메뉴 건너뛰기




Volumn 11, Issue 6, 2009, Pages 391-397

Heterologous production of non-ribosomal peptide LLD-ACV in Saccharomyces cerevisiae

Author keywords

Non ribosomal peptide synthetase; Phosphopantetheinyl transferase; S. cerevisiae; Secondary metabolites

Indexed keywords

ASPERGILLUS NIDULANS; BACILLUS SUBTILIS; BIOLOGICAL ACTIVITIES; CODON OPTIMIZATION; D-VALINE; ENCODING GENES; GENE COPY NUMBER; HETEROLOGOUS PRODUCTION; NON-RIBOSOMAL PEPTIDE SYNTHETASE; PENICILLIUM CHRYSOGENUM; PHOSPHOPANTETHEINYL TRANSFERASE; RATE LIMITING FACTORS; RIBOSOMAL PEPTIDES; S. CEREVISIAE; SACCHAROMYCES CEREVISIAE; SECONDARY METABOLITES; SYNTHETASES; YEAST GENOME; YEAST SACCHAROMYCES CEREVISIAE;

EID: 70449520062     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2009.08.002     Document Type: Article
Times cited : (37)

References (40)
  • 3
    • 19544372278 scopus 로고    scopus 로고
    • Context-dependent codon bias and messenger RNA longevity in the yeast transcriptome
    • Carlini D.B. Context-dependent codon bias and messenger RNA longevity in the yeast transcriptome. Mol. Biol. Evol. 22 (2005) 1403-1411
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1403-1411
    • Carlini, D.B.1
  • 4
    • 57649100762 scopus 로고    scopus 로고
    • Metabolic engineering for plant natural product biosynthesis in microbes
    • Chemler J.A., and Koffas M.A.G. Metabolic engineering for plant natural product biosynthesis in microbes. Curr. Opin. Biotechnol. 19 (2008) 597-605
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 597-605
    • Chemler, J.A.1    Koffas, M.A.G.2
  • 5
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: bringing together theory and experiment
    • Dobson C.M., and Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9 (1999) 92-101
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 6
    • 0033545834 scopus 로고    scopus 로고
    • Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5
    • Ehmann D.E., Gehring A.M., and Walsh C.T. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38 (1999) 6171-6177
    • (1999) Biochemistry , vol.38 , pp. 6171-6177
    • Ehmann, D.E.1    Gehring, A.M.2    Walsh, C.T.3
  • 7
    • 0035860821 scopus 로고    scopus 로고
    • Engineered biosynthesis of the peptide antibiotic bacitracin in the surrogate host Bacillus subtilis
    • Eppelmann K., Doekel S., and Marahiel M.A. Engineered biosynthesis of the peptide antibiotic bacitracin in the surrogate host Bacillus subtilis. J. Biol. Chem. 276 (2001) 34824-34831
    • (2001) J. Biol. Chem. , vol.276 , pp. 34824-34831
    • Eppelmann, K.1    Doekel, S.2    Marahiel, M.A.3
  • 8
    • 0034111426 scopus 로고    scopus 로고
    • A novel function of yeast fatty acid synthase. Subunit alpha is capable of self-pantetheinylation
    • Fichtlscherer F., Wellein C., Mittag M., and Schweizer E. A novel function of yeast fatty acid synthase. Subunit alpha is capable of self-pantetheinylation. Eur. J. Biochem. 267 (2000) 2666-2671
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2666-2671
    • Fichtlscherer, F.1    Wellein, C.2    Mittag, M.3    Schweizer, E.4
  • 9
  • 10
    • 44949114059 scopus 로고    scopus 로고
    • Heterologous production of secondary metabolites as pharmaceuticals in Saccharomyces cerevisiae
    • Huang B., Guo J., Yi B., Yu X., Sun L., and Chen W. Heterologous production of secondary metabolites as pharmaceuticals in Saccharomyces cerevisiae. Biotechnol. Lett. 30 (2008) 1121-1137
    • (2008) Biotechnol. Lett. , vol.30 , pp. 1121-1137
    • Huang, B.1    Guo, J.2    Yi, B.3    Yu, X.4    Sun, L.5    Chen, W.6
  • 11
    • 0021958933 scopus 로고
    • Codon usage and tRNA content in unicellular and multicellular organisms
    • Ikemura T. Codon usage and tRNA content in unicellular and multicellular organisms. Mol. Biol. Evol. 2 (1985) 13-34
    • (1985) Mol. Biol. Evol. , vol.2 , pp. 13-34
    • Ikemura, T.1
  • 12
    • 0033212786 scopus 로고    scopus 로고
