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Volumn 12, Issue , 2012, Pages

Identification and functional analysis of gene cluster involvement in biosynthesis of the cyclic lipopeptide antibiotic pelgipeptin produced by Paenibacillus elgii

Author keywords

Antimicrobial agent; Biosynthesis; Gene cluster; Non ribosomal peptide

Indexed keywords

AMINO ACID; LIPOPEPTIDE; PELGIPEPTIN; PELGIPEPTIN SYNTHETASE D; PELGIPEPTIN SYNTHETASE E; PELGIPEPTIN SYNTHETASE F; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84865829707     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-12-197     Document Type: Article
Times cited : (28)

References (28)
  • 1
    • 77955261432 scopus 로고    scopus 로고
    • Isolation and partial characterization of antibiotics produced by Paenibacillus elgii B69
    • 10.1111/j.1574-6968.2010.02040.x 20618851
    • Isolation and partial characterization of antibiotics produced by Paenibacillus elgii B69. Wu XC, Shen XB, Ding R, Qian CD, Fang HH, Li O, FEMS Microbiol Lett 2010 310 1 32 38 10.1111/j.1574-6968.2010.02040.x 20618851
    • (2010) FEMS Microbiol Lett , vol.310 , Issue.1 , pp. 32-38
    • Wu, X.C.1    Shen, X.B.2    Ding, R.3    Qian, C.D.4    Fang, H.H.5    Li, O.6
  • 2
    • 71549142267 scopus 로고    scopus 로고
    • Bacillus amyloliquefaciens GA 1 as a source of potent antibiotics and other secondary metabolites for biocontrol of plant pathogens
    • 19126236
    • Bacillus amyloliquefaciens GA 1 as a source of potent antibiotics and other secondary metabolites for biocontrol of plant pathogens. Arguelles-Arias A, Ongena M, Halimi B, Lara Y, Brans A, Joris B, Fickers P, Microb Cell Fact 2009 8 63 1 12 19126236
    • (2009) Microb Cell Fact , vol.8 , Issue.63 , pp. 1-12
    • Arguelles-Arias, A.1    Ongena, M.2    Halimi, B.3    Lara, Y.4    Brans, A.5    Joris, B.6    Fickers, P.7
  • 3
    • 84555177736 scopus 로고    scopus 로고
    • Isolation and identification of lipopeptide antibiotics from Paenibacillus elgii B69 with inhibitory activity against methicillin-resistant Staphylococcus aureus
    • 10.1007/s12275-011-1153-7 22203557
    • Isolation and identification of lipopeptide antibiotics from Paenibacillus elgii B69 with inhibitory activity against methicillin-resistant Staphylococcus aureus. Ding R, Wu XC, Qian CD, Teng Y, Li O, Zhan ZJ, Zhao YH, J Microbiol 2011 49 6 942 949 10.1007/s12275-011-1153-7 22203557
    • (2011) J Microbiol , vol.49 , Issue.6 , pp. 942-949
    • Ding, R.1    Wu, X.C.2    Qian, C.D.3    Teng, Y.4    Li, O.5    Zhan, Z.J.6    Zhao, Y.H.7
  • 4
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • DOI 10.1146/annurev.micro.58.030603.123615
    • Biosynthesis of nonribosomal peptides. Finking R, Marahiel MA, Annu Rev Microbiol 2004 58 453 488 10.1146/annurev.micro.58.030603.123615 15487945 (Pubitemid 39551994)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 5
    • 0037524493 scopus 로고    scopus 로고
    • Nonribosomal peptides: From genes to products
    • DOI 10.1039/b111145k
    • Nonribosomal peptides: from genes to products. Schwarzer D, Finking R, Marahiel MA, Nat Prod Rep 2003 20 3 275 287 10.1039/b111145k 12828367 (Pubitemid 36770356)
    • (2003) Natural Product Reports , vol.20 , Issue.3 , pp. 275-287
    • Schwarzer, D.1    Finking, R.2    Marahiel, M.A.3
  • 7
    • 64249084052 scopus 로고    scopus 로고
    • Methods for in silico prediction of microbial secondary metabolic pathways from dna sequence data
