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Volumn 8, Issue , 2017, Pages

Dissection of goadsporin biosynthesis by in vitro reconstitution leading to designer analogues expressed in vivo

Author keywords

[No Author keywords available]

Indexed keywords

GOADSPORIN; GODD PEPTIDE; GODE PEPTIDE; GODF PEPTIDE; GODH PEPTIDE; NATURAL PRODUCT; PEPTIDE; PYRROLE DERIVATIVE; RECOMBINANT PROTEIN; SYNTHETIC DNA; TRANSFER RNA; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN;

EID: 85011857408     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms14207     Document Type: Article
Times cited : (64)

References (37)
  • 1
    • 0035702646 scopus 로고    scopus 로고
    • Goadsporin, a chemical substance which promotes secondary metabolism and morphogenesis in streptomycetes. II. Structure determination
    • Igarashi, Y. et al. Goadsporin, a chemical substance which promotes secondary metabolism and morphogenesis in streptomycetes. II. Structure determination. J. Antibiot. (Tokyo) 54, 1045-1053 (2001).
    • (2001) J. Antibiot. (Tokyo) , vol.54 , pp. 1045-1053
    • Igarashi, Y.1
  • 2
    • 0035704064 scopus 로고    scopus 로고
    • Goadsporin, a chemical substance which promotes secondary metabolism and morphogenesis in streptomycetes. I. Purification and characterization
    • Onaka, H., Tabata, H., Igarashi, Y., Sato, Y. & Furumai, T. Goadsporin, a chemical substance which promotes secondary metabolism and morphogenesis in streptomycetes. I. Purification and characterization. J. Antibiot. (Tokyo) 54, 1036-1044 (2001).
    • (2001) J. Antibiot. (Tokyo) , vol.54 , pp. 1036-1044
    • Onaka, H.1    Tabata, H.2    Igarashi, Y.3    Sato, Y.4    Furumai, T.5
  • 3
    • 29244470531 scopus 로고    scopus 로고
    • Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp
    • Onaka, H., Nakaho, M., Hayashi, K., Igarashi, Y. & Furumai, T. Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584. Microbiology 151, 3923-3933 (2005).
    • (2005) TP-A0584. Microbiology , vol.151 , pp. 3923-3933
    • Onaka, H.1    Nakaho, M.2    Hayashi, K.3    Igarashi, Y.4    Furumai, T.5
  • 4
    • 84870918230 scopus 로고    scopus 로고
    • Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature
    • Arnison, P. G. et al. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature. Nat. Prod. Rep. 30, 108-160 (2013).
    • (2013) Nat. Prod. Rep. , vol.30 , pp. 108-160
    • Arnison, P.G.1
  • 5
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Li, Y. M., Milne, J. C., Madison, L. L., Kolter, R. & Walsh, C. T. From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 274, 1188-1193 (1996).
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 6
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
    • Dunbar, K. L., Melby, J. O. & Mitchell, D. A. YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations. Nat. Chem. Biol. 8, 569-575 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 7
    • 84922019867 scopus 로고    scopus 로고
    • Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis
    • Dunbar, K. L. et al. Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Nat. Chem. Biol. 10, 823-829 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 823-829
    • Dunbar, K.L.1
  • 8
    • 84890606879 scopus 로고    scopus 로고
    • The cyanobactin heterocyclase enzyme: A processive adenylase that operates with a defined order of reaction
    • Koehnke, J. et al. The cyanobactin heterocyclase enzyme: A processive adenylase that operates with a defined order of reaction. Angew. Chem. Int. Ed. Engl. 52, 13991-13996 (2013).
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 13991-13996
    • Koehnke, J.1
  • 9
    • 18844410256 scopus 로고    scopus 로고
    • Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella
    • Schmidt, E. W. et al. Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. Proc. Natl Acad. Sci. USA 102, 7315-7320 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7315-7320
    • Schmidt, E.W.1
  • 10
    • 84892775984 scopus 로고    scopus 로고
    • Orchestration of enzymatic processing by thiazole/oxazole-modified microcin dehydrogenases
    • Melby, J. O., Li, X. & Mitchell, D. A. Orchestration of enzymatic processing by thiazole/oxazole-modified microcin dehydrogenases. Biochemistry 53, 413-422 (2014).
    • (2014) Biochemistry , vol.53 , pp. 413-422
    • Melby, J.O.1    Li, X.2    Mitchell, D.A.3
  • 11
    • 0039130745 scopus 로고    scopus 로고
    • Cofactor requirements and reconstitution of microcin B17 synthetase: A multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17
