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Volumn 11, Issue 3, 2004, Pages 357-366

Starter unit choice determines the production of two tetraene macrolides, rimocidin and CE-108, in Streptomyces diastaticus var. 108

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); STREPTOMYCES; STREPTOMYCES DIASTATICUS;

EID: 6444244005     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.02.017     Document Type: Article
Times cited : (60)

References (43)
  • 4
    • 0035677498 scopus 로고    scopus 로고
    • Genetic approaches for controlling ratios of related polyketide products in fermentation processes
    • Cropp A., Chen S., Liu H., Zhang W., Reynolds K.A. Genetic approaches for controlling ratios of related polyketide products in fermentation processes. J. Ind. Microbiol. Biotechnol. 27:2001;368-377.
    • (2001) J. Ind. Microbiol. Biotechnol. , vol.27 , pp. 368-377
    • Cropp, A.1    Chen, S.2    Liu, H.3    Zhang, W.4    Reynolds, K.A.5
  • 5
    • 0032879027 scopus 로고    scopus 로고
    • Forty years of genetics with Streptomyces: From in vivo through in vitro to in silico
    • Hopwood D.A. Forty years of genetics with Streptomyces. from in vivo through in vitro to in silico Microbiol. 145:1999;2183-2202.
    • (1999) Microbiol. , vol.145 , pp. 2183-2202
    • Hopwood, D.A.1
  • 6
    • 0025081416 scopus 로고
    • An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea
    • Cortés J., Haydock S.F., Roberts G.A., Bevitt D.J., Leadlay P.F. An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea. Nature. 348:1990;176-178.
    • (1990) Nature , vol.348 , pp. 176-178
    • Cortés, J.1    Haydock, S.F.2    Roberts, G.A.3    Bevitt, D.J.4    Leadlay, P.F.5
  • 7
    • 0026415106 scopus 로고
    • Modular organisation of genes required for complex polyketide biosynthesis
    • Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L. Modular organisation of genes required for complex polyketide biosynthesis. Science. 252:1991;675-679.
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 8
    • 0026511543 scopus 로고
    • 6-Deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme
    • Bevitt D.J., Cortes J., Haydock S.F., Leadlay P.F. 6-Deoxyerythronolide- B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme. Eur. J. Biochem. 204:1992;39-49.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 39-49
    • Bevitt, D.J.1    Cortes, J.2    Haydock, S.F.3    Leadlay, P.F.4
  • 9
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood D.A. Genetic contributions to understanding polyketide synthases. Chem. Rev. 97:1997;2465-2497.
    • (1997) Chem. Rev. , vol.97 , pp. 2465-2497
    • Hopwood, D.A.1
  • 10
    • 0002628418 scopus 로고    scopus 로고
    • Polyene antibiotics
    • W.R. Strohl. New York: Marcel Dekker
    • Gil J.A., Martín J.F. Polyene antibiotics. Strohl W.R. Biotechnology of Antibiotics. 1997;551-575 Marcel Dekker, New York.
    • (1997) Biotechnology of Antibiotics , pp. 551-575
    • Gil, J.A.1    Martín, J.F.2
  • 11
    • 0015800484 scopus 로고
    • Chemistry and biology of the polyene macrolide antibiotics
    • Hamilton-Miller J.M.T. Chemistry and biology of the polyene macrolide antibiotics. Bacteriol. Rev. 37:1973;166-196.
    • (1973) Bacteriol. Rev. , vol.37 , pp. 166-196
    • Hamilton-Miller, J.M.T.1
  • 12
    • 0022862167 scopus 로고
    • How do the polyene macrolide antibiotics affect the cellular membrane properties?
