메뉴 건너뛰기




Volumn 51, Issue 3, 2007, Pages 946-957

Cloning and characterization of the pyrrolomycin biosynthetic gene clusters from Actinosporangium vitaminophilum ATCC 31673 and Streptomyces sp. strain UC 11065

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL DNA; NITRATE REDUCTASE; POLYKETIDE; PYOLUTEORIN; PYRROLOMYCIN; PYRROLOMYCIN A; PYRROLOMYCIN B; PYRROLOMYCIN C; PYRROLOMYCIN D; PYRROLOMYCIN G; PYRROLOMYCIN H; PYRROLOMYCIN I; PYRROLOMYCIN J; PYRROXAMYCIN; UNCLASSIFIED DRUG;

EID: 33847681412     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.01214-06     Document Type: Article
Times cited : (64)

References (49)
  • 1
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia-coli to Streptomyces spp
    • Bierman, M., R. Logan, K. Obrien, E. T. Seno, R. N. Rao, and B. E. Schoner. 1992. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia-coli to Streptomyces spp. Gene 116:43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    Obrien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 4
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • Challis, G. L., J. Ravel, and C. A. Townsend. 2000. Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem. Biol. 7:211-224.
    • (2000) Chem. Biol , vol.7 , pp. 211-224
    • Challis, G.L.1    Ravel, J.2    Townsend, C.A.3
  • 7
    • 25444465451 scopus 로고    scopus 로고
    • Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis
    • Dorrestein, P. C., E. Yeh, S. Garneau-Tsodikova, N. L. Kelleher, and C. T. Walsh. 2005. Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis. Proc. Natl. Acad. Sci. USA 102:13843-13848.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13843-13848
    • Dorrestein, P.C.1    Yeh, E.2    Garneau-Tsodikova, S.3    Kelleher, N.L.4    Walsh, C.T.5
  • 10
    • 0348087044 scopus 로고    scopus 로고
    • Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore synthesis in Pseudomonas aeruginosa
    • Finking, R., J. Solsbacher, D. Konz, M. Schobert, A. Schafer, D. Jahn, and M. A. Marahiel. 2002. Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore synthesis in Pseudomonas aeruginosa. J. Biol. Chem. 277:50293-50302.
    • (2002) J. Biol. Chem , vol.277 , pp. 50293-50302
    • Finking, R.1    Solsbacher, J.2    Konz, D.3    Schobert, M.4    Schafer, A.5    Jahn, D.6    Marahiel, M.A.7
  • 11
    • 0030908709 scopus 로고    scopus 로고
    • Four genes from Pseudomonas fluorescens that encode the biosynthesis of pyrrolnitrin
    • Hammer, P. E., D. S. Hill, S. T. Lam, K.-H. van Pee, and J. M. Ligon. 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 Pee, K.-H.4    Ligon, J.M.5
  • 12
    • 1642388928 scopus 로고    scopus 로고
    • Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: Involvement of an unprecedented N-oxygenase
    • He, J., and C. Hertweck. 2004. Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: involvement of an unprecedented N-oxygenase. J. Am. Chem. Soc. 126:3694-3695.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3694-3695
    • He, J.1    Hertweck, C.2
  • 13
    • 0346968190 scopus 로고    scopus 로고
    • Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster
    • He, J., and C. Hertweck. 2003. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem. Biol. 10:1225-1232.
    • (2003) Chem. Biol , vol.10 , pp. 1225-1232
    • He, J.1    Hertweck, C.2
  • 14
    • 0033636188 scopus 로고    scopus 로고
    • The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin A production and pathogenicity
    • Healy, F. G., M. Wach, S. B. Krasnoff, D. M. Gibson, and R. Loria. 2000. The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin A production and pathogenicity. Mol. Microbiol. 38:794-804.
    • (2000) Mol. Microbiol , vol.38 , pp. 794-804
    • Healy, F.G.1    Wach, M.2    Krasnoff, S.B.3    Gibson, D.M.4    Loria, R.5
  • 15
    • 0035068571 scopus 로고    scopus 로고
    • Role of type II thioesterases: Evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units
    • Heathcote, M. L., J. Staunton, and P. F. Leadlay. 2001. Role of type II thioesterases: evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units. Chem. Biol. 8:207-220.
