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Volumn 92, Issue 3, 2011, Pages 571-581

Bioinformatics and molecular approaches to detect NRPS genes involved in the biosynthesis of kurstakin from Bacillus thuringiensis

Author keywords

Bacillus thuringiensis; Kurstakins; MALDI ToF; Nonribosomal lipopeptides; PCR; Spreading

Indexed keywords

BACILLUS THURINGIENSIS; KURSTAKINS; LIPOPEPTIDES; MALDI-TOF; PCR; SPREADING;

EID: 82355169760     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3453-6     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 3442896886 scopus 로고    scopus 로고
    • NRPS-PKS: A knowledge-based resource for analysis of NRPS/PKS megasynthases
    • 10.1093/nar/gkh359
    • MZ Ansari G Yadav RS Gokhale D Mohanty 2004 NRPS-PKS: a knowledge-based resource for analysis of NRPS/PKS megasynthases Nucleic Acids Res 32 405 413 10.1093/nar/gkh359
    • (2004) Nucleic Acids Res , vol.32 , pp. 405-413
    • Ansari, M.Z.1    Yadav, G.2    Gokhale, R.S.3    Mohanty, D.4
  • 2
    • 64249084052 scopus 로고    scopus 로고
    • Methods for in silico prediction of microbial polyketide and nonribosomal peptide biosynthetic pathways from DNA sequence data
    • 10.1016/S0076-6879(09)04808-3 1:CAS:528:DC%2BD1MXpsFejs7c%3D
    • BO Bachmann J Ravel 2009 Methods for in silico prediction of microbial polyketide and nonribosomal peptide biosynthetic pathways from DNA sequence data Methods Enzymol 458 181 217 10.1016/S0076-6879(09)04808-3 1:CAS:528: DC%2BD1MXpsFejs7c%3D
    • (2009) Methods Enzymol , vol.458 , pp. 181-217
    • Bachmann, B.O.1    Ravel, J.2
  • 3
    • 70349959824 scopus 로고    scopus 로고
    • A proteomics approach to discovering natural products and their biosynthetic pathways
    • 10.1038/nbt.1565 1:CAS:528:DC%2BD1MXhtFGjt73J
    • SB Bumpus BS Evans PM Thomas I Ntai NL Kelleher 2009 A proteomics approach to discovering natural products and their biosynthetic pathways Nat Biotechnol 27 951 956 10.1038/nbt.1565 1:CAS:528:DC%2BD1MXhtFGjt73J
    • (2009) Nat Biotechnol , vol.27 , pp. 951-956
    • Bumpus, S.B.1    Evans, B.S.2    Thomas, P.M.3    Ntai, I.4    Kelleher, N.L.5
  • 6
    • 0031006666 scopus 로고    scopus 로고
    • Recherche de souches de Bacillus thuringiensis dans différents biotopes à travers le monde
    • 10.1139/m97-047
    • J Chauffaux M Marchal N Gilois I Jehanno C Buisson 1997 Recherche de souches de Bacillus thuringiensis dans différents biotopes à travers le monde Can J Microbiol 43 337 343 10.1139/m97-047
    • (1997) Can J Microbiol , vol.43 , pp. 337-343
    • Chauffaux, J.1    Marchal, M.2    Gilois, N.3    Jehanno, I.4    Buisson, C.5
  • 7
    • 61649125590 scopus 로고    scopus 로고
    • Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens
    • 10.1016/j.jbiotec.2008.10.011 1:CAS:528:DC%2BD1MXjtFOjtLg%3D
    • XH Chen A Koumoutsi R Scholz K Schneider J Vate R Süssmuth J Piel R Borriss 2009 Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens J Biotechnol 140 27 37 10.1016/j.jbiotec.2008.10.011 1:CAS:528:DC%2BD1MXjtFOjtLg%3D
    • (2009) J Biotechnol , vol.140 , pp. 27-37
    • Chen, X.H.1    Koumoutsi, A.2    Scholz, R.3    Schneider, K.4    Vate, J.5    Süssmuth, R.6    Piel, J.7    Borriss, R.8
  • 8
    • 0035313205 scopus 로고    scopus 로고
    • How Bacillus thuringiensis has evolved specific toxins to colonize the insect world
    • 10.1016/S0168-9525(01)02237-5
    • RA De Maagd A Bravo N Crickmore 2001 How Bacillus thuringiensis has evolved specific toxins to colonize the insect world Trends Genet 17 193 199 10.1016/S0168-9525(01)02237-5
    • (2001) Trends Genet , vol.17 , pp. 193-199
    • De Maagd, R.A.1    Bravo, A.2    Crickmore, N.3
  • 9
    • 0033709514 scopus 로고    scopus 로고