    • Bolard J. How do the polyene macrolide antibiotics affect the cellular membrane properties? Biochim. Biophys. Acta. 864:1986;257-304.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 257-304
    • Bolard, J.1
  • 16
    • 0141714803 scopus 로고
    • Rimocidin II. Oxygenation pattern of the aglycone
    • Cope A.C., Axen U., Burrows E.P. Rimocidin II. Oxygenation pattern of the aglycone. J. Am. Chem. Soc. 88:1966;4221-4227.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 4221-4227
    • Cope, A.C.1    Axen, U.2    Burrows, E.P.3
  • 19
    • 0024341196 scopus 로고
    • A vector system with temperature-sensitive replication for gene disruption and mutational cloning in streptomycetes
    • Muth G., Nubbaumer B., Wohlleben W., Puhler A. A vector system with temperature-sensitive replication for gene disruption and mutational cloning in streptomycetes. Mol. Gen. Genet. 219:1989;341-348.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 341-348
    • Muth, G.1    Nubbaumer, B.2    Wohlleben, W.3    Puhler, A.4
  • 20
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman M., Logan R., O'Brien K., Seno E.T., Rao R.N., Schoner B.E. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene. 116:1992;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
  • 21
    • 0033537959 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the 26-membered ring polyene macrolide pimaricin: A new polyketide synthase organization encoded by two subclusters separated by functionalization genes
    • Aparicio J.F., Colina A.J., Ceballos E., Martín J.F. The biosynthetic gene cluster for the 26-membered ring polyene macrolide pimaricin. a new polyketide synthase organization encoded by two subclusters separated by functionalization genes J. Biol. Chem. 274:1999;10133-10139.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10133-10139
    • Aparicio, J.F.1    Colina, A.J.2    Ceballos, E.3    Martín, J.F.4
  • 22
    • 0034047123 scopus 로고    scopus 로고
    • Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: Analysis of the gene cluster and deduction of the biosynthetic pathway
    • Brautaset T., Sekurova O.N., Sletta H., Ellingsen T.E., Strom A.R., Valla S., Zotchev S.B. Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455. analysis of the gene cluster and deduction of the biosynthetic pathway Chem. Biol. 7:2000;395-403.
    • (2000) Chem. Biol. , vol.7 , pp. 395-403
    • Brautaset, T.1    Sekurova, O.N.2    Sletta, H.3    Ellingsen, T.E.4    Strom, A.R.5    Valla, S.6    Zotchev, S.B.7
  • 23
    • 0034930476 scopus 로고    scopus 로고
    • Amphotericin biosynthesis in Streptomyces nodosus: Deductions from analysis of polyketide synthase and late genes
    • Caffrey P., Lynch S., Flood E., Finnan S., Oliynyk M. Amphotericin biosynthesis in Streptomyces nodosus. deductions from analysis of polyketide synthase and late genes Chem. Biol. 8:2001;713-723.
    • (2001) Chem. Biol. , vol.8 , pp. 713-723
    • Caffrey, P.1    Lynch, S.2    Flood, E.3    Finnan, S.4    Oliynyk, M.5
  • 25
    • 0033763409 scopus 로고    scopus 로고
    • A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis
    • Aparicio J.F., Fouces R., Mendes M.V., Olivera N., Martín J.F. A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis. Chem. Biol. 7:2000;895-905.
    • (2000) Chem. Biol. , vol.7 , pp. 895-905
    • Aparicio, J.F.1    Fouces, R.2    Mendes, M.V.3    Olivera, N.4    Martín, J.F.5
  • 26
    • 0025831899 scopus 로고
    • Occurrence and biological function of cytochrome-P450 monooxygenases in the actinomycetes
    • O'Keefe D.P., Harder P.A. Occurrence and biological function of cytochrome-P450 monooxygenases in the actinomycetes. Mol. Microbiol. 5:1991;2099-2105.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2099-2105
    • O'Keefe, D.P.1    Harder, P.A.2
  • 27
    • 0028808264 scopus 로고
    • Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli
    • Wallace K.K., Bao Z.Y., Dai H., Digate R., Schuler G., Speedie M.K., Reynolds K.A. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur. J. Biochem. 233:1995;954-962.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 954-962
    • Wallace, K.K.1    Bao, Z.Y.2    Dai, H.3    Digate, R.4    Schuler, G.5    Speedie, M.K.6    Reynolds, K.A.7
  • 28
    • 0031922404 scopus 로고    scopus 로고
    • A 7,6 kb DNA region from Streptomyces kasugaensis M338-M1 includes some genes responsible for kasugamycin biosynthesis
    • Ikeno S., Tsuji T., Higashide K., Kinoshita N., Hamada M., Hori M. A 7,6 kb DNA region from Streptomyces kasugaensis M338-M1 includes some genes responsible for kasugamycin biosynthesis. J. Antibiot. (Tokyo). 51:1998;341-352.
    • (1998) J. Antibiot. (Tokyo) , vol.51 , pp. 341-352
    • Ikeno, S.1    Tsuji, T.2    Higashide, K.3    Kinoshita, N.4    Hamada, M.5    Hori, M.6
  • 30
    • 0028841535 scopus 로고
    • Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases
    • Haydock S., Aparicio J.F., Molnar I., Schwecke T., Konig A., Marsden A.F.A., Galloway I.S., Staunton J., Leadlay P.F. Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases. FEBS Lett. 374:1995;246-248.
