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Volumn 203, Issue 1, 1997, Pages 1-9

A second type-I PKS gene cluster isolated from Streptomyces hygroscopicus ATCC 29253, a rapamycin-producing strain

Author keywords

Acyltransferase; DAHP synthase; HTH motif; Ligase; Pteridine dependent dioxygenase

Indexed keywords

2 DEHYDRO 3 DEOXYPHOSPHOHEPTONATE ALDOLASE; FUNGAL DNA; PHENAZINE; RAPAMYCIN; SYNTHETASE;

EID: 0030729349     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00450-2     Document Type: Article
Times cited : (47)

References (33)
  • 3
    • 0029872079 scopus 로고    scopus 로고
    • Organization of 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., Leadlay P.F. Organization of biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase. Gene. 169:1996;9-16.
    • (1996) Gene , vol.169 , 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
  • 4
    • 0026697224 scopus 로고
    • Identification of DEBS1, DEBS2 AND DEBS3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea
    • Caffrey P., Bevitt D.J., Staunton J., Leadlay P.F. Identification of DEBS1, DEBS2 AND DEBS3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea. FEBS Lett. 304:1992;225-228.
    • (1992) FEBS Lett. , vol.304 , pp. 225-228
    • Caffrey, P.1    Bevitt, D.J.2    Staunton, J.3    Leadlay, P.F.4
  • 5
    • 0027522976 scopus 로고
    • The biosynthesis and synthesis of shikimic acid, chorismic acid and related compounds
    • Campbell M.M., Sainsbury M., Searle P.A. The biosynthesis and synthesis of shikimic acid, chorismic acid and related compounds. Synthesis. 2:1993;179-193.
    • (1993) Synthesis , vol.2 , pp. 179-193
    • Campbell, M.M.1    Sainsbury, M.2    Searle, P.A.3
  • 6
    • 0002901362 scopus 로고    scopus 로고
    • The chemistry and biology of fatty acid, polyketide, and nonribosomal peptide biosynthesis
    • Carreras C.W., Pieper R., Khosla C. The chemistry and biology of fatty acid, polyketide, and nonribosomal peptide biosynthesis. Top. Curr. Chem. 188:1997;85-126.
    • (1997) Top. Curr. Chem. , vol.188 , pp. 85-126
    • Carreras, C.W.1    Pieper, R.2    Khosla, C.3
  • 8
    • 0022394968 scopus 로고
    • Evidence for a sex factor in Streptomyces erythreus
    • Dewitt J.P. Evidence for a sex factor in Streptomyces erythreus. J. Bacteriol. 164:1985;969-971.
    • (1985) J. Bacteriol. , vol.164 , pp. 969-971
    • Dewitt, J.P.1
  • 9
    • 0026559262 scopus 로고
    • Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythraea
    • Donadio S., Katz L. Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythraea. Gene. 111:1992;51-60.
    • (1992) Gene , vol.111 , pp. 51-60
    • Donadio, S.1    Katz, L.2
  • 10
    • 0028841535 scopus 로고
    • Divergent structural motifs correlated with the substrate specificity of (methyl)malonyl-CoA: Acylcarrier 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 structural motifs correlated with the substrate specificity of (methyl)malonyl-CoA: acylcarrier 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
  • 11
    • 0025997703 scopus 로고
    • Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack
    • Keith B., Dong X., Ausubel F.M., Fink G.R. Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack. Proc. Natl. Acad. Sci. USA. 88:1991;8821-8825.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8821-8825
    • Keith, B.1    Dong, X.2    Ausubel, F.M.3    Fink, G.R.4
  • 12
    • 0026514560 scopus 로고
    • Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3- deoxy-D-arabino-heptulosonate-7-phosphate synthase of Saccharomyces cerevisiae
    • Kunzler M., Paravicini G., Egli C.M., Irniger S., Braus G.H. Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3- deoxy-D-arabino-heptulosonate-7-phosphate synthase of Saccharomyces cerevisiae. Gene. 113:1992;67-74.
