메뉴 건너뛰기




Volumn 64, Issue 9, 1998, Pages 3140-3146

Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analysis of its biosynthetic gene cluster

Author keywords

[No Author keywords available]

Indexed keywords

EPICIDIN 280; GENE PRODUCT; LANTIBIOTIC; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0031665461     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.9.3140-3146.1998     Document Type: Article
Times cited : (114)

References (48)
  • 1
    • 0022929886 scopus 로고
    • Epidermin: Sequencing of a heterodet tetracyclic 21-peptide amide antibiotic
    • Allgaier, H., G. Jung, R. G. Werner, U. Schneider, and H. Zähner. 1986. Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic. Eur. J. Biochem. 160:9-22.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 9-22
    • Allgaier, H.1    Jung, G.2    Werner, R.G.3    Schneider, U.4    Zähner, H.5
  • 4
    • 85084726291 scopus 로고
    • Construction of an expression system for mutagenesis of the lantibiotic Pep5
    • Bierbaum, G., M. Reis, C. Szekat, and H.-G. Sahl. 1994. Construction of an expression system for mutagenesis of the lantibiotic Pep5. Appl. Environ. Microbiol. 60:2876-2883.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2876-2883
    • Bierbaum, G.1    Reis, M.2    Szekat, C.3    Sahl, H.-G.4
  • 6
    • 0028952641 scopus 로고
    • Mode of action of the lantibiotic mersacidm: Inhibition of peptidogiycan biosynthesis via a novel mechanism?
    • Brötz, H., G. Bierbaum, A. Markus, E. Molitor, and H.-G. Sahl. 1995. Mode of action of the lantibiotic mersacidm: inhibition of peptidogiycan biosynthesis via a novel mechanism? Antimicrob. Agents Chemother. 39:714-719.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 714-719
    • Brötz, H.1    Bierbaum, G.2    Markus, A.3    Molitor, E.4    Sahl, H.-G.5
  • 7
    • 0029028865 scopus 로고
    • Maturation pathway of nisin and other lantibiotics: Post-translationally mod- Ified antimicrobial peptides exported by Gram-positive bacteria
    • De Vos, W. M., O.P. Kuipers, J. R, Vanner Meer, and R. J. Siezen. 1995. Maturation pathway of nisin and other lantibiotics: post-translationally mod- ified antimicrobial peptides exported by Gram-positive bacteria. Mol. Microbiol. 17:427-437.
    • (1995) Mol. Microbiol. , vol.17 , pp. 427-437
    • De Vos, W.M.1    Kuipers, O.P.2    Vanner Meer, J.R.3    Siezen, R.J.4
  • 8
    • 0021705344 scopus 로고
    • Plasmid involvement in production and immunity to the staphyloeoccin-like peptide Pep5
    • Ersfeld-Dreßen, H., H.-G. Sahl, and H. Brandis. 1984. Plasmid involvement in production and immunity to the staphyloeoccin-like peptide Pep5. J. Gen. Microbiol. 130:3029-3035.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 3029-3035
    • Ersfeld-Dreßen, H.1    Sahl, H.-G.2    Brandis, H.3
  • 9
    • 0023255862 scopus 로고
    • Homologous direct repeat sequences associated with mercury, methicillin, tetracycline and trimethoprim resistance determinants in Staphylococcus aureus
    • Gillespie, M. T., B. R. Lyon, L. S. L. Loo, P. R. Matthews, P. R. Stewart, and R. A. Skurray. 1987. Homologous direct repeat sequences associated with mercury, methicillin, tetracycline and trimethoprim resistance determinants in Staphylococcus aureus. FEMS Lett, 43:165-171
    • (1987) FEMS Lett , vol.43 , pp. 165-171
    • Gillespie, M.T.1    Lyon, B.R.2    Loo, L.S.L.3    Matthews, P.R.4    Stewart, P.R.5    Skurray, R.A.6
  • 10
    • 0015215446 scopus 로고
    • The structure of nisin
    • Gross, E., and J. L. Morell. 1971. The structure of nisin. J. Am. Chem. Soc. 93:4634-4635.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 4634-4635
    • Gross, E.1    Morell, J.L.2
  • 13
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 14
    • 0014682230 scopus 로고
    • Synthesis of the antibiotic nisin: Formation of lanthionine and methyl-lanthionine
    • Ingram, L. C. 1969. Synthesis of the antibiotic nisin: formation of lanthionine and methyl-lanthionine. Biochim. Biophys. Acta 184:216-219.
    • (1969) Biochim. Biophys. Acta , vol.184 , pp. 216-219
    • Ingram, L.C.1
  • 15
    • 0022973209 scopus 로고
    • Nucleotide sequence of the luxB gene of Vibrio harveyi and the complete amino acid sequence of the beta subunit of bacterial lucifera.se