    • Use of silent mutations in cDNA encoding human glutathione transferase M2-2 for optimized expression in Escherichia coli
    • Johansson A.S., Bolton-Grob R., and Mannervik B. Use of silent mutations in cDNA encoding human glutathione transferase M2-2 for optimized expression in Escherichia coli. Protein Expr. Purif. 17 (1999) 105-112
    • (1999) Protein Expr. Purif. , vol.17 , pp. 105-112
    • Johansson, A.S.1    Bolton-Grob, R.2    Mannervik, B.3
  • 13
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6 (1995) 494-500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 14
    • 0031905709 scopus 로고    scopus 로고
    • Production of a polyketide natural product in nonpolyketide-producing prokaryotic and eukaryotic hosts
    • Kealey J.T., Liu L., Santi D.V., Betlach M.C., and Barr P.J. Production of a polyketide natural product in nonpolyketide-producing prokaryotic and eukaryotic hosts. Proc. Natl. Acad. Sci. USA 95 (1998) 505-509
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 505-509
    • Kealey, J.T.1    Liu, L.2    Santi, D.V.3    Betlach, M.C.4    Barr, P.J.5
  • 15
    • 0038112130 scopus 로고    scopus 로고
    • The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans
    • Keszenman-Pereyra D., Lawrence S., Twfieg M.E., Price J., and Turner G. The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans. Curr. Genet. 43 (2003) 186-190
    • (2003) Curr. Genet. , vol.43 , pp. 186-190
    • Keszenman-Pereyra, D.1    Lawrence, S.2    Twfieg, M.E.3    Price, J.4    Turner, G.5
  • 16
    • 0029921158 scopus 로고    scopus 로고
    • A nonribosomal system of peptide biosynthesis
    • Kleinkauf H., and von Doehren H. A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236 (1996) 335-351
    • (1996) Eur. J. Biochem. , vol.236 , pp. 335-351
    • Kleinkauf, H.1    von Doehren, H.2
  • 18
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li Z., Xiong F., Lin Q., d'Anjou M., Daugulis A.J., Yang D.S., and Hew C.L. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expr. Purif. 21 (2001) 438-445
    • (2001) Protein Expr. Purif. , vol.21 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.6    Hew, C.L.7
  • 19
    • 0038141976 scopus 로고    scopus 로고
    • Colocalization of multiple DNA double-strand breaks at a single Rad52 repair centre
    • Lisby M., Mortensen U.H., and Rothstein R. Colocalization of multiple DNA double-strand breaks at a single Rad52 repair centre. Nat. Cell Biol. 5 (2003) 572-577
    • (2003) Nat. Cell Biol. , vol.5 , pp. 572-577
    • Lisby, M.1    Mortensen, U.H.2    Rothstein, R.3
  • 21
    • 0035813125 scopus 로고    scopus 로고
    • 4'-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis
    • Mootz H.D., Finking R., and Marahiel M.A. 4'-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J. Biol. Chem. 276 (2001) 37289-37298
    • (2001) J. Biol. Chem. , vol.276 , pp. 37289-37298
    • Mootz, H.D.1    Finking, R.2    Marahiel, M.A.3
  • 22
    • 33645057433 scopus 로고    scopus 로고
    • Metabolic pathway engineering for complex polyketide biosynthesis in Saccharomyces cerevisiae
    • Mutka S.C., Bondi S.M., Carney J.R., Da Silva N.A., and Kealey J.T. Metabolic pathway engineering for complex polyketide biosynthesis in Saccharomyces cerevisiae. FEMS Yeast Res. 6 (2005) 40-47
    • (2005) FEMS Yeast Res. , vol.6 , pp. 40-47
    • Mutka, S.C.1    Bondi, S.M.2    Carney, J.R.3    Da Silva, N.A.4    Kealey, J.T.5
  • 23
    • 50249084003 scopus 로고    scopus 로고
    • Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering
    • Olano C., Lombó F., Méndez C., and Salas J.A. Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering. Metab. Eng. 10 (2008) 281-292
    • (2008) Metab. Eng. , vol.10 , pp. 281-292
    • Olano, C.1    Lombó, F.2    Méndez, C.3    Salas, J.A.4
  • 24
    • 17444449538 scopus 로고    scopus 로고
    • Transfer RNA gene redundancy and translational selection in Saccharomyces cerevisiae
