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Volumn 17, Issue 2, 2010, Pages 149-159

Isolation and Purification of a New Kalimantacin/Batumin-Related Polyketide Antibiotic and Elucidation of Its Biosynthesis Gene Cluster

Author keywords

CHEMBIO

Indexed keywords

ANTIINFECTIVE AGENT; BATUMIN; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; NON RIBOSOMAL PEPTIDE SYNTHASE; NON-RIBOSOMAL PEPTIDE SYNTHASE; ORGANIC COMPOUND; PEPTIDE SYNTHASE; POLYKETIDE SYNTHASE;

EID: 77049112083     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.01.014     Document Type: Article
Times cited : (71)

References (47)
  • 1
    • 0029872079 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster of rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase
    • Aparicio J.F., Molanar I., Schwecke T., Koning A., Haydock S.F., Khaw L.E., Staunton J., and Leadlay P.F. Organization of the biosynthetic gene cluster of rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase. Gene 169 (1996) 9-16
    • (1996) Gene , vol.169 , pp. 9-16
    • Aparicio, J.F.1    Molanar, I.2    Schwecke, T.3    Koning, A.4    Haydock, S.F.5    Khaw, L.E.6    Staunton, J.7    Leadlay, P.F.8
  • 2
    • 0013902668 scopus 로고
    • Antibiotic susceptibility testing by a standardized single disk method
    • Bauer A.W., Kirby W.M., Sherris J.C., and Turck M. Antibiotic susceptibility testing by a standardized single disk method. Am. J. Clin. Pathol. 45 (1966) 493-496
    • (1966) Am. J. Clin. Pathol. , vol.45 , pp. 493-496
    • Bauer, A.W.1    Kirby, W.M.2    Sherris, J.C.3    Turck, M.4
  • 4
    • 51349147485 scopus 로고    scopus 로고
    • Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis
    • Bumpus S.B., Magarvey N.A., Kelleher N.L., Walsh C.T., and Calderone C.T. Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis. J. Am. Chem. Soc. 130 (2008) 11614-11616
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11614-11616
    • Bumpus, S.B.1    Magarvey, N.A.2    Kelleher, N.L.3    Walsh, C.T.4    Calderone, C.T.5
  • 5
    • 26944433084 scopus 로고    scopus 로고
    • The stereochemistry of ketoreduction
    • Caffrey P. The stereochemistry of ketoreduction. Chem. Biol. 12 (2005) 1060-1062
    • (2005) Chem. Biol. , vol.12 , pp. 1060-1062
    • Caffrey, P.1
  • 6
    • 33745181160 scopus 로고    scopus 로고
    • Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis
    • Calderone C.T., Kowtoniuk W.E., Kelleher N.L., Walsh C.T., and Dorrestein P.C. Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 103 (2006) 8977-8982
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8977-8982
    • Calderone, C.T.1    Kowtoniuk, W.E.2    Kelleher, N.L.3    Walsh, C.T.4    Dorrestein, P.C.5
  • 7
    • 4344645019 scopus 로고    scopus 로고
    • Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula
    • Chang Z., Sitachitta N., Rossi J.V., Roberts M.A., Flatt P.M., Jia J., Sherman D.H., and Gerwick W.H. Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula. J. Nat. Prod. 67 (2004) 1356-1367
    • (2004) J. Nat. Prod. , vol.67 , pp. 1356-1367
    • Chang, Z.1    Sitachitta, N.2    Rossi, J.V.3    Roberts, M.A.4    Flatt, P.M.5    Jia, J.6    Sherman, D.H.7    Gerwick, W.H.8
  • 9
    • 0029126219 scopus 로고
    • Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3′-hydroxymethylcephem O-carbamoyltransferase for cephamycin biosynthesis
    • Coque J.J., Pérez-Llarena F.J., Enguita F.J., Fuente J.L., Martín J.F., and Liras P. Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3′-hydroxymethylcephem O-carbamoyltransferase for cephamycin biosynthesis. Gene 162 (1995) 21-27
    • (1995) Gene , vol.162 , pp. 21-27
    • Coque, J.J.1    Pérez-Llarena, F.J.2    Enguita, F.J.3    Fuente, J.L.4    Martín, J.F.5    Liras, P.6
  • 10
    • 0024459873 scopus 로고
    • How antibiotic-producing organisms avoid suicide
    • Cundliffe E. How antibiotic-producing organisms avoid suicide. Annu. Rev. Microbiol. 43 (1989) 207-233
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 207-233
    • Cundliffe, E.1
  • 13
    • 0026559262 scopus 로고
    • Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythraea
    • Donadio S., and Katz L. Organization of the enzymatic domains in the multifunctional polyketide synthase involved in erythromycin formation in Saccharopolyspora erythraea. Gene 111 (1992) 51-60
    • (1992) Gene , vol.111 , pp. 51-60
