메뉴 건너뛰기




Volumn 6, Issue 8, 2011, Pages

Biosynthetic gene cluster for the cladoniamides, bis-indoles with a rearranged scaffold

Author keywords

[No Author keywords available]

Indexed keywords

ALKALOID; ALPHA BETA HYDROLASE; CARBAZOLE DERIVATIVE; CLADONIAMIDE; HYDROLASE; INDOLOCARBAZOLE; METHYLTRANSFERASE; MOLECULAR SCAFFOLD; OXYGENASE; QUERCETIN; TRYPTOPHAN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARBOLINE DERIVATIVE; INDOLE DERIVATIVE; REBECCAMYCIN; TRYPTOLINE;

EID: 80051853410     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023694     Document Type: Article
Times cited : (33)

References (46)
  • 3
    • 54049085036 scopus 로고    scopus 로고
    • Cladoniamides A-G, tryptophan-derived alkaloids produced in culture by Streptomyces uncialis
    • Williams DE, Davies J, Patrick BO, Bottriell H, Tarling T, et al. (2008) Cladoniamides A-G, tryptophan-derived alkaloids produced in culture by Streptomyces uncialis. Org Lett 10: 3501-3504.
    • (2008) Org Lett , vol.10 , pp. 3501-3504
    • Williams, D.E.1    Davies, J.2    Patrick, B.O.3    Bottriell, H.4    Tarling, T.5
  • 4
    • 33751335837 scopus 로고    scopus 로고
    • Indolocarbazole natural products: occurrence, biosynthesis, and biological activity
    • Sánchez C, Méndez C, Salas JA, (2006) Indolocarbazole natural products: occurrence, biosynthesis, and biological activity. Nat Prod Rep 23: 1007-1045.
    • (2006) Nat Prod Rep , vol.23 , pp. 1007-1045
    • Sánchez, C.1    Méndez, C.2    Salas, J.A.3
  • 5
    • 0023178261 scopus 로고
    • Production and biological activity of rebeccamycin, a novel antitumor agent
    • (Tokyo)
    • Bush JA, Long BH, Catino JJ, Bradner WT, Tomita K, (1987) Production and biological activity of rebeccamycin, a novel antitumor agent. J Antibiot (Tokyo) 40: 668-678.
    • (1987) J Antibiot , vol.40 , pp. 668-678
    • Bush, J.A.1    Long, B.H.2    Catino, J.J.3    Bradner, W.T.4    Tomita, K.5
  • 6
    • 0037294445 scopus 로고    scopus 로고
    • Rebeccamycin analogues as anti-cancer agents
    • Prudhomme M, (2003) Rebeccamycin analogues as anti-cancer agents. Eur J Med Chem 38: 123-140.
    • (2003) Eur J Med Chem , vol.38 , pp. 123-140
    • Prudhomme, M.1
  • 7
    • 0017395981 scopus 로고
    • A new alkaloid AM-2282 of Streptomyces origin. Taxonomy, fermentation, isolation and preliminary characterization
    • (Tokyo)
    • Omura S, Iwai Y, Hirano A, Nakagawa A, Awaya J, et al. (1977) A new alkaloid AM-2282 of Streptomyces origin. Taxonomy, fermentation, isolation and preliminary characterization. J Antibiot (Tokyo) 30: 275-282.
    • (1977) J Antibiot , vol.30 , pp. 275-282
    • Omura, S.1    Iwai, Y.2    Hirano, A.3    Nakagawa, A.4    Awaya, J.5
  • 8
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases
    • Ruegg UT, Burgess GM, (1989) Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases. Trends Pharmacol Sci 10: 218-220.
    • (1989) Trends Pharmacol Sci , vol.10 , pp. 218-220
    • Ruegg, U.T.1    Burgess, G.M.2
  • 9
    • 0036952785 scopus 로고    scopus 로고
    • Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans
    • (Tokyo)
    • Onaka H, Taniguchi S, Igarashi Y, Furumai T, (2002) Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans. J Antibiot (Tokyo) 55: 1063-1071.
    • (2002) J Antibiot , vol.55 , pp. 1063-1071
    • Onaka, H.1    Taniguchi, S.2    Igarashi, Y.3    Furumai, T.4
  • 10
    • 0036235877 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the antitumor rebeccamycin: characterization and generation of indolocarbazole derivatives
    • Sánchez C, Butovich IA, Braña AF, Rohr J, Méndez C, et al. (2002) The biosynthetic gene cluster for the antitumor rebeccamycin: characterization and generation of indolocarbazole derivatives. Chem Biol 9: 519-531.
    • (2002) Chem Biol , vol.9 , pp. 519-531
    • Sánchez, C.1    Butovich, I.A.2    Braña, A.F.3    Rohr, J.4    Méndez, C.5
  • 11
    • 0012569067 scopus 로고    scopus 로고
