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Volumn 77, Issue 4, 2011, Pages 1501-1507

Reconstitution of the FK228 biosynthetic pathway reveals cross talk between modular polyketide synthases and fatty acid synthase

Author keywords

[No Author keywords available]

Indexed keywords

ANAEROBIC CULTIVATION; BACTERIAL STRAINS; BIO-AGENTS; BIOSYNTHETIC ENZYMES; BIOSYNTHETIC PATHWAY; CHAIN ELONGATION; CHROMOBACTERIUM VIOLACEUM; COENZYME A; COMPLEMENTATION; E. COLI; ENCODING GENES; ESCHERICHIA COLI CELLS; ESSENTIAL GENE; FATTY ACID BIOSYNTHESIS; FATTY ACID SYNTHASE; GENE CLUSTERS; GENE PRODUCTS; NATURAL PRODUCTS; NONRIBOSOMAL PEPTIDE SYNTHETASES; POLYKETIDE SYNTHASES; POLYKETIDES; SECONDARY METABOLISM;

EID: 79953208066     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01513-10     Document Type: Article
Times cited : (29)

References (33)
  • 1
    • 0031105099 scopus 로고    scopus 로고
    • A fatty acid synthase gene in Cochliobolus carbonum required for production of HC-toxin, cyclo(D-prolyl-L-alanyl-Dalanyl-L-2-amino-9, 10-epoxi-8-oxodecanoyl)
    • Ahn, J. H., and J. D. Walton. 1997. A fatty acid synthase gene in Cochliobolus carbonum required for production of HC-toxin, cyclo(D-prolyl-L-alanyl-Dalanyl-L-2-amino-9, 10-epoxi-8-oxodecanoyl). Mol. Plant Microbe Interact. 10:207-214.
    • (1997) Mol. Plant Microbe Interact. , vol.10 , pp. 207-214
    • Ahn, J.H.1    Walton, J.D.2
  • 3
    • 0032474472 scopus 로고    scopus 로고
    • Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis
    • Bao, W., E. Wendt-Pienkowski, and C. R. Hutchinson. 1998. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37:8132-8138.
    • (1998) Biochemistry , vol.37 , pp. 8132-8138
    • Bao, W.1    Wendt-Pienkowski, E.2    Hutchinson, C.R.3
  • 4
    • 0141758343 scopus 로고    scopus 로고
    • The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability
    • Brazilian National Genome Project Consortium
    • Brazilian National Genome Project Consortium. 2003. The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability. Proc. Natl. Acad. Sci. U. S. A. 100:11660-11665.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11660-11665
  • 6
    • 64049099639 scopus 로고    scopus 로고
    • Type I polyketide synthases that require discrete acyltransferases
    • Cheng, Y.-Q., J. M. Coughlin, S. K. Lim, and B. Shen. 2009. Type I polyketide synthases that require discrete acyltransferases. Methods Enzymol. 459:165-186.
    • (2009) Methods Enzymol , vol.459 , pp. 165-186
    • Cheng, Y.-Q.1    Coughlin, J.M.2    Lim, S.K.3    Shen, B.4
  • 7
    • 0037452928 scopus 로고    scopus 로고
    • Type I polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis
    • Cheng, Y.-Q., G. L. Tang, and B. Shen. 2003. Type I polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 100:3149-3154.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3149-3154
    • Cheng, Y.-Q.1    Tang, G.L.2    Shen, B.3
  • 8
    • 34249895594 scopus 로고    scopus 로고
    • Characterization of a gene cluster responsible for the biosynthesis of anticancer agent FK228 in Chromobacterium violaceum no. 968
    • Cheng, Y.-Q., M. Yang, and A. M. Matter. 2007. Characterization of a gene cluster responsible for the biosynthesis of anticancer agent FK228 in Chromobacterium violaceum no. 968. Appl. Environ. Microbiol. 73:3460-3469.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3460-3469
    • Cheng, Y.-Q.1    Yang, M.2    Matter, A.M.3
  • 9
    • 23044461889 scopus 로고    scopus 로고
    • An improved method for rapid generation of unmarked Pseudomonas aeruginosa deletion mutants
    • Choi, K. H., and H. P. Schweizer. 2005. An improved method for rapid generation of unmarked Pseudomonas aeruginosa deletion mutants. BMC Microbiol. 5:30.
    • (2005) BMC Microbiol , vol.5 , pp. 30
    • Choi, K.H.1    Schweizer, H.P.2
  • 10
    • 33646092296 scopus 로고    scopus 로고
    • The phosphopantetheinyl transferase superfamily: phylogenetic analysis and functional implications in cyanobacteria