    • (2001) Chem. Biol , vol.8 , pp. 207-220
    • Heathcote, M.L.1    Staunton, J.2    Leadlay, P.F.3
  • 16
    • 0042424849 scopus 로고    scopus 로고
    • A specific role of the Saccharopolyspora erythraea thioesterase II gene in the function of modular polyketide synthases
    • Hu, Z., B. A. Pfeifer, E. Chao, S. Murli, J. Kealey, J. R. Carney, G. Ashley, C. Khosla, and C. R. Hutchinson. 2003. A specific role of the Saccharopolyspora erythraea thioesterase II gene in the function of modular polyketide synthases. Microbiology 149:2213-2225.
    • (2003) Microbiology , vol.149 , pp. 2213-2225
    • Hu, Z.1    Pfeifer, B.A.2    Chao, E.3    Murli, S.4    Kealey, J.5    Carney, J.R.6    Ashley, G.7    Khosla, C.8    Hutchinson, C.R.9
  • 17
    • 1542315179 scopus 로고    scopus 로고
    • A gene cluster encoding resistomycin biosynthesis in Streptomyces resistomycificus; exploring polyketide cyclization beyond linear and angucyclic patterns
    • Jakobi, K., and C. Hertweck. 2004. A gene cluster encoding resistomycin biosynthesis in Streptomyces resistomycificus; exploring polyketide cyclization beyond linear and angucyclic patterns. J. Am. Chem. Soc. 126:2298-2299.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 2298-2299
    • Jakobi, K.1    Hertweck, C.2
  • 18
    • 3543029827 scopus 로고    scopus 로고
    • Tuning a nitrate reductase for function. The first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties
    • Jepson, B. J., L. J. Anderson, L. M. Rubio, C. J. Taylor, C. S. Butler, E. Flores, A. Herrero, J. N. Butt, and D. J. Richardson. 2004. Tuning a nitrate reductase for function. The first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties. J. Biol. Chem. 279:32212-32218.
    • (2004) J. Biol. Chem , vol.279 , pp. 32212-32218
    • Jepson, B.J.1    Anderson, L.J.2    Rubio, L.M.3    Taylor, C.J.4    Butler, C.S.5    Flores, E.6    Herrero, A.7    Butt, J.N.8    Richardson, D.J.9
  • 19
    • 0019855430 scopus 로고
    • Structure of pyrrolomycin B, a chlorinated nitro-pyrrole antibiotic
    • Kaneda, M., S. Nakamura, N. Ezaki, and Y. Iitaka. 1981. Structure of pyrrolomycin B, a chlorinated nitro-pyrrole antibiotic. J. Antibiot. (Tokyo) 34:1366-1368.
    • (1981) J. Antibiot. (Tokyo) , vol.34 , pp. 1366-1368
    • Kaneda, M.1    Nakamura, S.2    Ezaki, N.3    Iitaka, Y.4
  • 22
    • 0037073685 scopus 로고    scopus 로고
    • Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin
    • Kim, B. S., T. A. Cropp, B. J. Beck, D. H. Sherman, and K. A. Reynolds. 2002. Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin. J. Biol. Chem. 277:48028-48034.
    • (2002) J. Biol. Chem , vol.277 , pp. 48028-48034
    • Kim, B.S.1    Cropp, T.A.2    Beck, B.J.3    Sherman, D.H.4    Reynolds, K.A.5
  • 24
    • 0019808017 scopus 로고
    • Structure and synthesis of pyrrolomycin A, a chlorinated nitro-pyrrole antibiotic
    • Koyama, M., Y. Kodama, T. Tsuruoka, N. Ezaki, T. Niwa, and S. Inouye. 1981. Structure and synthesis of pyrrolomycin A, a chlorinated nitro-pyrrole antibiotic. J. Antibiot. (Tokyo) 34:1569-1576.
    • (1981) J. Antibiot. (Tokyo) , vol.34 , pp. 1569-1576
    • Koyama, M.1    Kodama, Y.2    Tsuruoka, T.3    Ezaki, N.4    Niwa, T.5    Inouye, S.6
  • 26
    • 16744369183 scopus 로고    scopus 로고
    • A probable link between the DedA protein and resistance to selenite
    • Ledgham, F., B. Quest, T. Vallaeys, M. Mergeay, and J. Coves. 2005. A probable link between the DedA protein and resistance to selenite. Res. Microbiol. 156:367-374.
