메뉴 건너뛰기




Volumn 193, Issue 1, 2011, Pages 215-224

Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42

Author keywords

[No Author keywords available]

Indexed keywords

CYSTINE; MICROCIN B17; PLANTAZOLICIN; SERINE; STREPTOLYSIN S; THREONINE; UNCLASSIFIED DRUG;

EID: 78650083538     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00784-10     Document Type: Article
Times cited : (166)

References (39)
  • 2
    • 79961051980 scopus 로고    scopus 로고
    • Relationship of Bacillus amyloliquefaciens clades associated with strains DSM7T and FZB42: A proposal for Bacillus amyloliquefaciens subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens subsp. plantarum subsp. nov. based on their discriminating complete genome sequences
    • 3 September [Epub ahead of print.] doi:10.1099/ijs.0.023267-0
    • Borriss, R., X. Chen, C. Rueckert, J. Blom, A. Becker, B. Baumgarth, B. Fan, R. Pukall, P. Schumann, C. Sproer, H. Junge, J. Vater, A. Puhler, and H. P. Klenk. 3 September 2010. Relationship of Bacillus amyloliquefaciens clades associated with strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens subsp. plantarum subsp. nov. based on their discriminating complete genome sequences. Int. J. Syst. Evol. Microbiol. [Epub ahead of print.] doi:10.1099/ijs.0.023267-0.
    • (2010) Int. J. Syst. Evol. Microbiol.
    • Borriss, R.1    Chen, X.2    Rueckert, C.3    Blom, J.4    Becker, A.5    Baumgarth, B.6    Fan, B.7    Pukall, R.8    Schumann, P.9    Sproer, C.10    Junge, H.11    Vater, J.12    Puhler, A.13    Klenk, H.P.14
  • 3
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L. S., M. A. Pennella, and D. P. Giedroc. 2003. The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 27:131-143.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 4
    • 33645803827 scopus 로고    scopus 로고
    • Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli
    • Butcher, B. G., and J. D. Helmann. 2006. Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli. Mol. Microbiol. 60:765-782.
    • (2006) Mol. Microbiol. , vol.60 , pp. 765-782
    • Butcher, B.G.1    Helmann, J.D.2
  • 6
    • 55249127380 scopus 로고    scopus 로고
    • More than anticipated-production of antibiotics and other secondary metabolites by Bacillus amyloliquefaciens FZB42
    • Chen, X.-H., A. Koumoutsi, R. Scholz, and R. Borriss. 2009. More than anticipated-production of antibiotics and other secondary metabolites by Bacillus amyloliquefaciens FZB42. J. Mol. Microbiol. Biotechnol. 16:14-24.
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.16 , pp. 14-24
    • Chen, X.-H.1    Koumoutsi, A.2    Scholz, R.3    Borriss, R.4
  • 9
    • 61649127530 scopus 로고    scopus 로고
    • Difficidin and bacilysin produced by plant-associated Bacillus amyloliquefaciens are efficient in controlling fire blight disease
    • Chen, X.-H., R. Scholz, M. Borriss, H. Junge, G. Mogel, S. Kunz, and R. Borriss. 2009. Difficidin and bacilysin produced by plant-associated Bacillus amyloliquefaciens are efficient in controlling fire blight disease. J. Biotechnol. 140:38-44.
    • (2009) J. Biotechnol. , vol.140 , pp. 38-44
    • Chen, X.-H.1    Scholz, R.2    Borriss, M.3    Junge, H.4    Mogel, G.5    Kunz, S.6    Borriss, R.7
  • 10
    • 69949150299 scopus 로고    scopus 로고
    • Interactions of Bacillus spp. and plants - With special reference to induced systemic resistance (ISR)
    • Choudhary, D. K., and B. N. Johri. 2009. Interactions of Bacillus spp. and plants - with special reference to induced systemic resistance (ISR). Microbiol. Res. 164:493-513.
    • (2009) Microbiol. Res. , vol.164 , pp. 493-513
    • Choudhary, D.K.1    Johri, B.N.2
  • 12
    • 17644385827 scopus 로고    scopus 로고
    • Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection
    • Datta, V., S. M. Myskowski, L. A. Kwinn, D. N. Chiem, N. Varki, R. G. Kansal, M. Kotb, and V. Nizet. 2005. Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection. Mol. Microbiol. 56:681-695.
    • (2005) Mol. Microbiol. , vol.56 , pp. 681-695
