptomyces coelicolor A3(2). J. Bacteriol., 185 (2), 601-9, 2003.
    • (2003) J. Bacteriol. , vol.185 , Issue.2 , pp. 601-609
    • Okamoto, S.1    Lezhava, A.2    Hosaka, T.3    Okamoto-Hosoya, Y.4    Ochi, K.5
  • 129
    • 0037224691 scopus 로고    scopus 로고
    • Accumulation of S-adenosyl-L-methionine enhances production of actinorhodin but inhibits sporulation in Streptomyces lividans TK23
    • Kim, D. J., Huh, J. H., Yang, Y. Y., Kang, C. M., Lee, I. H., Hyun, C. G., Hong, S. K., and Suh, J. W. Accumulation of S-adenosyl-L-methionine enhances production of actinorhodin but inhibits sporulation in Streptomyces lividans TK23. J. Bacteriol., 185 (2), 592-600, 2003.
    • (2003) J. Bacteriol. , vol.185 , Issue.2 , pp. 592-600
    • Kim, D.J.1    Huh, J.H.2    Yang, Y.Y.3    Kang, C.M.4    Lee, I.H.5    Hyun, C.G.6    Hong, S.K.7    Suh, J.W.8
  • 130
    • 4444374760 scopus 로고    scopus 로고
    • Effect of S-adenosylmethionine on antibiotic production in Streptomyces griseus and Streptomyces griseuoflavus
    • Natsumi, S., Kazuhiko, K., Jun, X., Okamoto, X., and Ochi, K. Effect of S-adenosylmethionine on antibiotic production in Streptomyces griseus and Streptomyces griseuoflavus. Actinomyceteology, 17, 47-49, 2003.
    • (2003) Actinomyceteology , vol.17 , pp. 47-49
    • Natsumi, S.1    Kazuhiko, K.2    Jun, X.3    Okamoto, X.4    Ochi, K.5
  • 132
    • 0034746689 scopus 로고    scopus 로고
    • A sigmaB-like factor responsible for carotenoid biosynthesis in Streptomyces griseus
    • Lee, H. S., Ohnishi, Y., and Horinouchi, S. A sigmaB-like factor responsible for carotenoid biosynthesis in Streptomyces griseus. J. Mol. Microbiol. Biotechnol., 3 (1), 95-101, 2001.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , Issue.1 , pp. 95-101
    • Lee, H.S.1    Ohnishi, Y.2    Horinouchi, S.3
  • 133
    • 14244262147 scopus 로고    scopus 로고
    • Light-induced carotenogenesis in Streptomyces coelicolor A3(2): Identification of an extracytoplasmic function sigma factor that directs photodependent transcription of the carotenoid biosynthesis gene cluster
    • Takano, H., Obitsu, S., Beppu, T., and Ueda, K. Light-induced carotenogenesis in Streptomyces coelicolor A3(2): identification of an extracytoplasmic function sigma factor that directs photodependent transcription of the carotenoid biosynthesis gene cluster. J. Bacteriol., 187 (5), 1825-32, 2005.
    • (2005) J. Bacteriol. , vol.187 , Issue.5 , pp. 1825-1832
    • Takano, H.1    Obitsu, S.2    Beppu, T.3    Ueda, K.4
  • 134
    • 30844464360 scopus 로고    scopus 로고
    • Genetic control for light-induced carotenoid production in non-phototrophic bacteria
    • Takano, H., Asker, D., Beppu, T., and Ueda, K. Genetic control for light-induced carotenoid production in non-phototrophic bacteria. J. Ind. Microbiol. Biotechnol., 33 (2), 88-93, 2006.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , Issue.2 , pp. 88-93
    • Takano, H.1    Asker, D.2    Beppu, T.3    Ueda, K.4
  • 135
    • 33644907519 scopus 로고    scopus 로고
    • Rethinking ‘secondary’ metabolism: Physiological roles for phenazine antibiotics
    • Price-Whelan, A., Dietrich, L. E., and Newman, D. K. Rethinking ‘secondary’ metabolism: physiological roles for phenazine antibiotics. Nat. Chem. Biol., 2 (2), 71-78, 2006.