    • Kurstakins: A new class of lipopeptides isolated from Bacillus thuringiensis
    • 10.1021/np000169q 1:CAS:528:DC%2BD3cXmsVCqsb4%3D
    • Y Hathout YP Ho V Ryzhov P Demirev C Fenselau 2000 Kurstakins: a new class of lipopeptides isolated from Bacillus thuringiensis J Nat Prod 63 1492 1496 10.1021/np000169q 1:CAS:528:DC%2BD3cXmsVCqsb4%3D
    • (2000) J Nat Prod , vol.63 , pp. 1492-1496
    • Hathout, Y.1    Ho, Y.P.2    Ryzhov, V.3    Demirev, P.4    Fenselau, C.5
  • 10
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • 1:CAS:528:DyaL1MXltFajt78%3D
    • H Hofte HR Whiteley 1989 Insecticidal crystal proteins of Bacillus thuringiensis Microbiol Rev 53 242 255 1:CAS:528:DyaL1MXltFajt78%3D
    • (1989) Microbiol Rev , vol.53 , pp. 242-255
    • Hofte, H.1    Whiteley, H.R.2
  • 11
    • 0025246102 scopus 로고
    • 2 with a Mu d(lac) element for ecological studies
    • 1:CAS:528:DyaK3cXkt1SktLc%3D
    • 2 with a Mu d(lac) element for ecological studies Appl Environ Microbiol 56 1046 1052 1:CAS:528:DyaK3cXkt1SktLc%3D
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1046-1052
    • Hofte, M.1    Mergeay, M.2    Verstraete, W.3
  • 12
    • 6344275158 scopus 로고    scopus 로고
    • Purification and characterization of a lipopeptide produced by Bacillus thuringiensis CMB26
    • 10.1111/j.1365-2672.2004.02356.x 1:CAS:528:DC%2BD2cXhtVahtLzI
    • PI Kim H Bai D Bai H Chae S Chung Y Kim R Park YT Chi 2004 Purification and characterization of a lipopeptide produced by Bacillus thuringiensis CMB26 J Appl Microbiol 97 942 949 10.1111/j.1365-2672.2004.02356.x 1:CAS:528: DC%2BD2cXhtVahtLzI
    • (2004) J Appl Microbiol , vol.97 , pp. 942-949
    • Kim, P.I.1    Bai, H.2    Bai, D.3    Chae, H.4    Chung, S.5    Kim, Y.6    Park, R.7    Chi, Y.T.8
  • 13
    • 0020085068 scopus 로고
    • Utilization of a thermosensitive episome bearing transposon Tn10 to isolate Hfr donor strains of Erwinia carotovora subsp. chrysanthemi
    • 1:CAS:528:DyaL38XhvFChtL0%3D
    • A Kotoujansky M Lemattre P Boistard 1982 Utilization of a thermosensitive episome bearing transposon Tn10 to isolate Hfr donor strains of Erwinia carotovora subsp. chrysanthemi J Bacteriol 150 122 131 1:CAS:528: DyaL38XhvFChtL0%3D
    • (1982) J Bacteriol , vol.150 , pp. 122-131
    • Kotoujansky, A.1    Lemattre, M.2    Boistard, P.3
  • 15
    • 33751427700 scopus 로고    scopus 로고
    • The lipopeptides mycosubtilin and surfactin enhance spreading of Bacillus subtilis strains by their surface-active properties
    • 10.1007/s00203-006-0163-z
    • V Leclère R Marti M Bechet P Fickers P Jacques 2006 The lipopeptides mycosubtilin and surfactin enhance spreading of Bacillus subtilis strains by their surface-active properties Arch Microbiol 186 475 483 10.1007/s00203-006-0163-z
    • (2006) Arch Microbiol , vol.186 , pp. 475-483
    • Leclère, V.1    Marti, R.2    Bechet, M.3    Fickers, P.4    Jacques, P.5
  • 16
    • 21344458408 scopus 로고    scopus 로고
    • Chromosomal integration of sfp gene in Bacillus subtilis to enhance bioavailability of hydrophobic liquids
    • 10.1007/s00253-004-1847-4 1:CAS:528:DC%2BD2MXltlChsro%3D
    • YK Lee SB Kim CS Park JG Kim HM Oh BD Yoon HS Kim 2005 Chromosomal integration of sfp gene in Bacillus subtilis to enhance bioavailability of hydrophobic liquids Appl Microbiol Biotechnol 67 789 794 10.1007/s00253-004- 1847-4 1:CAS:528:DC%2BD2MXltlChsro%3D
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 789-794
    • Lee, Y.K.1    Kim, S.B.2    Park, C.S.3    Kim, J.G.4    Oh, H.M.5    Yoon, B.D.6    Kim, H.S.7
  • 17
    • 0032913465 scopus 로고    scopus 로고
    • Rapid typing of Bacillus subtilis strains by their secondary metabolites using matrix-assisted laser desorption/ionization mass spectrometry of intact cells