    • Datta, V.1    Myskowski, S.M.2    Kwinn, L.A.3    Chiem, D.N.4    Varki, N.5    Kansal, R.G.6    Kotb, M.7    Nizet, V.8
  • 13
    • 2942525390 scopus 로고    scopus 로고
    • Screening genomes of Gram-positive bacteria for double-glycine-motif- containing peptides
    • Dirix, G., P. Monsieurs, K. Marchal, J. Vanderleyden, and J. Michiels. 2004. Screening genomes of Gram-positive bacteria for double-glycine-motif- containing peptides. Microbiology 150:1121-1126. (Pubitemid 38744710)
    • (2004) Microbiology , vol.150 , Issue.5 , pp. 1121-1126
    • Dirix, G.1    Monsieurs, P.2    Marchal, K.3    Vanderleyden, J.4    Michiels, J.5
  • 14
    • 77952511174 scopus 로고    scopus 로고
    • Expansion of ribosomally produced natural products: A nitrile hydratase- and Nif11-related precursor family
    • Haft, D. H., M. K. Basu, and D. A. Mitchell. 2010. Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family. BMC Biol. 8:70.
    • (2010) BMC Biol. , vol.8 , pp. 70
    • Haft, D.H.1    Basu, M.K.2    Mitchell, D.A.3
  • 15
    • 76549163077 scopus 로고
    • The mechanism of the Schiff reaction as studied with histochemical model systems
    • Hardonk, M. J., and D. Van. 1964. The mechanism of the Schiff reaction as studied with histochemical model systems. J. Histochem. Cytochem. 12:748-751.
    • (1964) J. Histochem. Cytochem. , vol.12 , pp. 748-751
    • Hardonk, M.J.1    Van, D.2
  • 16
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction
    • Horton, R. M., Z. L. Cai, S. N. Ho, and L. R. Pease. 1990. Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques 8:528-535.
    • (1990) Biotechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 17
    • 0036064383 scopus 로고    scopus 로고
    • Extracellular phytase activity of Bacillus amyloliquefaciens FZB45 contributes to its plant-growth-promoting effect
    • Idriss, E. E., O. Makarewicz, A. Farouk, K. Rosner, R. Greiner, H. Bochow, T. Richter, and R. Borriss. 2002. Extracellular phytase activity of Bacillus amyloliquefaciens FZB45 contributes to its plant-growth-promoting effect. Microbiology 148:2097-2109.
    • (2002) Microbiology , vol.148 , pp. 2097-2109
    • Idriss, E.E.1    Makarewicz, O.2    Farouk, A.3    Rosner, K.4    Greiner, R.5    Bochow, H.6    Richter, T.7    Borriss, R.8
  • 18
    • 67749113468 scopus 로고    scopus 로고
    • Thiostrepton biosynthesis: Prototype for a new family of bacteriocins
    • Kelly, W. L., L. Pan, and C. Li. 2009. Thiostrepton biosynthesis: prototype for a new family of bacteriocins. J. Am. Chem. Soc. 131:4327-4334.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4327-4334
    • Kelly, W.L.1    Pan, L.2    Li, C.3
  • 19
    • 1142298587 scopus 로고    scopus 로고
    • Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42
    • Koumoutsi, A., X.-H. Chen, A. Henne, H. Liesegang, G. Hitzeroth, P. Franke, J. Vater, and R. Borriss. 2004. Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42. J. Bacteriol. 186:1084-1096.
    • (2004) J. Bacteriol. , vol.186 , pp. 1084-1096
    • Koumoutsi, A.1    Chen, X.-H.2    Henne, A.3    Liesegang, H.4    Hitzeroth, G.5    Franke, P.6    Vater, J.7    Borriss, R.8
  • 20
    • 35948941266 scopus 로고    scopus 로고
    • DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42
    • Koumoutsi, A., X.-H. Chen, J. Vater, and R. Borriss. 2007. DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42. Appl. Environ. Microbiol. 73:6953-6964.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6953-6964
    • Koumoutsi, A.1    Chen, X.-H.2    Vater, J.3    Borriss, R.4
  • 21
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and G. Rapoport. 1995. Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J. Bacteriol. 177:2403-2407.
    • (1995) J. Bacteriol. , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 22
    • 33644857535 scopus 로고    scopus 로고
    • In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon
    • Le Breton, Y., N. P. Mohapatra, and W. G. Haldenwang. 2006. In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon. Appl. Environ. Microbiol. 72:327-333.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 327-333