    • Milne, J. C. et al. Cofactor requirements and reconstitution of microcin B17 synthetase: A multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17. Biochemistry 38, 4768-4781 (1999).
    • (1999) Biochemistry , vol.38 , pp. 4768-4781
    • Milne, J.C.1
  • 12
    • 84925460979 scopus 로고    scopus 로고
    • Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
    • Ortega, M. A. et al. Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB. Nature 517, 509-512 (2015).
    • (2015) Nature , vol.517 , pp. 509-512
    • Ortega, M.A.1
  • 13
    • 84956950124 scopus 로고    scopus 로고
    • Insights into the biosynthesis of dehydroalanines in goadsporin
    • Ozaki, T. et al. Insights into the biosynthesis of dehydroalanines in goadsporin. Chembiochem. 17, 218-223 (2016).
    • (2016) Chembiochem. , vol.17 , pp. 218-223
    • Ozaki, T.1
  • 15
    • 9744255506 scopus 로고    scopus 로고
    • Structure and functions of the GNAT superfamily of acetyltransferases
    • Vetting, M. W. et al. Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433, 212-226 (2005).
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 212-226
    • Vetting, M.W.1
  • 16
    • 84976870713 scopus 로고    scopus 로고
    • Leader peptide-free in vitro reconstitution of microviridin biosynthesis enables design of synthetic protease-targeted libraries
    • Reyna-González, E., Schmid, B., Petras, D., Süssmuth, R. D. & Dittmann, E. Leader peptide-free in vitro reconstitution of microviridin biosynthesis enables design of synthetic protease-targeted libraries. Angew. Chem. Int. Ed. Engl. 55, 9398-9401 (2016).
    • (2016) Angew. Chem. Int. Ed. Engl. , vol.55 , pp. 9398-9401
    • Reyna-González, E.1    Schmid, B.2    Petras, D.3    Süssmuth, R.D.4    Dittmann, E.5
  • 17
    • 84866973856 scopus 로고    scopus 로고
    • In vivo production of thiopeptide variants
    • Zhang, F. & Kelly, W. L. In vivo production of thiopeptide variants. Methods Enzymol. 516, 3-24 (2012).
    • (2012) Methods Enzymol. , vol.516 , pp. 3-24
    • Zhang, F.1    Kelly, W.L.2
  • 18
    • 84872523556 scopus 로고    scopus 로고
    • Biosynthesis of thiopeptide antibiotics and their pathway engineering
    • Zhang, Q. & Liu, W. Biosynthesis of thiopeptide antibiotics and their pathway engineering. Nat. Prod. Rep. 30, 218-226 (2013).
    • (2013) Nat. Prod. Rep. , vol.30 , pp. 218-226
    • Zhang, Q.1    Liu, W.2
  • 19
    • 84884652959 scopus 로고    scopus 로고
    • Engineering unnatural variants of plantazolicin through codon reprogramming
    • Deane, C. D., Melby, J. O., Molohon, K. J., Susarrey, A. R. & Mitchell, D. A. Engineering unnatural variants of plantazolicin through codon reprogramming. ACS Chem. Biol. 8, 1998-2008 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1998-2008
    • Deane, C.D.1    Melby, J.O.2    Molohon, K.J.3    Susarrey, A.R.4    Mitchell, D.A.5
  • 21
    • 84903151161 scopus 로고    scopus 로고
    • One-pot synthesis of azolinecontaining peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase
    • Goto, Y., Ito, Y., Kato, Y., Tsunoda, S. & Suga, H. One-pot synthesis of azolinecontaining peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase. Chem. Biol. 21, 766-774 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 766-774
    • Goto, Y.1    Ito, Y.2    Kato, Y.3    Tsunoda, S.4    Suga, H.5
  • 22
    • 79958158209 scopus 로고    scopus 로고
    • Flexizymes for genetic code reprogramming
    • Goto, Y., Katoh, T. & Suga, H. Flexizymes for genetic code reprogramming. Nat. Protoc. 6, 779-790 (2011).
    • (2011) Nat. Protoc. , vol.6 , pp. 779-790
    • Goto, Y.1    Katoh, T.2    Suga, H.3
  • 23
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • Shimizu, Y. et al. Cell-free translation reconstituted with purified components. Nat. Biotech. 19, 751-755 (2001).
    • (2001) Nat. Biotech. , vol.19 , pp. 751-755
    • Shimizu, Y.1
  • 24
    • 84873389412 scopus 로고    scopus 로고
    • Reevaluation of the D-amino acid compatibility with the elongation event in translation
    • Fujino, T., Goto, Y., Suga, H. & Murakami, H. Reevaluation of the D-amino acid compatibility with the elongation event in translation. J. Am. Chem. Soc. 135, 1830-1837 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1830-1837
    • Fujino, T.1    Goto, Y.2    Suga, H.3    Murakami, H.4
  • 25
    • 84901428333 scopus 로고    scopus 로고
    • Genome mining reveals a minimum gene set for the biosynthesis of 32-membered macrocyclic thiopeptides lactazoles