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.2 , pp. 71-78
    • Price-Whelan, A.1    Dietrich, L.E.2    Newman, D.K.3
  • 136
    • 0037378570 scopus 로고    scopus 로고
    • Identification, timing, and signal specificity of Pseudomonas aeruginosa quorum-controlled genes: A transcriptome analysis
    • Schuster, M., Lostroh, C. P., Ogi, T., and Greenberg, E. P. Identification, timing, and signal specificity of Pseudomonas aeruginosa quorum-controlled genes: a transcriptome analysis. J. Bacteriol., 185 (7), 2066-79, 2003.
    • (2003) J. Bacteriol. , vol.185 , Issue.7 , pp. 2066-2079
    • Schuster, M.1    Lostroh, C.P.2    Ogi, T.3    Greenberg, E.P.4
  • 137
    • 0037377827 scopus 로고    scopus 로고
    • Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: Effects of growth phase and environment
    • Wagner, V. E., Bushnell, D., Passador, L., Brooks, A. I., and Iglewski, B. H. Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: effects of growth phase and environment. J. Bacteriol., 185 (7), 2080-95, 2003.
    • (2003) J. Bacteriol. , vol.185 , Issue.7 , pp. 2080-2095
    • Wagner, V.E.1    Bushnell, D.2    Passador, L.3    Brooks, A.I.4    Iglewski, B.H.5
  • 138
    • 0029831296 scopus 로고    scopus 로고
    • A hierarchical quorum-sensing cascade in Pseudomonas aeruginosa links the transcriptional activators LasR and RhIR (VsmR) to expression of the stationary-phase sigma factor RpoS
    • Latifi, A., Foglino, M., Tanaka, K., Williams, P., and Lazdunski, A. A hierarchical quorum-sensing cascade in Pseudomonas aeruginosa links the transcriptional activators LasR and RhIR (VsmR) to expression of the stationary-phase sigma factor RpoS. Mol. Microbiol., 21 (6), 1137-46, 1996.
    • (1996) Mol. Microbiol. , vol.21 , Issue.6 , pp. 1137-1146
    • Latifi, A.1    Foglino, M.2    Tanaka, K.3    Williams, P.4    Lazdunski, A.5
  • 139
    • 0346492813 scopus 로고    scopus 로고
    • Dueling quorum sensing systems in Pseudomonas aeruginosa control the production of the Pseudomonas quinolone signal (PQS)
    • McGrath, S., Wade, D. S., and Pesci, E. C. Dueling quorum sensing systems in Pseudomonas aeruginosa control the production of the Pseudomonas quinolone signal (PQS). FEMS Microbiol., Lett 230 (1), 27-34, 2004.
    • (2004) FEMS Microbiol., Lett , vol.230 , Issue.1 , pp. 27-34
    • McGrath, S.1    Wade, D.S.2    Pesci, E.C.3
  • 140
    • 0035807973 scopus 로고    scopus 로고
    • A quorum sensing-associated virulence gene of Pseudomonas aeruginosa encodes a LysR-like transcription regulator with a unique self-regulatory mechanism
    • Cao, H., Krishnan, G., Goumnerov, B., Tsongalis, J., Tompkins, R., and Rahme, L. G. A quorum sensing-associated virulence gene of Pseudomonas aeruginosa encodes a LysR-like transcription regulator with a unique self-regulatory mechanism. Proc. Natl. Acad. Sci. USA, 98 (25), 14613-18, 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.25 , pp. 14613-14618
    • Cao, H.1    Krishnan, G.2    Goumnerov, B.3    Tsongalis, J.4    Tompkins, R.5    Rahme, L.G.6
  • 141
  • 142
    • 0141595872 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa quinolone signal molecule overcomes the cell density-dependency of the quorum sensing hierarchy, regulates rhl-dependent genes at the onset of stationary phase and can be produced in the absence of LasR
    • Diggle, S. P., Winzer, K., Chhabra, S. R., Worrall, K. E., Camara, M., and Williams, P. The Pseudomonas aeruginosa quinolone signal molecule overcomes the cell density-dependency of the quorum sensing hierarchy, regulates rhl-dependent genes at the onset of stationary phase and can be produced in the absence of LasR. Mol. Microbiol., 50 (1), 29-43, 2003.