    • 10.1002/(SICI)1097-0231(19990530)13:10<943::AID-RCM591>3.0.CO;2-0 1:CAS:528:DyaK1MXjsVyntbc%3D
    • F Leenders TH Stein B Kablitz P Franke J Vater 1999 Rapid typing of Bacillus subtilis strains by their secondary metabolites using matrix-assisted laser desorption/ionization mass spectrometry of intact cells Rapid Commun Mass Spectrom 13 943 949 10.1002/(SICI)1097-0231(19990530)13:10<943::AID- RCM591>3.0.CO;2-0 1:CAS:528:DyaK1MXjsVyntbc%3D
    • (1999) Rapid Commun Mass Spectrom , vol.13 , pp. 943-949
    • Leenders, F.1    Stein, T.H.2    Kablitz, B.3    Franke, P.4    Vater, J.5
  • 18
    • 64249155091 scopus 로고    scopus 로고
    • Nonribosomal peptide synthetases mechanistic and structural aspects of essential domains
    • 10.1016/S0076-6879(09)04813-7 1:CAS:528:DC%2BD1MXpsFejsLo%3D
    • MA Marahiel LO Essen 2009 Nonribosomal peptide synthetases mechanistic and structural aspects of essential domains Methods Enzymol 458 337 351 10.1016/S0076-6879(09)04813-7 1:CAS:528:DC%2BD1MXpsFejsLo%3D
    • (2009) Methods Enzymol , vol.458 , pp. 337-351
    • Marahiel, M.A.1    Essen, L.O.2
  • 19
    • 0035831486 scopus 로고    scopus 로고
    • The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
    • 10.1074/jbc.M009140200 1:CAS:528:DC%2BD3MXislyisr0%3D
    • JJ May TM Wendrich MA Marahiel 2001 The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin J Biol Chem 276 7209 7217 10.1074/jbc.M009140200 1:CAS:528:DC%2BD3MXislyisr0%3D
    • (2001) J Biol Chem , vol.276 , pp. 7209-7217
    • May, J.J.1    Wendrich, T.M.2    Marahiel, M.A.3
  • 20
    • 1942438128 scopus 로고    scopus 로고
    • Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D
    • 10.1111/j.1574-6968.2004.tb09511.x 1:CAS:528:DC%2BD2cXjsVensbc%3D
    • AL Moyne TE Cleveland S Tuzun 2004 Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D FEMS Microbiol Lett 234 43 49 10.1111/j.1574-6968.2004.tb09511.x 1:CAS:528: DC%2BD2cXjsVensbc%3D
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 43-49
    • Moyne, A.L.1    Cleveland, T.E.2    Tuzun, S.3
  • 21
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • 10.1016/0022-2836(70)90057-4 1:CAS:528:DyaE3cXktVShu74%3D
    • SB Needleman CD Wunsch 1970 A general method applicable to the search for similarities in the amino acid sequence of two proteins J Mol Biol 48 443 453 10.1016/0022-2836(70)90057-4 1:CAS:528:DyaE3cXktVShu74%3D
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 22
    • 67649597336 scopus 로고    scopus 로고
    • Ecological fitness of Bacillus subtilis BGS3 regarding production of the surfactin lipopeptide in the rhizosphere
    • 10.1111/j.1758-2229.2009.00017.x 1:CAS:528:DC%2BD1MXotlaktr4%3D
    • V Nihorimbere P Fickers P Thonart M Ongena 2009 Ecological fitness of Bacillus subtilis BGS3 regarding production of the surfactin lipopeptide in the rhizosphere Env Microbiol Reports 1 124 130 10.1111/j.1758-2229.2009.00017.x 1:CAS:528:DC%2BD1MXotlaktr4%3D
    • (2009) Env Microbiol Reports , vol.1 , pp. 124-130
    • Nihorimbere, V.1    Fickers, P.2    Thonart, P.3    Ongena, M.4
  • 23
    • 40049086245 scopus 로고    scopus 로고
    • Bacillus lipopeptides: Versatile weapons for plant disease biocontrol
    • 10.1016/j.tim.2007.12.009
    • M Ongena P Jacques 2008 Bacillus lipopeptides: versatile weapons for plant disease biocontrol Trends Microbiol 16 116 125 10.1016/j.tim.2007.12.009
    • (2008) Trends Microbiol , vol.16 , pp. 116-125
    • Ongena, M.1    Jacques, P.2
  • 24
    • 33947158100 scopus 로고    scopus 로고
    • Surfactin and fengycin lipopeptides of Bacillus subtilis as elicitors of induced systemic resistance in plants
