메뉴 건너뛰기




Volumn 127, Issue 5, 2000, Pages 779-789

Polyketide synthase gene coupled to the peptide synthetase module involved in the biosynthesis of the cyclic heptapeptide microcystin

Author keywords

Cyanobacteria; Microcystin biosynthesis; Multifunctional enzyme complex; Peptide synthetase gene; Polyketide synthase gene

Indexed keywords

BACTERIAL ENZYME; CYANOGINOSIN; GLUTAMIC ACID; PEPTIDE SYNTHASE; POLYKETIDE SYNTHASE;

EID: 0034115536     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022670     Document Type: Article
Times cited : (221)

References (48)
  • 1
    • 0002766875 scopus 로고
    • The toxins of cyanobacteria
    • January
    • Carmichael, W.W. (1994) The toxins of cyanobacteria. Sci. Am. January, 64-72
    • (1994) Sci. Am. , pp. 64-72
    • Carmichael, W.W.1
  • 4
    • 0025333146 scopus 로고
    • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants
    • MacKintosh, C., Beattie, K.A., Klumpp, S., Cohen, P., and Codd, G.A. (1990) Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Lett. 264, 187-192
    • (1990) FEBS Lett. , vol.264 , pp. 187-192
    • MacKintosh, C.1    Beattie, K.A.2    Klumpp, S.3    Cohen, P.4    Codd, G.A.5
  • 6
    • 0031459595 scopus 로고    scopus 로고
    • The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: Molecular characterization of three multimodular peptide synthetases
    • Konz, D., Klens, A., Schörgendorfer, K., and Marahiel, M.A. (1997) The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: molecular characterization of three multimodular peptide synthetases. Chem. Biol. 4, 927-937
    • (1997) Chem. Biol. , vol.4 , pp. 927-937
    • Konz, D.1    Klens, A.2    Schörgendorfer, K.3    Marahiel, M.A.4
  • 7
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • Marahiel, M.A. (1997) Protein templates for the biosynthesis of peptide antibiotics. Chem. Biol. 4, 561-567
    • (1997) Chem. Biol. , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 8
    • 0028837014 scopus 로고
    • Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis
    • Stachelhaus, T. and Marahiel, M.A. (1995) Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis. FEMS Microbiol. Lett. 125, 3-14
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 3-14
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 9
    • 0030723581 scopus 로고    scopus 로고
    • Insertional mutagenesis of a peptide synthetase gene that is responsible for hepatotoxin produciton in the cyanobacterium Microcystis aeruginosa PCC7806
    • Dittmann, E., Neilan, B.A., Erhard, M., von Döhren, H., and Börner, T. (1997) Insertional mutagenesis of a peptide synthetase gene that is responsible for hepatotoxin produciton in the cyanobacterium Microcystis aeruginosa PCC7806. Mol. Microbiol. 26, 779-787
    • (1997) Mol. Microbiol. , vol.26 , pp. 779-787
    • Dittmann, E.1    Neilan, B.A.2    Erhard, M.3    Von Döhren, H.4    Börner, T.5
  • 10
    • 0032873121 scopus 로고    scopus 로고
    • Genetic analysis of the peptide synthetase genes for a cyclic heptapeptide microcystin in Microcystis spp
    • Nishizawa, T., Asayama, M., Fujii, K., Harada, K-I., and Shirai, M. (1999) Genetic analysis of the peptide synthetase genes for a cyclic heptapeptide microcystin in Microcystis spp. J. Biochem. 126, 520-529
    • (1999) J. Biochem. , vol.126 , pp. 520-529
    • Nishizawa, T.1    Asayama, M.2    Fujii, K.3    Harada, K.-I.4    Shirai, M.5
  • 11
    • 0001344734 scopus 로고
    • Biosynthesis of Microcystin-LR. Origin of the carbons in the Adda and Masp units
    • Moore, R.E., Chen, J.L., Moore, B.S., and Patterson, G.M.L. (1991) Biosynthesis of Microcystin-LR. Origin of the carbons in the Adda and Masp units. J. Am. Chem. Soc. 113, 5083-5084
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5083-5084