    • (2003) Mol. Microbiol. , vol.50 , Issue.1 , pp. 29-43
    • Diggle, S.P.1    Winzer, K.2    Chhabra, S.R.3    Worrall, K.E.4    Camara, M.5    Williams, P.6
  • 144
    • 0036889038 scopus 로고    scopus 로고
    • Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa
    • Gallagher, L. A., McKnight, S. L., Kuznetsova, M. S., Pesci, E. C., and Manoil, C. Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa. J. Bacteriol., 184 (23), 6472-80, 2002.
    • (2002) J. Bacteriol. , vol.184 , Issue.23 , pp. 6472-6480
    • Gallagher, L.A.1    McKnight, S.L.2    Kuznetsova, M.S.3    Pesci, E.C.4    Manoil, C.5
  • 145
    • 0842320989 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa 4-hydroxy-2-alkylquinolines (HAQs) reveals a role for 4-hydroxy-2-heptylquinoline in cell-to-cell communication
    • Deziel, E., Lepine, F., Milot, S., He, J., Mindrinos, M. N., Tompkins, R. G., and Rahme, L. G. Analysis of Pseudomonas aeruginosa 4-hydroxy-2-alkylquinolines (HAQs) reveals a role for 4-hydroxy-2-heptylquinoline in cell-to-cell communication. Proc. Natl. Acad. Sci. USA, 101 (5), 1339-44, 2004.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.5 , pp. 1339-1344
    • Deziel, E.1    Lepine, F.2    Milot, S.3    He, J.4    Mindrinos, M.N.5    Tompkins, R.G.6    Rahme, L.G.7
  • 146
    • 25144456544 scopus 로고    scopus 로고
    • Membrane vesicles traffic signals and facilitate group activities in a prokaryote
    • Mashburn, L. M. and Whiteley, M. Membrane vesicles traffic signals and facilitate group activities in a prokaryote. Nature, 437 (7057), 422-5, 2005.
    • (2005) Nature , vol.437 , Issue.7057 , pp. 422-425
    • Mashburn, L.M.1    Whiteley, M.2
  • 147
    • 0035685204 scopus 로고    scopus 로고
    • Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1
    • Mavrodi, D. V., Bonsall, R. F., Delaney, S. M., Soule, M. J., Phillips, G., and Thomashow, L. S. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J. Bacteriol., 183 (21), 6454-65, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.21 , pp. 6454-6465
    • Mavrodi, D.V.1    Bonsall, R.F.2    Delaney, S.M.3    Soule, M.J.4    Phillips, G.5    Thomashow, L.S.6
  • 148
    • 33644862308 scopus 로고    scopus 로고
    • 4-quinolone signalling in Pseudomonas aeruginosa: Old molecules, new perspectives
    • Diggle, S. P., Cornelis, P., Williams, P., and Camara, M. 4-quinolone signalling in Pseudomonas aeruginosa: old molecules, new perspectives. Int. J. Med. Microbiol., 296 (2-3), 83-91, 2006.
    • (2006) Int. J. Med. Microbiol. , vol.296 , Issue.2-3 , pp. 83-91
    • Diggle, S.P.1    Cornelis, P.2    Williams, P.3    Camara, M.4
  • 149
    • 0037385875 scopus 로고    scopus 로고
    • Interactions of the quorum sensing regulator QscR: Interaction with itself and the other regulators of Pseudomonas aeruginosa LasR and RhlR
    • Ledgham, F., Ventre, I., Soscia, C., Foglino, M., Sturgis, J. N., and Lazdunski, A. Interactions of the quorum sensing regulator QscR: interaction with itself and the other regulators of Pseudomonas aeruginosa LasR and RhlR. Mol. Microbiol., 48 (1), 199-210, 2003.