    • Donadio, S.1    Katz, L.2
  • 14
    • 3042551455 scopus 로고    scopus 로고
    • Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula
    • Edwards D.J., Marquez B.L., Nogle L.M., McPhail K., Goeger D.E., Roberts M.A., and Gerwick W.H. Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula. Chem. Biol. 11 (2004) 817-833
    • (2004) Chem. Biol. , vol.11 , pp. 817-833
    • Edwards, D.J.1    Marquez, B.L.2    Nogle, L.M.3    McPhail, K.4    Goeger, D.E.5    Roberts, M.A.6    Gerwick, W.H.7
  • 15
    • 0034875096 scopus 로고    scopus 로고
    • Quorum-sensing-dependent regulation of biosynthesis of the polyketide antibiotic mupirocin in Pseudomonas fluorescens NCIMB 10586
    • El-Sayed A.K., Hothersall J., and Thomas C.M. Quorum-sensing-dependent regulation of biosynthesis of the polyketide antibiotic mupirocin in Pseudomonas fluorescens NCIMB 10586. Microbiology 147 (2001) 2127-2139
    • (2001) Microbiology , vol.147 , pp. 2127-2139
    • El-Sayed, A.K.1    Hothersall, J.2    Thomas, C.M.3
  • 16
    • 0038183856 scopus 로고    scopus 로고
    • Characterization of the mupirocin biosynthesis gene cluster from Pseudomonas fluorescens NCIMB 10586
    • El-Sayed A.K., Hothersall J., Cooper S.M., Stephens E., Simpson T.J., and Thomas C.M. Characterization of the mupirocin biosynthesis gene cluster from Pseudomonas fluorescens NCIMB 10586. Chem. Biol. 10 (2003) 419-430
    • (2003) Chem. Biol. , vol.10 , pp. 419-430
    • El-Sayed, A.K.1    Hothersall, J.2    Cooper, S.M.3    Stephens, E.4    Simpson, T.J.5    Thomas, C.M.6
  • 17
    • 57449121088 scopus 로고    scopus 로고
    • In vivo manipulation of the bleomycin biosynthetic gene cluster in Streptomyces verticillus ATCC15003 revealing new insights into its biosynthetic pathway
    • Galm U., Wang L., Wendt-Pienkowski E., Yang R., Liu W., Tao M., Coughlin J.M., and Shen B. In vivo manipulation of the bleomycin biosynthetic gene cluster in Streptomyces verticillus ATCC15003 revealing new insights into its biosynthetic pathway. J. Biol. Chem. 283 (2008) 28236-28245
    • (2008) J. Biol. Chem. , vol.283 , pp. 28236-28245
    • Galm, U.1    Wang, L.2    Wendt-Pienkowski, E.3    Yang, R.4    Liu, W.5    Tao, M.6    Coughlin, J.M.7    Shen, B.8
  • 18
    • 33746032962 scopus 로고    scopus 로고
    • Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: functional identification of a mechanistically diverse enzyme pair
    • Gu L., Jia J., Liu H., Håkansson K., Gerwick W.H., and Sherman D.H. Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: functional identification of a mechanistically diverse enzyme pair. J. Am. Chem. Soc. 128 (2006) 9014-9015
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9014-9015
    • Gu, L.1    Jia, J.2    Liu, H.3    Håkansson, K.4    Gerwick, W.H.5    Sherman, D.H.6
  • 19
    • 19344377446 scopus 로고    scopus 로고
    • Cracking the polyketide code
    • Hopwood D.A. Cracking the polyketide code. PLoS Biol. 2 (2004) e35
    • (2004) PLoS Biol. , vol.2
    • Hopwood, D.A.1
  • 20
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan R.M., and Clarke S. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch. Biochem. Biophys. 310 (1994) 417-427
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 21
    • 0029962312 scopus 로고    scopus 로고
    • Kalimantacins A, B and C, novel antibiotics from Alcaligenes sp. YL-02632S. I. Taxonomy, fermentation, isolation and biological properties
    • Kamigiri K., Suzuki Y., Shibazaki M., Morioka M., Suzuki K., Tokunaga T., Setiawan B., and Rantiatmodjo R.M. Kalimantacins A, B and C, novel antibiotics from Alcaligenes sp. YL-02632S. I. Taxonomy, fermentation, isolation and biological properties. J. Antibiot. (Tokyo) 49 (1996) 136-139
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 136-139
    • Kamigiri, K.1    Suzuki, Y.2    Shibazaki, M.3    Morioka, M.4    Suzuki, K.5    Tokunaga, T.6    Setiawan, B.7    Rantiatmodjo, R.M.8
  • 23
    • 0033080078 scopus 로고    scopus 로고
    • How do peptide synthetases generate structural diversity?
    • Konz D., and Marahiel M.A. How do peptide synthetases generate structural diversity?. Chem. Biol. 6 (1999) R39-R48
    • (1999) Chem. Biol. , vol.6
    • Konz, D.1    Marahiel, M.A.2
  • 24
    • 34147098650 scopus 로고    scopus 로고
    • The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together