    • Moore, R.E.1    Chen, J.L.2    Moore, B.S.3    Patterson, G.M.L.4
  • 12
    • 0026559262 scopus 로고
    • Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythaea
    • Donadio, S. and Katz, L. (1992) Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythaea. Gene 111, 51-60
    • (1992) Gene , vol.111 , pp. 51-60
    • Donadio, S.1    Katz, L.2
  • 14
    • 0029064652 scopus 로고
    • Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
    • McDaniel, R., Ebert-Khosla, S., Hopwood, D.A., and Khosla, C. (1995) Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature 375, 549-554
    • (1995) Nature , vol.375 , pp. 549-554
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 15
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D.E., Walsh, C.T., and Khosla, C. (1998) Harnessing the biosynthetic code: combinations, permutations, and mutations. Science 282, 63-68
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 16
    • 0033616687 scopus 로고    scopus 로고
    • Microbial polyketide synthases: More and more prolific
    • Hutchinson, C.R. (1999) Microbial polyketide synthases: More and more prolific. Proc. Natl. Acad. Sci. USA 95, 3336-3338
    • (1999) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3336-3338
    • Hutchinson, C.R.1
  • 22
    • 0032584941 scopus 로고    scopus 로고
    • Characterization of the enzymatic domains in the modular polyketide synthase involved in rifamycin B biosynthesis by Amycolatopsis mediterranei
    • Tang, L., Yoon, Y.J., Choi, C., and Hutchinson, C.R. (1998) Characterization of the enzymatic domains in the modular polyketide synthase involved in rifamycin B biosynthesis by Amycolatopsis mediterranei. Gene 216, 255-265
    • (1998) Gene , vol.216 , pp. 255-265
    • Tang, L.1    Yoon, Y.J.2    Choi, C.3    Hutchinson, C.R.4
  • 23
    • 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.F., Aparicio, J.F., Molnar, I., Schwecke, T., Ee Khaw, L., Konig, A., Marsden, A.F.A., Galloway, I.S., Staunton, J., and Leadlay, P.F. (1995) Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases. FEBS Lett. 374, 246-248
    • (1995) FEBS Lett. , vol.374 , pp. 246-248
    • Haydock, S.F.1    Aparicio, J.F.2    Molnar, I.3    Schwecke, T.4    Ee Khaw, L.5    Konig, A.6    Marsden, A.F.A.7    Galloway, I.S.8    Staunton, J.9    Leadlay, P.F.10
  • 24
    • 0033582596 scopus 로고    scopus 로고
    • The first gene in the biosynthesis of the polyketide antibiotic TA of Myxococcus xanthus codes for a unique PKS module coupled to a peptide synthetase
    • Paitan, Y, Alon, G., Orr, E., Ron, E.Z., and Rosenberg, E. (1999) The first gene in the biosynthesis of the polyketide antibiotic TA of Myxococcus xanthus codes for a unique PKS module coupled to a peptide synthetase. J. Mol. Biol. 286, 456-474
    • (1999) J. Mol. Biol. , vol.286 , pp. 456-474
    • Paitan, Y.1    Alon, G.2    Orr, E.3    Ron, E.Z.4    Rosenberg, E.5
  • 25
    • 0027466435 scopus 로고
    • Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi
    • Haese, A., Schubert, M., Herrmann, M., and Zocher, R. (1993) Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi. Mol. Microbiol. 7, 905-914
    • (1993) Mol. Microbiol. , vol.7 , pp. 905-914
    • Haese, A.1    Schubert, M.2    Herrmann, M.3    Zocher, R.4
  • 26
    • 0025978680 scopus 로고
    • Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli
    • Grimm, B., Bull, A., and Breu, V. (1991) Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli. Mol.Gen. Genet. 225, 1-10
    • (1991) Mol.Gen. Genet. , vol.225 , pp. 1-10
    • Grimm, B.1    Bull, A.2    Breu, V.3
  • 27
    • 0028807689 scopus 로고
    • Multi-enzymatic non ribosomal peptide biosynthesis: Identification of the functional domains catalysing peptide elongation and epimerisation