    • Hayashi, S. et al. Genome mining reveals a minimum gene set for the biosynthesis of 32-membered macrocyclic thiopeptides lactazoles. Chem. Biol. 21, 679-688 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 679-688
    • Hayashi, S.1
  • 26
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J. & van der Donk, W. A. Follow the leader: The use of leader peptides to guide natural product biosynthesis. Nat. Chem. Biol. 6, 9-18 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 27
    • 84934925970 scopus 로고    scopus 로고
    • Identification of an auxiliary leader peptide-binding protein required for azoline formation in ribosomal natural products
    • Dunbar, K. L., Tietz, J. I., Cox, C. L., Burkhart, B. J. & Mitchell, D. A. Identification of an auxiliary leader peptide-binding protein required for azoline formation in ribosomal natural products. J. Am. Chem. Soc. 137, 7672-7677 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 7672-7677
    • Dunbar, K.L.1    Tietz, J.I.2    Cox, C.L.3    Burkhart, B.J.4    Mitchell, D.A.5
  • 28
    • 84937395423 scopus 로고    scopus 로고
    • Structural analysis of leader peptide binding enables leaderfree cyanobactin processing
    • Koehnke, J. et al. Structural analysis of leader peptide binding enables leaderfree cyanobactin processing. Nat. Chem. Biol. 11, 558-563 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 558-563
    • Koehnke, J.1
  • 29
    • 84937438220 scopus 로고    scopus 로고
    • A prevalent peptide-binding domain guides ribosomal natural product biosynthesis
    • Burkhart, B. J., Hudson, G. A., Dunbar, K. L. & Mitchell, D. A. A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nat. Chem. Biol. 11, 564-570 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 564-570
    • Burkhart, B.J.1    Hudson, G.A.2    Dunbar, K.L.3    Mitchell, D.A.4
  • 30
    • 84983349011 scopus 로고    scopus 로고
    • In vitro biosynthesis and substrate tolerance of the plantazolicin family of natural products
    • Deane, C. D. et al. In vitro biosynthesis and substrate tolerance of the plantazolicin family of natural products. ACS Chem. Biol. 11, 2232-2243 (2016).
    • (2016) ACS Chem. Biol. , vol.11 , pp. 2232-2243
    • Deane, C.D.1
  • 31
    • 84926104192 scopus 로고    scopus 로고
    • Genetic approaches to generate hyper-producing strains of goadsporin: The relationships between productivity and gene duplication in secondary metabolite biosynthesis
    • Haginaka, K. et al. Genetic approaches to generate hyper-producing strains of goadsporin: The relationships between productivity and gene duplication in secondary metabolite biosynthesis. Biosci. Biotechnol. Biochem. 78, 394-399 (2014).
    • (2014) Biosci. Biotechnol. Biochem. , vol.78 , pp. 394-399
    • Haginaka, K.1
  • 32
    • 84937735393 scopus 로고    scopus 로고
    • Modularity of RiPP enzymes enables designed synthesis of decorated peptides
    • Sardar, D., Lin, Z. & Schmidt, E. W. Modularity of RiPP enzymes enables designed synthesis of decorated peptides. Chem. Biol. 22, 907-916 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 907-916
    • Sardar, D.1    Lin, Z.2    Schmidt, E.W.3
  • 34
    • 84965002440 scopus 로고    scopus 로고
    • Structure and tRNA specificity of MibB, a lantibiotic dehydratase from Actinobacteria involved in NAI-107 biosynthesis
    • Ortega, M. A. et al. Structure and tRNA specificity of MibB, a lantibiotic dehydratase from Actinobacteria involved in NAI-107 biosynthesis. Cell Chem. Biol. 23, 370-380 (2016).
    • (2016) Cell Chem. Biol. , vol.23 , pp. 370-380
    • Ortega, M.A.1
  • 35
    • 84939811853 scopus 로고    scopus 로고
    • Use of a biosynthetic intermediate to explore the chemical diversity of pseudo-natural fungal polyketides
    • Asai, T. et al. Use of a biosynthetic intermediate to explore the chemical diversity of pseudo-natural fungal polyketides. Nat. Chem. 7, 737-743 2015
    • (2015) Nat. Chem. , vol.7 , pp. 737-743
    • Asai, T.1
  • 36
    • 84975456513 scopus 로고    scopus 로고
    • Ribosome-mediated synthesis of natural product-like peptides via cell-free translation
    • Maini, R., Umemoto, S. & Suga, H. Ribosome-mediated synthesis of natural product-like peptides via cell-free translation. Curr. Opin. Chem. Biol. 34, 44-52 (2016).
    • (2016) Curr. Opin. Chem. Biol. , vol.34 , pp. 44-52
    • Maini, R.1    Umemoto, S.2    Suga, H.3
  • 37
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein. Expr. Purif. 41, 207-234 (2005).
    • (2005) Protein. Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1


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