    • 19374984
    • Methods for In Silico Prediction of Microbial Secondary Metabolic Pathways from DNA Sequence Data. Bachmann BO, Ravel J, Methods Enzymol 2009 458 181 217 19374984
    • (2009) Methods Enzymol , vol.458 , pp. 181-217
    • Bachmann, B.O.1    Ravel, J.2
  • 8
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • DOI 10.1093/nar/gki885
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). Rausch C, Weber T, Kohlbacher O, Wohlleben W, Huson DH, Nucleic Acids Res 2005 33 18 5799 10.1093/nar/gki885 16221976 (Pubitemid 41742599)
    • (2005) Nucleic Acids Research , vol.33 , Issue.18 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3    Wohlleben, W.4    Huson, D.H.5
  • 9
    • 80053647666 scopus 로고    scopus 로고
    • Identification and analysis of the gene cluster involved in biosynthesis of paenibactin, a catecholate siderophore produced by Paenibacillus elgii B69
    • 10.1111/j.1462-2920.2011.02542.x 21883794
    • Identification and analysis of the gene cluster involved in biosynthesis of paenibactin, a catecholate siderophore produced by Paenibacillus elgii B69. Wen Y, Wu X, Teng Y, Qian C, Zhan Z, Zhao Y, Li O, Environ Microbiol 2011 13 10 2726 2737 10.1111/j.1462-2920.2011.02542.x 21883794
    • (2011) Environ Microbiol , vol.13 , Issue.10 , pp. 2726-2737
    • Wen, Y.1    Wu, X.2    Teng, Y.3    Qian, C.4    Zhan, Z.5    Zhao, Y.6    Li, O.7
  • 10
    • 59749101384 scopus 로고    scopus 로고
    • A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis
    • 10.1016/j.ab.2008.12.014 19135023
    • A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis. McQuade TJ, Shallop AD, Sheoran A, Delproposto JE, Tsodikov OV, Garneau-Tsodikova S, Anal Biochem 2009 386 2 244 250 10.1016/j.ab.2008.12.014 19135023
    • (2009) Anal Biochem , vol.386 , Issue.2 , pp. 244-250
    • McQuade, T.J.1    Shallop, A.D.2    Sheoran, A.3    Delproposto, J.E.4    Tsodikov, O.V.5    Garneau-Tsodikova, S.6
  • 11
    • 80052308568 scopus 로고    scopus 로고
    • Draft Genome Sequence of Paenibacillus elgii B69, a Strain with Broad Antimicrobial Activity
    • 10.1128/JB.00406-11 21705583
    • Draft Genome Sequence of Paenibacillus elgii B69, a Strain with Broad Antimicrobial Activity. Ding R, Li Y, Qian C, Wu X, J Bacteriol 2011 193 17 4537 10.1128/JB.00406-11 21705583
    • (2011) J Bacteriol , vol.193 , Issue.17 , pp. 4537
    • Ding, R.1    Li, Y.2    Qian, C.3    Wu, X.4
  • 12
    • 65549086085 scopus 로고    scopus 로고
    • Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis
    • 10.1128/JB.01728-08 19304848
    • Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis. Choi SK, Park SY, Kim R, Kim SB, Lee CH, Kim JF, Park SH, J Bacteriol 2009 191 10 3350 3358 10.1128/JB.01728-08 19304848
    • (2009) J Bacteriol , vol.191 , Issue.10 , pp. 3350-3358
    • Choi, S.K.1    Park, S.Y.2    Kim, R.3    Kim, S.B.4    Lee, C.H.5    Kim, J.F.6    Park, S.H.7
  • 13
    • 34250710858 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
    • DOI 10.1186/1471-2148-7-78
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution. Rausch C, Hoof I, Weber T, Wohlleben W, Huson D, BMC Evol Biol 2007 7 1 78 10.1186/1471-2148-7-78 17506888 (Pubitemid 46964322)
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 78
    • Rausch, C.1    Hoof, I.2    Weber, T.3    Wohlleben, W.4    Huson, D.H.5
  • 14
    • 1542350231 scopus 로고    scopus 로고