    • de Crécy-Lagard, V., Marlière, P., and Saurin, W. (1995) Multi-enzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation. CR Acad. Sci. 318, 927-936
    • (1995) CR Acad. Sci. , vol.318 , pp. 927-936
    • De Crécy-Lagard, V.1    Marlière, P.2    Saurin, W.3
  • 28
    • 0029048654 scopus 로고
    • Characterization of tyrocidine synthetase 1 (TY1): Requirement of posttranslational modification for peptide biosynthesis
    • Pfeifer, E., Vrancic, M.P., von Döhren, H., and Kleinkauf, H. (1995) Characterization of tyrocidine synthetase 1 (TY1): Requirement of posttranslational modification for peptide biosynthesis. Biochemistry 34, 7450-7459
    • (1995) Biochemistry , vol.34 , pp. 7450-7459
    • Pfeifer, E.1    Vrancic, M.P.2    Von Döhren, H.3    Kleinkauf, H.4
  • 29
    • 0029811103 scopus 로고    scopus 로고
    • Gene for aspartate racemase from the sulfur-dependent hyperthermophilic archaeum, Desulfurococcus strain SY
    • Yohda, M., Endo, I., Ohta, T, Iida, T., Maruyama, T., and Kagawa, Y. (1996) Gene for aspartate racemase from the sulfur-dependent hyperthermophilic archaeum, Desulfurococcus strain SY. J. Biol. Chem. 271, 22017-22021
    • (1996) J. Biol. Chem. , vol.271 , pp. 22017-22021
    • Yohda, M.1    Endo, I.2    Ohta, T.3    Iida, T.4    Maruyama, T.5    Kagawa, Y.6
  • 31
    • 0030589120 scopus 로고    scopus 로고
    • Restriction barrier composed of an extracellular nuclease and restriction endonuclease in the unicellular cyanobacterium Microcystis sp
    • Takahashi, I., Hayano, D., Asayama, M., Masahiro, F., Watahiki, M., and Shirai, M. (1996) Restriction barrier composed of an extracellular nuclease and restriction endonuclease in the unicellular cyanobacterium Microcystis sp. FEMS Microbiol. Lett. 145, 107-111
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 107-111
    • Takahashi, I.1    Hayano, D.2    Asayama, M.3    Masahiro, F.4    Watahiki, M.5    Shirai, M.6
  • 33
    • 0026588298 scopus 로고
    • Four homologus domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay, K., Krause, M., and Marahiel, M.A. (1992) Four homologus domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6, 529-546
    • (1992) Mol. Microbiol. , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 35
    • 0027299621 scopus 로고
    • Nucleotide sequence of 5′ portion of srfA that contains the region required for competence establishment in Bacillus subtilis
    • Fuma, S., Fujishima, Y., Corbell, N., D'Souza, C., Nakano, M.M., Zuber, P., and Yamane, K. (1993) Nucleotide sequence of 5′ portion of srfA that contains the region required for competence establishment in Bacillus subtilis. Nucleic Acids Res. 21, 93-97
    • (1993) Nucleic Acids Res. , vol.21 , pp. 93-97
    • Fuma, S.1    Fujishima, Y.2    Corbell, N.3    D'Souza, C.4    Nakano, M.M.5    Zuber, P.6    Yamane, K.7
  • 36
    • 0030669091 scopus 로고    scopus 로고
    • The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains
    • Mootz, H.D. and Marahiel, M.A. (1997) The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179, 6843-6850
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 37
    • 0025004152 scopus 로고
    • The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases
    • Smith, D.J., Earl, A.J., and Turner, G. (1990) The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 9, 2743-2750
    • (1990) EMBO J. , vol.9 , pp. 2743-2750
    • Smith, D.J.1    Earl, A.J.2    Turner, G.3
  • 38
    • 0027087171 scopus 로고
    • The cyclic peptide synthetase catalyzing HC-toxin production in the filamentous fungus Cochliobolus carbonum is encoded by a 15.7-kilobase open reading frame
    • Scott-Craig, J.S., Panaccione, D.G., Pocard, J.-A., and Walton, J.D. (1992) The cyclic peptide synthetase catalyzing HC-toxin production in the filamentous fungus Cochliobolus carbonum is encoded by a 15.7-kilobase open reading frame. J. Biol. Chem. 267, 26044-26049