    • Lomakin I.B., Xiong Y., and Steitz T.A. The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell 129 (2007) 319-332
    • (2007) Cell , vol.129 , pp. 319-332
    • Lomakin, I.B.1    Xiong, Y.2    Steitz, T.A.3
  • 25
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • Marahiel M.A. Protein templates for the biosynthesis of peptide antibiotics. Chem. Biol. 4 (1997) 561-567
    • (1997) Chem. Biol. , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 26
    • 7744220004 scopus 로고    scopus 로고
    • Don't classify polyketide synthases
    • Muller R. Don't classify polyketide synthases. Chem. Biol. 11 (2004) 4-6
    • (2004) Chem. Biol. , vol.11 , pp. 4-6
    • Muller, R.1
  • 27
    • 7244245763 scopus 로고    scopus 로고
    • Antibiotics at the crossroads
    • Nathan C. Antibiotics at the crossroads. Nature 431 (2004) 899-902
    • (2004) Nature , vol.431 , pp. 899-902
    • Nathan, C.1
  • 31
    • 0037195174 scopus 로고    scopus 로고
    • A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles
    • Piel J. A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles. Proc. Natl. Acad. Sci. USA 99 (2002) 14002-14007
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14002-14007
    • Piel, J.1
  • 33
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • Rausch C., Weber T., Kohlbacher O., Wohlleben W., and Huson D.H. Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). Nucleic Acids Res. 33 (2005) 5799-5808
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3    Wohlleben, W.4    Huson, D.H.5
  • 35
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria
    • Simon R., Priefer U., and Pühler A. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Nat. Biotechnol. 1 (1983) 784-791
    • (1983) Nat. Biotechnol. , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 37
    • 0034048695 scopus 로고    scopus 로고
    • Identification of the novobiocin biosynthetic gene cluster of Streptomyces spheroides NCIB 11891
    • Steffensky M., Mühlenweg A., Wang Z.X., Li S.M., and Heide L. Identification of the novobiocin biosynthetic gene cluster of Streptomyces spheroides NCIB 11891. Antimicrob. Agents Chemother. 44 (2000) 1214-1222
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1214-1222
    • Steffensky, M.1    Mühlenweg, A.2    Wang, Z.X.3    Li, S.M.4    Heide, L.5
  • 38
    • 53149124737 scopus 로고    scopus 로고
    • Ligand recognition by ActR, a TetR-like regulator of actinorhodin export
    • Tahlan K., Yu Z., Xu Y., Davidson A.R., and Nodwell J.R. Ligand recognition by ActR, a TetR-like regulator of actinorhodin export. J. Mol. Biol. 383 (2008) 753-761
    • (2008) J. Mol. Biol. , vol.383 , pp. 753-761
    • Tahlan, K.1    Yu, Z.2    Xu, Y.3    Davidson, A.R.4    Nodwell, J.R.5
  • 39
    • 0029983925 scopus 로고    scopus 로고
    • Kalimantacin A, B, and C, novel antibiotics produced by Alcaligenes sp. YL-02632S. II. Physico-chemical properties and structure elucidation
    • Tokunaga T., Kamigiri K., Orita M., Nishikawa T., Shimizu M., and Kaniwa H. Kalimantacin A, B, and C, novel antibiotics produced by Alcaligenes sp. YL-02632S. II. Physico-chemical properties and structure elucidation. J. Antibiot. (Tokyo) 49 (1996) 140-144
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 140-144
    • Tokunaga, T.1    Kamigiri, K.2    Orita, M.3    Nishikawa, T.4    Shimizu, M.5    Kaniwa, H.6
  • 41
  • 44
    • 2642518095 scopus 로고    scopus 로고
    • New aminocoumarin antibiotics formed by a combined mutational and chemoenzymatic approach utilizing the carbamoyltransferase NovN
    • Xu H., Heide L., and Li S.M. New aminocoumarin antibiotics formed by a combined mutational and chemoenzymatic approach utilizing the carbamoyltransferase NovN. Chem. Biol. 11 (2004) 655-662
    • (2004) Chem. Biol. , vol.11 , pp. 655-662
    • Xu, H.1    Heide, L.2    Li, S.M.3
  • 45
    • 0037466331 scopus 로고    scopus 로고
    • Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases
    • Yadav G., Gokhale R.S., and Mohanty D. Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases. J. Mol. Biol. 328 (2003) 335-363
    • (2003) J. Mol. Biol. , vol.328 , pp. 335-363
    • Yadav, G.1    Gokhale, R.S.2    Mohanty, D.3
  • 46
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., and Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 (1985) 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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