    • The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains
    • DOI 10.1074/jbc.M309658200
    • The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains. Kessler N, Schuhmann H, Morneweg S, Linne U, Marahiel MA, Journal Biol Chem 2004 279 9 7413 7419 (Pubitemid 38294617)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7413-7419
    • Kessler, N.1    Schuhmann, H.2    Morneweg, S.3    Linne, U.4    Marahiel, M.A.5
  • 15
    • 38549164599 scopus 로고    scopus 로고
    • Growth phase-dependent switch in osmolyte strategy in a moderate halophile: Ectoine is a minor osmolyte but major stationary phase solute in Halobacillus halophilus
    • DOI 10.1111/j.1462-2920.2007.01494.x
    • Growth phase-dependent switch in osmolyte strategy in a moderate halophile: ectoine is a minor osmolyte but major stationary phase solute in Halobacillus halophilus. Saum SH, Muller V, Environ Microbiol 2008 10 3 716 726 10.1111/j.1462-2920.2007.01494.x 18093162 (Pubitemid 351160912)
    • (2008) Environmental Microbiology , vol.10 , Issue.3 , pp. 716-726
    • Saum, S.H.1    Muller, V.2
  • 16
    • 4344588817 scopus 로고    scopus 로고
    • Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1
    • DOI 10.1128/JB.186.17.5596-5602.2004
    • Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1. Vandenende CS, Vlasschaert M, Seah SYK, J Bacteriol 2004 186 17 5596 5602 10.1128/JB.186.17.5596-5602.2004 15317763 (Pubitemid 39128631)
    • (2004) Journal of Bacteriology , vol.186 , Issue.17 , pp. 5596-5602
    • Vandenende, C.S.1    Vlasschaert, M.2    Seah, S.Y.K.3
  • 17
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • 10.1128/MMBR.64.3.515-547.2000
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Tjalsma H, Bolhuis A, Jongbloed JDH, Bron S, Van Dijl JM, Microbiol Mol Biol R 2000 64 3 515 10.1128/MMBR.64.3.515-547. 2000
    • (2000) Microbiol Mol Biol R , vol.64 , Issue.3 , pp. 515
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    Van Dijl, J.M.5
  • 18
    • 0027359783 scopus 로고
    • Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa
    • DOI 10.1016/0014-5793(93)80501-K
    • Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa. Jaeger KE, Ransac S, Koch HB, Ferrato F, Dijkstra BW, FEBS Lett 1993 332 1-2 143 149 8405431 (Pubitemid 23295916)
    • (1993) FEBS Letters , vol.332 , Issue.1-2 , pp. 143-149
    • Jaeger, K.-E.1    Ransac, S.2    Koch, H.B.3    Ferrato, F.4    Dijkstra, B.W.5
  • 19
    • 0033762099 scopus 로고    scopus 로고
    • A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase
    • 10.1046/j.1432-1327.2000.01736.x 11029590
    • A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase. Eggert T, Pencreach G, Douchet I, Verger R, Jaeger KE, Eur J Biochem 2000 267 21 6459 6469 10.1046/j.1432-1327.2000.01736.x 11029590
    • (2000) Eur J Biochem , vol.267 , Issue.21 , pp. 6459-6469
    • Eggert, T.1    Pencreach, G.2    Douchet, I.3    Verger, R.4    Jaeger, K.E.5
  • 20
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • 10493927
    • Bacterial lipolytic enzymes: classification and properties. Arpigny JL, Jaeger KE, Biochem J 1999 343 Pt 1 177 10493927
    • (1999) Biochem J , vol.343 , Issue.PART 1 , pp. 177
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 21
    • 33846195912 scopus 로고    scopus 로고
    • Production of tripropeptins in media supplemented with precursors based on the biosynthetic pathway