    • (1995) FEBS Lett. , vol.374 , pp. 246-248
    • Haydock, S.1    Aparicio, J.F.2    Molnar, I.3    Schwecke, T.4    Konig, A.5    Marsden, A.F.A.6    Galloway, I.S.7    Staunton, J.8    Leadlay, P.F.9
  • 31
    • 0032730161 scopus 로고    scopus 로고
    • Role of crotonyl coenzyme a reductase in determining the ratio of polyketides monensin a and monensin B produced by Streptomyces cinnamonensis
    • Liu H., Reynolds K.A. Role of crotonyl coenzyme A reductase in determining the ratio of polyketides monensin A and monensin B produced by Streptomyces cinnamonensis. J. Bacteriol. 181:1999;6806-6813.
    • (1999) J. Bacteriol. , vol.181 , pp. 6806-6813
    • Liu, H.1    Reynolds, K.A.2
  • 32
    • 0028989612 scopus 로고
    • A second branched-chain alpha-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: Its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins
    • Denoya C.D., Fedechko R.W., Hafner E.W., McArthur H.A., Morgenstern M.R., Skinner D.D., Stutzman-Engwall K., Wax R.G., Wernau W.C. A second branched-chain alpha-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis. its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins J. Bacteriol. 177:1995;3504-3511.
    • (1995) J. Bacteriol. , vol.177 , pp. 3504-3511
    • Denoya, C.D.1    Fedechko, R.W.2    Hafner, E.W.3    McArthur, H.A.4    Morgenstern, M.R.5    Skinner, D.D.6    Stutzman-Engwall, K.7    Wax, R.G.8    Wernau, W.C.9
  • 33
    • 0033533388 scopus 로고    scopus 로고
    • Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine
    • Witkowski A., Joshi A.K., Lindqvist Y., Smith S. Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry. 38:1999;11643-11650.
    • (1999) Biochemistry , vol.38 , pp. 11643-11650
    • Witkowski, A.1    Joshi, A.K.2    Lindqvist, Y.3    Smith, S.4
  • 34
    • 0038690204 scopus 로고    scopus 로고
    • Site-specific mutagenesis and domain substitutions in the loading module of the nystatin polyketide synthase, and their effects on nystatin biosynthesis in Streptomyces noursei
    • Brautaset T., Borgos S.E.F., Sletta H., Ellingsen T.E., Zotchev S.B. Site-specific mutagenesis and domain substitutions in the loading module of the nystatin polyketide synthase, and their effects on nystatin biosynthesis in Streptomyces noursei. J. Biol. Chem. 278:2003;14913-14919.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14913-14919
    • Brautaset, T.1    Borgos, S.E.F.2    Sletta, H.3    Ellingsen, T.E.4    Zotchev, S.B.5
  • 38
    • 0023001541 scopus 로고
    • Physical and genetic characterisation of the gene cluster for the antibiotic actinorhodin in Streptomyces coelicolor A3(2)
    • Malpartida F., Hopwood D.A. Physical and genetic characterisation of the gene cluster for the antibiotic actinorhodin in Streptomyces coelicolor A3(2). Mol. Gen. Genet. 205:1986;66-73.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 66-73
    • Malpartida, F.1    Hopwood, D.A.2
  • 39
    • 0026673733 scopus 로고
    • The glucose kinase gene of Streptomyces coelicolor A3(2): Its nucleotide sequence, transcriptional analysis and role in glucose repression
    • Angell S., Schwarz E., Bibb M.J. The glucose kinase gene of Streptomyces coelicolor A3(2). its nucleotide sequence, transcriptional analysis and role in glucose repression Mol. Microbiol. 6:1992;2833-2844.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2833-2844
    • Angell, S.1    Schwarz, E.2    Bibb, M.J.3
  • 40
  • 42
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains. nucleotide sequences of the M13mp18 and pUC19 vectors Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 43
    • 0025129406 scopus 로고
    • Spore colour in Streptomyces coelicolor A3(2) involves the developmentally regulated synthesis of a compound biosynthetically related to polyketide antibiotics
    • Davis N.K., Chater K.F. Spore colour in Streptomyces coelicolor A3(2) involves the developmentally regulated synthesis of a compound biosynthetically related to polyketide antibiotics. Mol. Microbiol. 4:1990;1679-1691.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1679-1691
    • Davis, N.K.1    Chater, K.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.