    • 10.1111/j.1462-2920.2006.01202.x 1:CAS:528:DC%2BD2sXktlOrtbo%3D
    • M Ongena E Jourdan A Adam M Paquot A Brans B Joris JL Arpigny P Thonart 2007 Surfactin and fengycin lipopeptides of Bacillus subtilis as elicitors of induced systemic resistance in plants Environ Microbiol 9 1084 1090 10.1111/j.1462-2920.2006.01202.x 1:CAS:528:DC%2BD2sXktlOrtbo%3D
    • (2007) Environ Microbiol , vol.9 , pp. 1084-1090
    • Ongena, M.1    Jourdan, E.2    Adam, A.3    Paquot, M.4    Brans, A.5    Joris, B.6    Arpigny, J.L.7    Thonart, P.8
  • 25
    • 34247855134 scopus 로고    scopus 로고
    • Mass spectrometric analyses of lipopeptides from Bacillus strains isolated from diverse geographical locations
    • 10.1111/j.1574-6968.2007.00702.x 1:CAS:528:DC%2BD2sXlslSlsL8%3D
    • NP Price AP Rooney JL Swezey E Perry FM Cohan 2007 Mass spectrometric analyses of lipopeptides from Bacillus strains isolated from diverse geographical locations FEMS Microbiol Lett 271 83 89 10.1111/j.1574-6968.2007. 00702.x 1:CAS:528:DC%2BD2sXlslSlsL8%3D
    • (2007) FEMS Microbiol Lett , vol.271 , pp. 83-89
    • Price, N.P.1    Rooney, A.P.2    Swezey, J.L.3    Perry, E.4    Cohan, F.M.5
  • 26
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVM)
    • 10.1093/nar/gki885 1:CAS:528:DC%2BD2MXht1OmsbjI
    • C Rausch T Weber O Kohlbacher W Wohlleben DH Huson 2005 Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVM) Nucleic Acids Res 33 5799 5808 10.1093/nar/gki885 1:CAS:528:DC%2BD2MXht1OmsbjI
    • (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
  • 28
    • 76649110542 scopus 로고    scopus 로고
    • New approach for the detection of non ribosomal peptide synthetase genes in Bacillus strains by polymerase chain reaction
    • 10.1007/s00253-009-2176-4 1:CAS:528:DC%2BC3cXmvVGrtg%3D%3D
    • A Tapi M Chollet-Imbert B Scherens P Jacques 2010 New approach for the detection of non ribosomal peptide synthetase genes in Bacillus strains by polymerase chain reaction Appl Microbiol Biotechnol 85 1521 1531 10.1007/s00253-009-2176-4 1:CAS:528:DC%2BC3cXmvVGrtg%3D%3D
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1521-1531
    • Tapi, A.1    Chollet-Imbert, M.2    Scherens, B.3    Jacques, P.4
  • 29
    • 0037069317 scopus 로고    scopus 로고
    • Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase
    • 10.1021/bi026592a 1:CAS:528:DC%2BD38XnvVOjsbo%3D
    • CC Tseng SD Bruner RM Kohli MA Marahiel CT Walsh SA Sieber 2002 Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase Biochem 41 13350 13351 10.1021/bi026592a 1:CAS:528:DC%2BD38XnvVOjsbo%3D
    • (2002) Biochem , vol.41 , pp. 13350-13351
    • Tseng, C.C.1    Bruner, S.D.2    Kohli, R.M.3    Marahiel, M.A.4    Walsh, C.T.5    Sieber, S.A.6
  • 30
    • 0022457256 scopus 로고
    • Fengycin a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3
    • 1:CAS:528:DyaL28XltlSns7Y%3D
    • N Vanittanakom W Loeffler U Koch G Jung 1986 Fengycin a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3 J Antibiot 39 888 901 1:CAS:528:DyaL28XltlSns7Y%3D
    • (1986) J Antibiot , vol.39 , pp. 888-901
    • Vanittanakom, N.1    Loeffler, W.2    Koch, U.3    Jung, G.4
  • 31
    • 0036952601 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge
    • 10.1128/AEM.68.12.6210-6219.2002 1:CAS:528:DC%2BD38Xptlartb4%3D
    • J Vater B Kablitz C Wilde P Franke N Mehta SS Cameotra 2002 Matrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge Appl Environ Microbiol 68 6210 6219 10.1128/AEM.68.12.6210-6219.2002 1:CAS:528:DC%2BD38Xptlartb4%3D
    • (2002) Appl Environ Microbiol , vol.68 , pp. 6210-6219
    • Vater, J.1    Kablitz, B.2    Wilde, C.3    Franke, P.4    Mehta, N.5    Cameotra, S.S.6


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