    • Production of tripropeptins in media supplemented with precursors based on the biosynthetic pathway. Hashizume H, Nosaka C, Hirosawa S, Igarashi M, Nishimura Y, Akamatsu Y, ARKIVOC 2007 7 241 253
    • (2007) ARKIVOC , vol.7 , pp. 241-253
    • Hashizume, H.1    Nosaka, C.2    Hirosawa, S.3    Igarashi, M.4    Nishimura, Y.5    Akamatsu, Y.6
  • 22
    • 0037926641 scopus 로고    scopus 로고
    • Control of liposidomycin production through precursor-directed biosynthesis
    • Control of liposidomycin production through precursor-directed biosynthesis. Kagami S, Esumi Y, Nakakoshi M, Yoshihama M, Kimura KI, J Antibiot 2003 56 6 552 556 10.7164/antibiotics.56.552 12931865 (Pubitemid 36849943)
    • (2003) Journal of Antibiotics , vol.56 , Issue.6 , pp. 552-556
    • Kagami, S.1    Esumi, Y.2    Nakakoshi, M.3    Yoshihama, M.4    Kimura, K.-I.5
  • 23
    • 33646092296 scopus 로고    scopus 로고
    • The phosphopantetheinyl transferase superfamily: Phylogenetic analysis and functional implications in cyanobacteria
    • 10.1128/AEM.72.4.2298-2305.2006 16597923
    • The phosphopantetheinyl transferase superfamily: phylogenetic analysis and functional implications in cyanobacteria. Copp JN, Neilan BA, Appl Environ Microbiol 2006 72 4 2298 2305 10.1128/AEM.72.4.2298-2305.2006 16597923
    • (2006) Appl Environ Microbiol , vol.72 , Issue.4 , pp. 2298-2305
    • Copp, J.N.1    Neilan, B.A.2
  • 24
    • 0027289507 scopus 로고
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis. Cosmina P, Rodriguez F, de Ferra F, Grandi G, Perego M, Venema G, van Sinderen D, Mol Microbiol 1993 8 5 821 831 10.1111/j.1365-2958.1993.tb01629.x 8355609 (Pubitemid 23171464)
    • (1993) Molecular Microbiology , vol.8 , Issue.5 , pp. 821-831
    • Cosmina, P.1    Rodriguez, F.2    De Ferra, F.3    Grandi, G.4    Perego, M.5    Venema, G.6    Van Sinderen, D.7
  • 26
    • 0030663849 scopus 로고    scopus 로고
    • Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168
    • Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168. Tosato V, Albertini AM, Zotti M, Sonda S, Bruschi CV, Microbiology 1997 143 Pt 11 3443 3450 9387222 (Pubitemid 27496923)
    • (1997) Microbiology , vol.143 , Issue.11 , pp. 3443-3450
    • Tosato, V.1    Albertini, A.M.2    Zotti, M.3    Sonda, S.4    Bruschi, C.V.5
  • 27
    • 39149132471 scopus 로고    scopus 로고
    • Nonribosomal Biosynthesis of Fusaricidins by Paenibacillus polymyxa PKB1 Involves Direct Activation of a d-Amino Acid
    • DOI 10.1016/j.chembiol.2007.12.014, PII S1074552107004462
    • Nonribosomal biosynthesis of fusaricidins by Paenibacillus polymyxa PKB1 involves direct activation of a D-amino acid. Li J, Jensen SE, Chem Biol 2008 15 2 118 127 10.1016/j.chembiol.2007.12.014 18291316 (Pubitemid 351253613)
    • (2008) Chemistry and Biology , vol.15 , Issue.2 , pp. 118-127
    • Li, J.1    Jensen, S.E.2
  • 28
    • 4444252771 scopus 로고    scopus 로고
    • Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein
    • DOI 10.1021/bi0493416
    • Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein. Steller S, Sokoll A, Wilde C, Bernhard F, Franke P, Vater J, Biochemistry 2004 43 35 11331 11343 10.1021/bi0493416 15366943 (Pubitemid 39180377)
    • (2004) Biochemistry , vol.43 , Issue.35 , pp. 11331-11343
    • Steller, S.1    Sokoll, A.2    Wilde, C.3    Bernhard, F.4    Franke, P.5    Vater, J.6


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