    • (2003) Mol. Microbiol. , vol.48 , Issue.1 , pp. 199-210
    • Ledgham, F.1    Ventre, I.2    Soscia, C.3    Foglino, M.4    Sturgis, J.N.5    Lazdunski, A.6
  • 150
    • 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., Zurita, J., Ferreras, J. A., Worgall, S., Larone, D. H., Shi, L., Campagne, F., and Quadri, L. E. Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response. Infect. Immun., 73 (5), 2958-66, 2005.
    • (2005) Infect. Immun. , vol.73 , Issue.5 , 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.8
  • 151
    • 0033598693 scopus 로고    scopus 로고
    • Identification of genes controlled by quorum sensing in Pseudomonas aeruginosa
    • Whiteley, M., Lee, K. M., and Greenberg, E. P. Identification of genes controlled by quorum sensing in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA, 96 (24), 13904-9, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.24 , pp. 13904-13909
    • Whiteley, M.1    Lee, K.M.2    Greenberg, E.P.3
  • 152
    • 0036667424 scopus 로고    scopus 로고
    • Characterization of a new efflux pump, MexGHI-OpmD, from Pseudomonas aeruginosa that confers resistance to vanadium
    • Aendekerk, S., Ghysels, B., Cornelis, P., and Baysse, C. Characterization of a new efflux pump, MexGHI-OpmD, from Pseudomonas aeruginosa that confers resistance to vanadium. Microbiology, 148 (Pt 8), 2371-81, 2002.
    • (2002) Microbiology , vol.148 , pp. 2371-2381
    • Aendekerk, S.1    Ghysels, B.2    Cornelis, P.3    Baysse, C.4
  • 153
    • 17644369248 scopus 로고    scopus 로고
    • MexGHI-OpmD multidrug efflux pump controls growth, antibiotic susceptibility and virulence in Pseudomonas aeruginosa via 4-quinolone-dependent cell-to-cell communication
    • Aendekerk, S., Diggle, S. P., Song, Z., Hoiby, N., Cornelis, P., Williams, P., and Camara, M. The MexGHI-OpmD multidrug efflux pump controls growth, antibiotic susceptibility and virulence in Pseudomonas aeruginosa via 4-quinolone-dependent cell-to-cell communication. Microbiology, 151 (Pt 4), 1113-25, 2005.
    • (2005) Microbiology , vol.151 , pp. 1113-1125
    • Aendekerk, S.1    Diggle, S.P.2    Song, Z.3    Hoiby, N.4    Cornelis, P.5    Williams, P.6    Camara, M.7
  • 154
    • 0032989877 scopus 로고    scopus 로고
    • Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals
    • Pearson, J. P., Van Delden, C., and Iglewski, B. H. Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals. J. Bacteriol., 181 (4), 1203-10, 1999.
    • (1999) J. Bacteriol. , vol.181 , Issue.4 , pp. 1203-1210
    • Pearson, J.P.1    Van Delden, C.2    Iglewski, B.H.3
  • 155
    • 0034871821 scopus 로고    scopus 로고
    • Overexpression of the MexEF-OprN multidrug efflux system affects cell-to-cell signaling in Pseudomonas aeruginosa
    • Kohler, T., van Delden, C., Curty, L. K., Hamzehpour, M. M., and Pechere, J. C. Overexpression of the MexEF-OprN multidrug efflux system affects cell-to-cell signaling in Pseudomonas aeruginosa. J. Bacteriol., 183 (18), 5213-22, 2001.
    • (2001) J. Bacteriol. , vol.183 , Issue.18 , pp. 5213-5222
    • Kohler, T.1    van Delden, C.2    Curty, L.K.3    Hamzehpour, M.M.4    Pechere, J.C.5
  • 156
    • 0018818958 scopus 로고
    • Mechanism of the antibiotic action pyocyanine
    • Hassan, H. M. and Fridovich, I. Mechanism of the antibiotic action pyocyanine. J. Bacteriol., 141 (1), 156-63, 1980.
    • (1980) J. Bacteriol. , vol.141 , Issue.1 , pp. 156-163
    • Hassan, H.M.1    Fridovich, I.2


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