    • (2005) Res. Microbiol , vol.156 , pp. 367-374
    • Ledgham, F.1    Quest, B.2    Vallaeys, T.3    Mergeay, M.4    Coves, J.5
  • 27
    • 27744589609 scopus 로고    scopus 로고
    • Reconstitution and characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidation
    • Lee, J., M. Simurdiak, and H. Zhao. 2005. Reconstitution and characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidation. J. Biol. Chem. 280:36719-36727.
    • (2005) J. Biol. Chem , vol.280 , pp. 36719-36727
    • Lee, J.1    Simurdiak, M.2    Zhao, H.3
  • 28
    • 0026575735 scopus 로고
    • Analysis of Streptomyces-avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector
    • Macneil, D. J., K. M. Gewain, C. L. Ruby, G. Dezeny, P. H. Gibbons, and T. Macneil. 1992. Analysis of Streptomyces-avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector. Gene 111:61-68.
    • (1992) Gene , vol.111 , pp. 61-68
    • Macneil, D.J.1    Gewain, K.M.2    Ruby, C.L.3    Dezeny, G.4    Gibbons, P.H.5    Macneil, T.6
  • 29
    • 0025898429 scopus 로고
    • Pyrrolomycin group antibiotics inhibit substance P-induced release of myeloperoxidase from human polymorphonuclear leukocytes
    • Masuda, K., K. Suzuki, A. Ishida-Okawara, S. Mizuno, and K. Hotta. 1991. Pyrrolomycin group antibiotics inhibit substance P-induced release of myeloperoxidase from human polymorphonuclear leukocytes. J. Antibiot. (Tokyo) 44:533-540.
    • (1991) J. Antibiot. (Tokyo) , vol.44 , pp. 533-540
    • Masuda, K.1    Suzuki, K.2    Ishida-Okawara, A.3    Mizuno, S.4    Hotta, K.5
  • 30
    • 1542314758 scopus 로고    scopus 로고
    • Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide
    • Monzani, E., R. Roncone, M. Galliano, W. H. Koppenol, and L. Casella. 2004. Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide. Eur. J. Biochem. 271:895-906.
    • (2004) Eur. J. Biochem , vol.271 , pp. 895-906
    • Monzani, E.1    Roncone, R.2    Galliano, M.3    Koppenol, W.H.4    Casella, L.5
  • 32
    • 0032936731 scopus 로고    scopus 로고
    • Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescent Pf-5
    • Nowak-Thompson, B., N. Chaney, J. S. Wing, S. J. Gould, and J. E. Loper. 1999. Characterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescent Pf-5. J. Bacteriol. 181:2166-2174.
    • (1999) J. Bacteriol , vol.181 , pp. 2166-2174
    • Nowak-Thompson, B.1    Chaney, N.2    Wing, J.S.3    Gould, S.J.4    Loper, J.E.5
  • 33
    • 0031578827 scopus 로고    scopus 로고
    • Identification and sequence analysis of the genes encoding a polyketide synthase required for pyoluteorin biosynthesis in Pseudomonas fluorescens Pf-5
    • Nowak-Thompson, B., S. J. Gould, and J. E. Loper. 1997. Identification and sequence analysis of the genes encoding a polyketide synthase required for pyoluteorin biosynthesis in Pseudomonas fluorescens Pf-5. Gene 204:17-24.
    • (1997) Gene , vol.204 , pp. 17-24
    • Nowak-Thompson, B.1    Gould, S.J.2    Loper, J.E.3
  • 34
    • 0036023485 scopus 로고    scopus 로고
    • Use of degenerate primers and touch-down PCR to amplify a halogenase gene fragment from Streptomyces venezuelae ISP5230
    • Piraee, M., and L. C. Vining. 2002. Use of degenerate primers and touch-down PCR to amplify a halogenase gene fragment from Streptomyces venezuelae ISP5230. J. Ind. Microbiol. Biotechnol. 29:1-5.
    • (2002) J. Ind. Microbiol. Biotechnol , vol.29 , pp. 1-5
    • Piraee, M.1    Vining, L.C.2
  • 36
    • 3042802321 scopus 로고    scopus 로고
    • Peroxidase catalyzed nitration of tryptophan derivatives. Mechanism, products and comparison with chemical nitrating agents
    • Sala, A., S. Nicolis, R. Roncone, L. Casella, and E. Monzani. 2004. Peroxidase catalyzed nitration of tryptophan derivatives. Mechanism, products and comparison with chemical nitrating agents. Eur. J. Biochem. 271:2841-2852.