    • Characterization of the biosynthetic gene cluster of rebeccamycin from Lechevalieria aerocolonigenes ATCC 39243
    • Onaka H, Taniguchi S, Igarashi Y, Furumai T, (2003) Characterization of the biosynthetic gene cluster of rebeccamycin from Lechevalieria aerocolonigenes ATCC 39243. Biosci Biotechnol Biochem 67: 127-138.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 127-138
    • Onaka, H.1    Taniguchi, S.2    Igarashi, Y.3    Furumai, T.4
  • 13
    • 79959894320 scopus 로고    scopus 로고
    • Cloning and characterization of an environmental DNA-derived gene cluster that encodes the biosynthesis of the antitumor substance BE-54017
    • Chang FY, Brady SF, (2011) Cloning and characterization of an environmental DNA-derived gene cluster that encodes the biosynthesis of the antitumor substance BE-54017. J Am Chem Soc 133: 9996-9999.
    • (2011) J Am Chem Soc , vol.133 , pp. 9996-9999
    • Chang, F.Y.1    Brady, S.F.2
  • 14
    • 33748758449 scopus 로고    scopus 로고
    • Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid
    • Howard-Jones AR, Walsh CT, (2006) Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid. J Am Chem Soc 128: 12289-12298.
    • (2006) J Am Chem Soc , vol.128 , pp. 12289-12298
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 15
    • 70349464475 scopus 로고    scopus 로고
    • Genomic islands link secondary metabolism to functional adaptation in marine Actinobacteria
    • Penn K, Jenkins C, Nett M, Udwary DW, Gontang EA, et al. (2009) Genomic islands link secondary metabolism to functional adaptation in marine Actinobacteria. ISME J 3: 1193-1203.
    • (2009) ISME J , vol.3 , pp. 1193-1203
    • Penn, K.1    Jenkins, C.2    Nett, M.3    Udwary, D.W.4    Gontang, E.A.5
  • 16
    • 33746218306 scopus 로고    scopus 로고
    • Deciphering indolocarbazole and enediyne aminodideoxypentose biosynthesis through comparative genomics: insights from the AT2433 biosynthetic locus
    • Gao Q, Zhang C, Blanchard S, Thorson JS, (2006) Deciphering indolocarbazole and enediyne aminodideoxypentose biosynthesis through comparative genomics: insights from the AT2433 biosynthetic locus. Chem Biol 13: 733-743.
    • (2006) Chem Biol , vol.13 , pp. 733-743
    • Gao, Q.1    Zhang, C.2    Blanchard, S.3    Thorson, J.S.4
  • 17
    • 34250675327 scopus 로고    scopus 로고
    • Genetic organization of the biosynthetic gene cluster for the indolocarbazole K-252a in Nonomuraea longicatena JCM 11136
    • Kim SY, Park JS, Chae CS, Hyun CG, Choi BW, et al. (2007) Genetic organization of the biosynthetic gene cluster for the indolocarbazole K-252a in Nonomuraea longicatena JCM 11136. Appl Microbiol Biotechnol 75: 1119-1126.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1119-1126
    • Kim, S.Y.1    Park, J.S.2    Chae, C.S.3    Hyun, C.G.4    Choi, B.W.5
  • 19
    • 77958475358 scopus 로고    scopus 로고
    • The sequence of a 1.8-mb bacterial linear plasmid reveals a rich evolutionary reservoir of secondary metabolic pathways
    • Medema MH, Trefzer A, Kovalchuk A, van den Berg M, Müller U, et al. (2010) The sequence of a 1.8-mb bacterial linear plasmid reveals a rich evolutionary reservoir of secondary metabolic pathways. Genome Biol Evol 2: 212-224.
    • (2010) Genome Biol Evol , vol.2 , pp. 212-224
    • Medema, M.H.1    Trefzer, A.2    Kovalchuk, A.3    van den Berg, M.4    Müller, U.5
  • 20
    • 43249112810 scopus 로고    scopus 로고
    • Identifying the minimal enzymes required for anhydrotetracycline biosynthesis
    • Zhang W, Watanabe K, Cai X, Jung ME, Tang Y, et al. (2008) Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J Am Chem Soc 130: 6068-6069.
    • (2008) J Am Chem Soc , vol.130 , pp. 6068-6069
    • Zhang, W.1    Watanabe, K.2    Cai, X.3    Jung, M.E.4    Tang, Y.5
  • 21
    • 72249105298 scopus 로고    scopus 로고
    • Biochemical analysis of the biosynthetic pathway of an anticancer tetracycline SF2575