    • Copp, J. N., and B. A. Neilan. 2006. The phosphopantetheinyl transferase superfamily: phylogenetic analysis and functional implications in cyanobacteria. Appl. Environ. Microbiol. 72:2298-2305.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2298-2305
    • Copp, J.N.1    Neilan, B.A.2
  • 11
    • 50149095793 scopus 로고    scopus 로고
    • The genome sequencer FLX system-longer reads, more applications, straightforward bioinformatics and more complete data sets
    • Droege, M., and B. Hill. 2008. The genome sequencer FLX system-longer reads, more applications, straightforward bioinformatics and more complete data sets. J. Biotechnol. 136:3-10.
    • (2008) J. Biotechnol. , vol.136 , pp. 3-10
    • Droege, M.1    Hill, B.2
  • 12
    • 0037143585 scopus 로고    scopus 로고
    • Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity
    • Florova, G., G. Kazanina, and K. A. Reynolds. 2002. Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity. Biochemistry 41:10462-10471.
    • (2002) Biochemistry , vol.41 , pp. 10462-10471
    • Florova, G.1    Kazanina, G.2    Reynolds, K.A.3
  • 13
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai, R., et al. 2002. FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res. 62:4916-4921.
    • (2002) Cancer Res , vol.62 , pp. 4916-4921
    • Furumai, R.1
  • 14
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang, T. T., R. R. Karkhoff-Schweizer, A. J. Kutchma, and H. P. Schweizer. 1998. A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212:77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 15
    • 77951166486 scopus 로고    scopus 로고
    • Functional characterization and manipulation of the apicidin biosynthetic pathway in Fusarium semitectum
    • Jin, J. M., et al. 2010. Functional characterization and manipulation of the apicidin biosynthetic pathway in Fusarium semitectum. Mol. Microbiol. 76: 456-466.
    • (2010) Mol. Microbiol. , vol.76 , pp. 456-466
    • Jin, J.M.1
  • 16
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily-the phosphopantetheinyl transferases
    • Lambalot, R. H., et al. 1996. A new enzyme superfamily-the phosphopantetheinyl transferases. Chem. Biol. 3:923-936.
    • (1996) Chem. Biol. , vol.3 , pp. 923-936
    • Lambalot, R.H.1
  • 17
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane, A. A., and B. A. Chabner. 2009. Histone deacetylase inhibitors in cancer therapy. J. Clin. Oncol. 27:5459-5468.
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 18
    • 33646571612 scopus 로고    scopus 로고
    • Broad host range vectors for stable genomic library construction
    • Lynch, M. D., and R. T. Gill. 2006. Broad host range vectors for stable genomic library construction. Biotechnol. Bioeng. 94:151-158.
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 151-158
    • Lynch, M.D.1    Gill, R.T.2
  • 19
    • 1842613536 scopus 로고    scopus 로고
    • Clostridia in cancer therapy
    • Minton, N. P. 2003. Clostridia in cancer therapy. Nat. Rev. Microbiol. 1:237-242.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 237-242
    • Minton, N.P.1
  • 20
    • 0035813125 scopus 로고    scopus 로고
    • 4′-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis
    • Mootz, H. D., R. Finking, and M. A. Marahiel. 2001. 4′-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J. Biol. Chem. 276:37289-37298.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37289-37298
    • Mootz, H.D.1    Finking, R.2    Marahiel, M.A.3
  • 21
    • 77949342576 scopus 로고    scopus 로고
    • StatBite: FDA oncology drug product approvals in 2009
    • National Cancer Institute
    • National Cancer Institute. 2010. StatBite: FDA oncology drug product approvals in 2009. J. Natl. Cancer Inst. 102:219.
    • (2010) J. Natl. Cancer Inst. , vol.102 , pp. 219
  • 22
    • 79953173267 scopus 로고    scopus 로고
    • New insights into the genetic organization of the FK228 biosynthetic gene cluster in Chromobacterium violaceum strain 968
    • Potharla, V. Y., S. R. Wesener, and Y.-Q. Cheng. 2011. New insights into the genetic organization of the FK228 biosynthetic gene cluster in Chromobacterium violaceum strain 968. Appl. Environ. Microbiol. 77:1508-1511.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1508-1511