    • Percudani R., Pavesi A., and Ottonello S. Transfer RNA gene redundancy and translational selection in Saccharomyces cerevisiae. J. Mol. Biol. 268 (1997) 322-330
    • (1997) J. Mol. Biol. , vol.268 , pp. 322-330
    • Percudani, R.1    Pavesi, A.2    Ottonello, S.3
  • 25
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin
    • Quadri L.E., Sello J., Keating T.A., Weinreb P.H., and Walsh C.T. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5 (1998) 631-645
    • (1998) Chem. Biol. , vol.5 , pp. 631-645
    • Quadri, L.E.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 26
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri L.E., Weinreb P.H., Lei M., Nakano M.M., Zuber P., and Walsh C.T. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37 (1998) 1585-1595
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 27
    • 0036270546 scopus 로고    scopus 로고
    • Cloning-free genome alterations in Saccharomyces cerevisiae using adaptamer-mediated PCR
    • Reid R., Lisby M., and Rothstein R. Cloning-free genome alterations in Saccharomyces cerevisiae using adaptamer-mediated PCR. Methods Enzymol. 350 (2002) 258-277
    • (2002) Methods Enzymol. , vol.350 , pp. 258-277
    • Reid, R.1    Lisby, M.2    Rothstein, R.3
  • 28
    • 70449519545 scopus 로고    scopus 로고
    • Schoergendorfer, K, Kurnsteiner, H, 2005. New isolated Penicillium chrysogenum 4'-phosphopantethein transferase PPTase protein, useful for producing penicillin G or penicillin V. Patent WO2005040369
    • Schoergendorfer, K., Kurnsteiner, H., 2005. New isolated Penicillium chrysogenum 4'-phosphopantethein transferase PPTase protein, useful for producing penicillin G or penicillin V. Patent WO2005040369.
  • 29
  • 30
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics
    • Sieber S.A., and Marahiel M.A. Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics. Chem. Rev. 105 (2005) 715-738
    • (2005) Chem. Rev. , vol.105 , pp. 715-738
    • Sieber, S.A.1    Marahiel, M.A.2
  • 31
    • 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. 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 (1990) 2743-2750
    • (1990) EMBO J. , vol.9 , pp. 2743-2750
    • Smith, D.J.1    Earl, A.J.2    Turner, G.3
  • 34
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura S., and Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24 (2006) 179-185
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 35
    • 34247516876 scopus 로고    scopus 로고
    • The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
    • Vera A., González-Montalbán N., Arís A., and Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. 96 (2007) 1101-1106
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 1101-1106
    • Vera, A.1    González-Montalbán, N.2    Arís, A.3    Villaverde, A.4
  • 38
    • 50249105159 scopus 로고    scopus 로고
    • Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply
    • Wattanachaisaereekul S., Lantz A.E., Nielsen M.L., and Nielsen J. Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply. Metab. Eng. 10 (2008) 246-254
    • (2008) Metab. Eng. , vol.10 , pp. 246-254
    • Wattanachaisaereekul, S.1    Lantz, A.E.2    Nielsen, M.L.3    Nielsen, J.4
  • 39
    • 0028251292 scopus 로고
    • Disruption of the cyclosporin synthetase gene of Tolypocladium niveum
    • Weber G., and Leitner E. Disruption of the cyclosporin synthetase gene of Tolypocladium niveum. Curr. Genet. 26 (1994) 461-467
    • (1994) Curr. Genet. , vol.26 , pp. 461-467
    • Weber, G.1    Leitner, E.2
  • 40
    • 0030686417 scopus 로고    scopus 로고
    • Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli
    • Weickert M.J., Pagratis M., Curry S.R., and Blackmore R. Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli. Appl. Environ. Microbiol. 63 (1997) 4313-4320
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4313-4320
    • Weickert, M.J.1    Pagratis, M.2    Curry, S.R.3    Blackmore, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.