    • (1992) Gene , vol.113 , pp. 67-74
    • Kunzler, M.1    Paravicini, G.2    Egli, C.M.3    Irniger, S.4    Braus, G.H.5
  • 13
    • 0027151797 scopus 로고
    • Physical map of the Streptomyces lividans 66 genome and comparison with that of the related strain Streptomyces ceolicolor A3(2)
    • Leblond P., Redenbach M., Cullum J. Physical map of the Streptomyces lividans 66 genome and comparison with that of the related strain Streptomyces ceolicolor A3(2). J. Bacteriol. 175:1993;3422-3429.
    • (1993) J. Bacteriol. , vol.175 , pp. 3422-3429
    • Leblond, P.1    Redenbach, M.2    Cullum, J.3
  • 14
    • 0030898921 scopus 로고    scopus 로고
    • Gene disruption and replacement in the rapamycin-producing Streptomyces hygroscopicus strain ATCC 29253
    • Lomovskaya N., Fonstein L., Ruan X., Stassi D., Katz L., Hutchinson C.R. Gene disruption and replacement in the rapamycin-producing Streptomyces hygroscopicus strain ATCC 29253. Microbiology. 143:1997;875-883.
    • (1997) Microbiology , vol.143 , pp. 875-883
    • Lomovskaya, N.1    Fonstein, L.2    Ruan, X.3    Stassi, D.4    Katz, L.5    Hutchinson, C.R.6
  • 16
    • 0026667294 scopus 로고
    • Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase
    • MacNeil D.J., Occi J. L, Gewain K.M., MacNeil T., Gibbons P.H., Ruby C.L., Danis S.J. Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase. Gene. 115:1992;119-125.
    • (1992) Gene , vol.115 , pp. 119-125
    • MacNeil, D.J.1    Occi, J.L.2    Gewain, K.M.3    MacNeil, T.4    Gibbons, P.H.5    Ruby, C.L.6    Danis, S.J.7
  • 18
    • 0029883934 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of genes flanking the polyketide synthase
    • Molnar I., Aparicio J.F., Haydock S.F., Khaw L.E., Schwecke T., Konig A., Staunton J., Leadlay P.F. Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of genes flanking the polyketide synthase. Gene. 169:1996;1-7.
    • (1996) Gene , vol.169 , pp. 1-7
    • Molnar, I.1    Aparicio, J.F.2    Haydock, S.F.3    Khaw, L.E.4    Schwecke, T.5    Konig, A.6    Staunton, J.7    Leadlay, P.F.8
  • 19
    • 0031043482 scopus 로고    scopus 로고
    • Structural organization of a multifunctional polyketide synthase involved in the biosynthesis of the macrolide immunosuppressant FK506
    • Motamedi H., Cai S.J., Shafiee A., Elliston K.O. Structural organization of a multifunctional polyketide synthase involved in the biosynthesis of the macrolide immunosuppressant FK506. Eur. J. Biochem. 244:1997;74-80.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 74-80
    • Motamedi, H.1    Cai, S.J.2    Shafiee, A.3    Elliston, K.O.4
  • 20
    • 0027845217 scopus 로고
    • The cyclohexane moiety of rapamycin is derived from shikimic acid in Streptomyces hygroscopicus
    • Paiva N.L., Robert M.F., Demain A.L. The cyclohexane moiety of rapamycin is derived from shikimic acid in Streptomyces hygroscopicus. J. Ind. Microbiol. 12:1993;423-428.
    • (1993) J. Ind. Microbiol. , vol.12 , pp. 423-428
    • Paiva, N.L.1    Robert, M.F.2    Demain, A.L.3
  • 21
    • 0028834892 scopus 로고
    • Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84
    • Pierson III L.S., Gaffney T., Lam S., Gong F. Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84. FEMS Microbiol. Lett. 134:1995;299-307.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 299-307
    • Pierson L.S. III1    Gaffney, T.2    Lam, S.3    Gong, F.4
  • 22
    • 0025048136 scopus 로고
    • The P-loop: A common motif in ATP-binding and GTP-binding proteins
    • Saraste M., Sibbald P.R., Wittinghofer A. The P-loop: a common motif in ATP-binding and GTP-binding proteins. Trends Biol. Sci. 15:1990;430-434.
    • (1990) Trends Biol. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 24
    • 0021125701 scopus 로고