    • (1992) J. Biol. Chem. , vol.267 , pp. 26044-26049
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Pocard, J.-A.3    Walton, J.D.4
  • 39
    • 0025863049 scopus 로고
    • Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine
    • Rusnak, F, Sakaitani, M., Drueckhammer, D., Reichert, J., and Walsh, C.T. (1991) Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine. Biochemistry 30, 2916-2927
    • (1991) Biochemistry , vol.30 , pp. 2916-2927
    • Rusnak, F.1    Sakaitani, M.2    Drueckhammer, D.3    Reichert, J.4    Walsh, C.T.5
  • 40
    • 0025253038 scopus 로고
    • Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida
    • Martínez-Blanco, H., Reglero, A., Rodriguez-Aparicio, L.B., and Luengo, J.M. (1990) Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. J. Biol. Chem. 265, 7084-7090
    • (1990) J. Biol. Chem. , vol.265 , pp. 7084-7090
    • Martínez-Blanco, H.1    Reglero, A.2    Rodriguez-Aparicio, L.B.3    Luengo, J.M.4
  • 43
    • 0021205685 scopus 로고
    • High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-Mob transposon
    • Simon, R. (1984) High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-Mob transposon. Mol. Gen. Genet. 196, 413-420
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 413-420
    • Simon, R.1
  • 44
    • 0026657813 scopus 로고
    • Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin
    • Fernández-Moreno, M.A., Martínez, E., Boto, L., Hopwood, D.A., and Malpartida, F. (1992) Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin. J. Biol. Chem. 267, 19278-19290
    • (1992) J. Biol. Chem. , vol.267 , pp. 19278-19290
    • Fernández-Moreno, M.A.1    Martínez, E.2    Boto, L.3    Hopwood, D.A.4    Malpartida, F.5
  • 45
    • 0024449599 scopus 로고
    • Analysis of the nucleotide sequence of the Streptomyces glaucescens tcmI genes provides key information about the enzymology of polyketide antibiotic biosynthesis
    • Bibb, M.J., Biro, S., Motamedi, H., Collins, J.F., and Hutchinson, C.R. (1989) Analysis of the nucleotide sequence of the Streptomyces glaucescens tcmI genes provides key information about the enzymology of polyketide antibiotic biosynthesis. EMBO J. 8, 2727-2736
    • (1989) EMBO J. , vol.8 , pp. 2727-2736
    • Bibb, M.J.1    Biro, S.2    Motamedi, H.3    Collins, J.F.4    Hutchinson, C.R.5
  • 46
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • Weber, G., Schörgendorfer, K., Schneider-Scherzer, E., and Leitner, E. (1994) The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr. Genet. 26, 120-125
    • (1994) Curr. Genet. , vol.26 , pp. 120-125
    • Weber, G.1    Schörgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 47
    • 0025999536 scopus 로고
    • Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: Sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases
    • Haydock, S.F., Dowson, J.A., Dhillon, N., Roberts, G.A., Cortes, J., and Leadlay, P.F. (1991) Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases. Mol. Gen. Genet. 230, 120-128
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 120-128
    • Haydock, S.F.1    Dowson, J.A.2    Dhillon, N.3    Roberts, G.A.4    Cortes, J.5    Leadlay, P.F.6
  • 48
    • 0002741237 scopus 로고    scopus 로고
    • Toxic and non-toxic strains of the cyanobacterium Microcystis aeruginosa contain sequences homologous to peptide synthetase genes
    • Meißner, K., Dittman, E., and Borner, T. (1996) Toxic and non-toxic strains of the cyanobacterium Microcystis aeruginosa contain sequences homologous to peptide synthetase genes. FEMS Microbiol. Lett. 135, 295-303
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 295-303
    • Meißner, K.1    Dittman, E.2    Borner, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.