    • (2004) Eur. J. Biochem , vol.271 , pp. 2841-2852
    • Sala, A.1    Nicolis, S.2    Roncone, R.3    Casella, L.4    Monzani, E.5
  • 39
    • 0027301951 scopus 로고
    • Tetracenomycin F1 monooxygenase: Oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens
    • Shen, B., and C. R. Hutchinson. 1993. Tetracenomycin F1 monooxygenase: oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens. Biochemistry 32:6656-6663.
    • (1993) Biochemistry , vol.32 , pp. 6656-6663
    • Shen, B.1    Hutchinson, C.R.2
  • 41
    • 33747196928 scopus 로고    scopus 로고
    • A new class of arylamine oxygenases: Evidence that p-aminobenzoate N-oxygenase (AurF) is a di-iron enzyme and further mechanistic studies
    • Simurdiak, M., J. Lee, and H. Zhao. 2006. A new class of arylamine oxygenases: evidence that p-aminobenzoate N-oxygenase (AurF) is a di-iron enzyme and further mechanistic studies. Chem. Biol. Chem. 7:1169-1172.
    • (2006) Chem. Biol. Chem , vol.7 , pp. 1169-1172
    • Simurdiak, M.1    Lee, J.2    Zhao, H.3
  • 43
    • 0038167479 scopus 로고    scopus 로고
    • The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species
    • Sosio, M., S. Stinchi, F. Beltrametti, A. Lazzarini, and S. Donadio. 2003. The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species. Chem. Biol. 10:541-549.
    • (2003) Chem. Biol , vol.10 , pp. 541-549
    • Sosio, M.1    Stinchi, S.2    Beltrametti, F.3    Lazzarini, A.4    Donadio, S.5
  • 44
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus, T., H. D. Mootz, and M. A. Marahiel. 1999. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 6:493-505.
    • (1999) Chem. Biol , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 45
    • 0036008844 scopus 로고    scopus 로고
    • Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis
    • Thomas, M. G., M. D. Burkart, and C. T. Walsh. 2002. Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis. Chem. Biol. 9:171-184.
    • (2002) Chem. Biol , vol.9 , pp. 171-184
    • Thomas, M.G.1    Burkart, M.D.2    Walsh, C.T.3
  • 46
    • 0034102009 scopus 로고    scopus 로고
    • Biosynthesis of pyrrolnitrin and other phenylpyrrole derivatives by bacteria
    • van Pee, K.-H., and J. M. Ligon. 2000. Biosynthesis of pyrrolnitrin and other phenylpyrrole derivatives by bacteria. Nat. Prod. Rep. 17:157-164.
    • (2000) Nat. Prod. Rep , vol.17 , pp. 157-164
    • van Pee, K.-H.1    Ligon, J.M.2
  • 47
    • 0002268707 scopus 로고
    • Chloramphenicol
    • L. C. Vining and C. Stuttard ed, Butterworth-Heinemann, Boston, MA
    • Vining, L. C., and C. Stuttard. 1994. Chloramphenicol, p. 505-530. In L. C. Vining and C. Stuttard (ed.), Genetics and biochemistry of antibiotic production. Butterworth-Heinemann, Boston, MA.
    • (1994) Genetics and biochemistry of antibiotic production , pp. 505-530
    • Vining, L.C.1    Stuttard, C.2
  • 48
    • 4143127694 scopus 로고    scopus 로고
    • A novel halogenase gene from the pentachloropseudilin producer Actinoplanes sp. ATCC 33002 and detection of in vitro halogenase activity
    • Wynands, I., and K. H. van Pee. 2004. A novel halogenase gene from the pentachloropseudilin producer Actinoplanes sp. ATCC 33002 and detection of in vitro halogenase activity. FEMS Microbiol. Lett. 237:363-367.
    • (2004) FEMS Microbiol. Lett , vol.237 , pp. 363-367
    • Wynands, I.1    van Pee, K.H.2
  • 49
    • 17844408703 scopus 로고    scopus 로고
    • A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005
    • Zehner, S., A. Kotzsch, B. Bister, R. D. Sussmuth, C. Mendez, J. A. Salas, and K. H. van Pee. 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    Sussmuth, R.D.4    Mendez, C.5    Salas, J.A.6    van Pee, K.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.