    • Potharla, V.Y.1    Wesener, S.R.2    Cheng, Y.-Q.3
  • 23
    • 0029059472 scopus 로고
    • Purification of a malonyltransferase from Streptomyces coelicolor A3(2) and analysis of its genetic determinant
    • Revill, W. P., M. J. Bibb, and D. A. Hopwood. 1995. Purification of a malonyltransferase from Streptomyces coelicolor A3(2) and analysis of its genetic determinant. J. Bacteriol. 177:3946-3952.
    • (1995) J. Bacteriol. , vol.177 , pp. 3946-3952
    • Revill, W.P.1    Bibb, M.J.2    Hopwood, D.A.3
  • 25
    • 15744381452 scopus 로고    scopus 로고
    • Functional cross-talk between fatty acid synthesis and nonribosomal peptide synthesis in quinoxaline antibiotic-producing streptomycetes
    • Schmoock, G., et al. 2005. Functional cross-talk between fatty acid synthesis and nonribosomal peptide synthesis in quinoxaline antibiotic-producing streptomycetes. J. Biol. Chem. 280:4339-4349.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4339-4349
    • Schmoock, G.1
  • 26
    • 0037398774 scopus 로고    scopus 로고
    • Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms
    • Shen, B. 2003. Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms. Curr. Opin. Chem. Biol. 7:285-295.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 285-295
    • Shen, B.1
  • 27
    • 51149101636 scopus 로고    scopus 로고
    • Biochemistry: an enzyme assembly line
    • Smith, J. L., and D. H. Sherman. 2008. Biochemistry: an enzyme assembly line. Science 321:1304-1305.
    • (2008) Science , vol.321 , pp. 1304-1305
    • Smith, J.L.1    Sherman, D.H.2
  • 28
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: a millennium review
    • Staunton, J., and K. J. Weissman. 2001. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18:380-416.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 29
    • 0029125339 scopus 로고
    • Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and polyketide biosynthesis
    • Summers, R. G., A. Ali, B. Shen, W. A. Wessel, and C. R. Hutchinson. 1995. Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and polyketide biosynthesis. Biochemistry 34:9389-9402.
    • (1995) Biochemistry , vol.34 , pp. 9389-9402
    • Summers, R.G.1    Ali, A.2    Shen, B.3    Wessel, W.A.4    Hutchinson, C.R.5
  • 30
    • 1142293995 scopus 로고    scopus 로고
    • Leinamycin biosynthesis revealing unprecedented architectural complexity for a hybrid polyketide synthase and nonribosomal peptide synthetase
    • Tang, G. L., Y.-Q. Cheng, and B. Shen. 2004. Leinamycin biosynthesis revealing unprecedented architectural complexity for a hybrid polyketide synthase and nonribosomal peptide synthetase. Chem. Biol. 11:33-45.
    • (2004) Chem. Biol. , vol.11 , pp. 33-45
    • Tang, G.L.1    Cheng, Y.-Q.2    Shen, B.3
  • 31
    • 67649522901 scopus 로고    scopus 로고
    • An FAD-dependent pyridine nucleotide-disulfide oxidoreductase is involved in disulfide bond formation in FK228 anticancer depsipeptide
    • Wang, C., S. R. Wesener, H. Zhang, and Y.-Q. Cheng. 2009. An FAD-dependent pyridine nucleotide-disulfide oxidoreductase is involved in disulfide bond formation in FK228 anticancer depsipeptide. Chem. Biol. 16:585-593.
    • (2009) Chem. Biol. , vol.16 , pp. 585-593
    • Wang, C.1    Wesener, S.R.2    Zhang, H.3    Cheng, Y.-Q.4
  • 32
    • 33846576538 scopus 로고    scopus 로고
    • Facultative or obligate anaerobic bacteria have the potential for multimodality therapy of solid tumours
    • Wei, M. Q., et al. 2007. Facultative or obligate anaerobic bacteria have the potential for multimodality therapy of solid tumours. Eur. J. Cancer 43:490-496.
    • (2007) Eur. J. Cancer , vol.43 , pp. 490-496
    • Wei, M.Q.1
  • 33
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: past, present and future
    • Yoo, C. B., and P. A. Jones. 2006. Epigenetic therapy of cancer: past, present and future. Nat. Rev. Drug Discov. 5:37-50.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.