    • The nucleotide sequence of the AroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase
    • Schultz J., Hermondson M.A., Garner C.C., Herrmann K.M. The nucleotide sequence of the AroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase. J. Biol. Chem. 259:1984;9655-9661.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9655-9661
    • Schultz, J.1    Hermondson, M.A.2    Garner, C.C.3    Herrmann, K.M.4
  • 25
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton N.S., Berry A., Perham R.N. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature. 343:1990;38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 26
    • 0026549146 scopus 로고
    • Compilation and analysis of DNA sequences associated with apparent Streptomycete promoters
    • Strohl W.R. Compilation and analysis of DNA sequences associated with apparent Streptomycete promoters. Nucleic Acids Res. 20:1992;961-974.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 961-974
    • Strohl, W.R.1
  • 27
    • 0028044628 scopus 로고
    • Characterization of a Streptomyces antibioticus gene encoding a type I polyketide synthase which has an unusual coding sequence
    • Swan D.G., Rodriguez A.M., Vilches C., Mendez C., Salas J.A. Characterization of a Streptomyces antibioticus gene encoding a type I polyketide synthase which has an unusual coding sequence. Mol. Gen. Genet. 242:1994;358-362.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 358-362
    • Swan, D.G.1    Rodriguez, A.M.2    Vilches, C.3    Mendez, C.4    Salas, J.A.5
  • 28
    • 0025335890 scopus 로고
    • Cloning of genes involved in erythromycin biosynthesis from Saccharopolyspora erythraea using a novel actinomycete-Escherichia coli cosmid
    • Tuan J.S., Weber J.M., Staver M.J., Leung J.O., Donadio S., Katz L. Cloning of genes involved in erythromycin biosynthesis from Saccharopolyspora erythraea using a novel actinomycete-Escherichia coli cosmid. Gene. 90:1990;21-29.
    • (1990) Gene , vol.90 , pp. 21-29
    • Tuan, J.S.1    Weber, J.M.2    Staver, M.J.3    Leung, J.O.4    Donadio, S.5    Katz, L.6
  • 29
    • 0026926521 scopus 로고
    • Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay K., Krause M., Marahiel M.A. Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6:1992;529-546.
    • (1992) Mol. Microbiol. , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 30
    • 0029846030 scopus 로고    scopus 로고
    • Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2) Streptomyces rimosus and Neurospora crassa
    • Walker G.E., Dunbar B., Hunter I., Nimmo H.G., Coggins J. Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2) Streptomyces rimosus and Neurospora crassa. Microbiology. 142:1996;1973-1982.
    • (1996) Microbiology , vol.142 , pp. 1973-1982
    • Walker, G.E.1    Dunbar, B.2    Hunter, I.3    Nimmo, H.G.4    Coggins, J.5
  • 31
    • 0005647566 scopus 로고
    • Cloning and nucleotide sequence of a complementary DNA encoding 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases from tobacco
    • Wang Y., Herrmann K.M., Weller S.C., Doldsbrough P.B. Cloning and nucleotide sequence of a complementary DNA encoding 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases from tobacco. Plant Physiol. 97:1991;847-848.
    • (1991) Plant Physiol. , vol.97 , pp. 847-848
    • Wang, Y.1    Herrmann, K.M.2    Weller, S.C.3    Doldsbrough, P.B.4
  • 33
    • 0005757157 scopus 로고
    • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Solanum tuberosum L
    • Zhao J., Herrmann K.M. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Solanum tuberosum L. Plant Physiol. 100:1992;1075-1076.
    • (1992) Plant Physiol. , vol.100 , pp. 1075-1076
    • Zhao, J.1    Herrmann, K.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.