    • Le Breton, Y.1    Mohapatra, N.P.2    Haldenwang, W.G.3
  • 24
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Li, Y. M., J. C. Milne, L. L. Madison, R. Kolter, and C. T. Walsh. 1996. From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 274:1188-1193.
    • (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
  • 25
    • 60549109637 scopus 로고    scopus 로고
    • Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications
    • Liao, R., L. Duan, C. Lei, H. Pan, Y. Ding, Q. Zhang, D. Chen, B. Shen, Y. Yu, and W. Liu. 2009. Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. Chem. Biol. 16:141-147.
    • (2009) Chem. Biol. , vol.16 , pp. 141-147
    • Liao, R.1    Duan, L.2    Lei, C.3    Pan, H.4    Ding, Y.5    Zhang, Q.6    Chen, D.7    Shen, B.8    Yu, Y.9    Liu, W.10
  • 26
    • 67649730080 scopus 로고    scopus 로고
    • Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S
    • Mitchell, D. A., S. W. Lee, M. A. Pence, A. L. Markley, J. D. Limm, V. Nizet, and J. E. Dixon. 2009. Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S. J. Biol. Chem. 284:13004-13012.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13004-13012
    • Mitchell, D.A.1    Lee, S.W.2    Pence, M.A.3    Markley, A.L.4    Limm, J.D.5    Nizet, V.6    Dixon, J.E.7
  • 28
    • 70350170630 scopus 로고    scopus 로고
    • Insights into the mode of action of the two-peptide lantibiotic haloduracin
    • Oman, T. J., and W. A. van der Donk. 2009. Insights into the mode of action of the two-peptide lantibiotic haloduracin. ACS Chem. Biol. 4:865-874.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 865-874
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 29
    • 0035339494 scopus 로고    scopus 로고
    • Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
    • Pei, J., and N. V. Grishin. 2001. Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem. Sci. 26:275-277.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 275-277
    • Pei, J.1    Grishin, N.V.2
  • 31
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 33
    • 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., J. T. Nelson, D. A. Rasko, S. Sudek, J. A. Eisen, M. G. Haygood, and J. Ravel. 2005. Patellamide A and C biosynthesis by a microcin- like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. Proc. Natl. Acad. Sci. U. S. A. 102:7315-7320.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7315-7320
    • Schmidt, E.W.1    Nelson, J.T.2    Rasko, D.A.3    Sudek, S.4    Eisen, J.A.5    Haygood, M.G.6    Ravel, J.7
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0030944568 scopus 로고    scopus 로고
    • Double-glycinetype leader peptides direct secretion of bacteriocins by ABC transporters: Colicin V secretion in Lactococcus lactis
    • van Belkum, M. J., R. W. Worobo, and M. E. Stiles. 1997. Double-glycinetype leader peptides direct secretion of bacteriocins by ABC transporters: colicin V secretion in Lactococcus lactis. Mol. Microbiol. 23:1293-1301.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1293-1301
    • Van Belkum, M.J.1    Worobo, R.W.2    Stiles, M.E.3
  • 36
    • 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
    • Vater, J., B. Kablitz, C. Wilde, P. Franke, N. Mehta, and S. S. 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.
    • (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
  • 38
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund, H., and A. Elofsson. 2008. OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24:1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 39
    • 62449284698 scopus 로고    scopus 로고
    • Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
    • Wieland Brown, L. C., et al. 2009. Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin. Proc. Natl. Acad. Sci. U. S. A. 106:2549-2553.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2549-2553
    • Wieland Brown, L.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.