    • Pickens LB, Kim W, Wang P, Zhou H, Watanabe K, et al. (2009) Biochemical analysis of the biosynthetic pathway of an anticancer tetracycline SF2575. J Am Chem Soc 131: 17677-17689.
    • (2009) J Am Chem Soc , vol.131 , pp. 17677-17689
    • Pickens, L.B.1    Kim, W.2    Wang, P.3    Zhou, H.4    Watanabe, K.5
  • 22
    • 33748572673 scopus 로고    scopus 로고
    • Premithramycinone G, an early shunt product of the mithramycin biosynthetic pathway accumulated upon inactivation of oxygenase MtmOII
    • Abdelfattah MS, Rohr J, (2006) Premithramycinone G, an early shunt product of the mithramycin biosynthetic pathway accumulated upon inactivation of oxygenase MtmOII. Angew Chem Int Ed Engl 45: 5685-5689.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5685-5689
    • Abdelfattah, M.S.1    Rohr, J.2
  • 23
    • 0034609696 scopus 로고    scopus 로고
    • Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O(2) and one molecule of H(2)O
    • Rafanan ER Jr, Hutchinson CR, Shen B, (2000) Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O(2) and one molecule of H(2)O. Org Lett 2: 3225-3227.
    • (2000) Org Lett , vol.2 , pp. 3225-3227
    • Rafanan Jr., E.R.1    Hutchinson, C.R.2    Shen, B.3
  • 24
    • 33751013733 scopus 로고    scopus 로고
    • The boat-shaped polyketide resistoflavin results from re-facial central hydroxylation of the discoid metabolite resistomycin
    • Ishida K, Maksimenka K, Fritzsche K, Scherlach K, Bringmann G, et al. (2006) The boat-shaped polyketide resistoflavin results from re-facial central hydroxylation of the discoid metabolite resistomycin. J Am Chem Soc 128: 14619-14624.
    • (2006) J Am Chem Soc , vol.128 , pp. 14619-14624
    • Ishida, K.1    Maksimenka, K.2    Fritzsche, K.3    Scherlach, K.4    Bringmann, G.5
  • 26
    • 54849415919 scopus 로고    scopus 로고
    • Tandem action of the O2- and FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly
    • Heemstra JR Jr, Walsh CT, (2008) Tandem action of the O2- and FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly. J Am Chem Soc 130: 14024-14025.
    • (2008) J Am Chem Soc , vol.130 , pp. 14024-14025
    • Heemstra Jr., J.R.1    Walsh, C.T.2
  • 27
    • 17844408703 scopus 로고    scopus 로고
    • A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005
    • Zehner S, Kotzsch A, Bister B, Süssmuth RD, Méndez C, et al. (2005) A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005. Chem Biol 12: 445-452.
    • (2005) Chem Biol , vol.12 , pp. 445-452
    • Zehner, S.1    Kotzsch, A.2    Bister, B.3    Süssmuth, R.D.4    Méndez, C.5
  • 28
    • 15244349569 scopus 로고    scopus 로고
    • Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis
    • Yeh E, Garneau S, Walsh CT, (2005) Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis. Proc Natl Acad Sci U S A 102: 3960-3965.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3960-3965
    • Yeh, E.1    Garneau, S.2    Walsh, C.T.3
  • 29
    • 0030908709 scopus 로고    scopus 로고
    • Four genes from Pseudomonas fluorescens that encode the biosynthesis of pyrrolnitrin
    • Hammer PE, Hill DS, Lam ST, Van Pée KH, Ligon JM, (1997) Four genes from Pseudomonas fluorescens that encode the biosynthesis of pyrrolnitrin. Appl Environ Microbiol 63: 2147-2154.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2147-2154
    • Hammer, P.E.1    Hill, D.S.2    Lam, S.T.3    Van Pée, K.H.4    Ligon, J.M.5
  • 30
    • 0034600905 scopus 로고    scopus 로고
    • Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens
    • Keller S, Wage T, Hohaus K, Hölzer M, Eichhorn E, et al. (2000) Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens. Angew Chem Int Ed Engl 39: 2300-2302.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 2300-2302
    • Keller, S.1    Wage, T.2    Hohaus, K.3    Hölzer, M.4    Eichhorn, E.5
  • 31
    • 65549137958 scopus 로고    scopus 로고
    • Organisation of the biosynthetic gene cluster and tailoring enzymes in the biosynthesis of the tetracyclic quinone glycoside antibiotic polyketomycin
    • Daum M, Peintner I, Linnenbrink A, Frerich A, Weber M, et al. (2009) Organisation of the biosynthetic gene cluster and tailoring enzymes in the biosynthesis of the tetracyclic quinone glycoside antibiotic polyketomycin. Chembiochem 10: 1073-1083.
    • (2009) Chembiochem , vol.10 , pp. 1073-1083
    • Daum, M.1    Peintner, I.2    Linnenbrink, A.3    Frerich, A.4    Weber, M.5
  • 32
    • 42949168430 scopus 로고    scopus 로고
    • Biosynthesis of elloramycin in Streptomyces olivaceus requires glycosylation by enzymes encoded outside the aglycon cluster
    • Ramos A, Lombó F, Braña AF, Rohr J, Méndez C, et al. (2008) Biosynthesis of elloramycin in Streptomyces olivaceus requires glycosylation by enzymes encoded outside the aglycon cluster. Microbiology 154: 781-788.
    • (2008) Microbiology , vol.154 , pp. 781-788
    • Ramos, A.1    Lombó, F.2    Braña, A.F.3    Rohr, J.4    Méndez, C.5
  • 33
    • 28444466613 scopus 로고    scopus 로고
    • Cloning, sequencing, analysis, and heterologous expression of the fredericamycin biosynthetic gene cluster from Streptomyces griseus
    • Wendt-Pienkowski E, Huang Y, Zhang J, Li B, Jiang H, et al. (2005) Cloning, sequencing, analysis, and heterologous expression of the fredericamycin biosynthetic gene cluster from Streptomyces griseus. J Am Chem Soc 127: 16442-16452.
    • (2005) J Am Chem Soc , vol.127 , pp. 16442-16452
    • Wendt-Pienkowski, E.1    Huang, Y.2    Zhang, J.3    Li, B.4    Jiang, H.5
  • 34
    • 0033145727 scopus 로고    scopus 로고
    • A subfamily of MalT-related ATP-dependent regulators in the LuxR family
    • De Schrijver A, De Mot R, (1999) A subfamily of MalT-related ATP-dependent regulators in the LuxR family. Microbiology 145 (Pt 6): 1287-1288.
    • (1999) Microbiology , vol.145 , Issue.Pt 6 , pp. 1287-1288
    • De Schrijver, A.1    De Mot, R.2
  • 37
    • 14644432391 scopus 로고    scopus 로고
    • Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
    • Nishizawa T, Aldrich CC, Sherman DH, (2005) Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J Bacteriol 187: 2084-2092.
    • (2005) J Bacteriol , vol.187 , pp. 2084-2092
    • Nishizawa, T.1    Aldrich, C.C.2    Sherman, D.H.3
  • 38
    • 53049087315 scopus 로고    scopus 로고
    • Structure and mechanism of the rebeccamycin sugar 4′-O-methyltransferase RebM
    • Singh S, McCoy JG, Zhang C, Bingman CA, Phillips GN Jr, et al. (2008) Structure and mechanism of the rebeccamycin sugar 4′-O-methyltransferase RebM. J Biol Chem 283: 22628-22636.
    • (2008) J Biol Chem , vol.283 , pp. 22628-22636
    • Singh, S.1    McCoy, J.G.2    Zhang, C.3    Bingman, C.A.4    Phillips Jr., G.N.5
  • 40
    • 28544449005 scopus 로고    scopus 로고
    • Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD
    • Howard-Jones AR, Walsh CT, (2005) Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44: 15652-15663.
    • (2005) Biochemistry , vol.44 , pp. 15652-15663
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 42
    • 0032942468 scopus 로고    scopus 로고
    • FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G + C content
    • Ishikawa J, Hotta K, (1999) FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G + C content. FEMS Microbiol Lett 174: 251-253.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 251-253
    • Ishikawa, J.1    Hotta, K.2
  • 44
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL, (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 45
    • 0037929203 scopus 로고    scopus 로고
    • Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2′-carbon of FAD with fluorine
    • Palfey BA, Murthy YV, Massey V, (2003) Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2′-carbon of FAD with fluorine. J Biol Chem 278: 22210-22216.
    • (2003) J Biol Chem , vol.278 , pp. 22210-22216
    • Palfey, B.A.1    Murthy, Y.V.2    Massey, V.3
  • 46


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.