    • Johnston, T. C., R. B. Thompson, and T. O. Baldwin. 1986. Nucleotide sequence of the luxB gene of Vibrio harveyi and the complete amino acid sequence of the beta subunit of bacterial lucifera.se. J. Biol. Chem. 261:4805-4811.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4805-4811
    • Johnston, T.C.1    Thompson, R.B.2    Baldwin, T.O.3
  • 17
    • 3543023946 scopus 로고
    • Lantibiotics-ribosomally synthesised biologically active polypeptides containing sulphide rings and α,β-didehydroamino acids
    • G. Jung and H.-G. Sahl (ed.), Escom, Leiden, The Netherlands
    • Jung, G. 1991. Lantibiotics-ribosomally synthesised biologically active polypeptides containing sulphide rings and α,β-didehydroamino acids, p. 2-34. In G. Jung and H.-G. Sahl (ed.), Nisin and novel lantibiotics, Escom, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 2-34
    • Jung, G.1
  • 19
    • 0026530785 scopus 로고
    • Analysis of genes involved in biosynthesis of the lantibiotic subtilin
    • Klein, C., C. Kaletta, N. Schnell, and K.-D. Entian. 1992. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl. Environ. Microbiol. 58:132-142.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 132-142
    • Klein, C.1    Kaletta, C.2    Schnell, N.3    Entian, K.-D.4
  • 20
    • 0028037950 scopus 로고
    • Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis
    • Klein, C., and K.-D. Entian. 1994. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis. Appl. Environ. Microbiol. 60:2793-2801.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2793-2801
    • Klein, C.1    Entian, K.-D.2
  • 21
    • 0023858915 scopus 로고
    • Mode of action of the staphylococcin-like peptide Pep5: Voltage-dependent depolarization of bacterial and artificial membranes
    • Kordel, M., R. Benz, and H.-G, Sahl. 1988. Mode of action of the staphylococcin-like peptide Pep5: voltage-dependent depolarization of bacterial and artificial membranes. J. Bacteriol. 170:84-88.
    • (1988) J. Bacteriol. , vol.170 , pp. 84-88
    • Kordel, M.1    Benz, R.2    Sahl, H.-G.3
  • 22
    • 0027162304 scopus 로고
    • Characterisation of the nisin gene cluster nisABTCIPR of Lactococcus lactis: Requirement of the expression of nisA and nisI genes for development of immunity
    • Kuipers, O. P., M. M. Beerthuyzen, R. J. Siezen, and W. M. De Vos. 1993. Characterisation of the nisin gene cluster nisABTCIPR of Lactococcus lactis: requirement of the expression of nisA and nisI genes for development of immunity. Eur. J. Biochem. 216:281-292.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 281-292
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    De Vos, W.M.4
  • 23
    • 0029115380 scopus 로고
    • Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of Pep5 and PepC; evidence for a role of PepC in the thioether formation
    • Meyer, C., G. Bierbaum, C. Heidrich, M, Reis, J. Süling, M. I. Iglesias-Wind, C. Kempter, E. Molitor, and H.-G. Sahl. 1995. Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of Pep5 and PepC; evidence for a role of PepC in the thioether formation. Eur. J. Biochem. 232:478-489.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 478-489
    • Meyer, C.1    Bierbaum, G.2    Heidrich, C.3    Reis, M.4    Süling, J.5    Iglesias-Wind, M.I.6    Kempter, C.7    Molitor, E.8    Sahl, H.-G.9
  • 24
    • 0028007156 scopus 로고
    • Sequence analysis of lantibiotics: Chemical derivatizalion procedures allow a fast access to complete Edman degradation
    • Meyer, H. E., M. Heber, B. Eisermann, H. Korte, J. W. Metzger, and G. Jung. 1994. Sequence analysis of lantibiotics: chemical derivatizalion procedures allow a fast access to complete Edman degradation. Anal. Biochem. 223:185-190.
    • (1994) Anal. Biochem. , vol.223 , pp. 185-190
    • Meyer, H.E.1    Heber, M.2    Eisermann, B.3    Korte, H.4    Metzger, J.W.5    Jung, G.6
  • 25
    • 0030983728 scopus 로고    scopus 로고
    • Secretion of the lantibiotics epidermin and gallidermin: Sequence, influence on epidermin production, and regulation of gdmT and gdmH by EpiQ
    • Peschel, A., N. Schnell, M. Hille, K.-D. Entian, and F. Götz. 1997. Secretion of the lantibiotics epidermin and gallidermin: sequence, influence on epidermin production, and regulation of gdmT and gdmH by EpiQ. Mol. Gen. Genet. 254:312-318.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 312-318
    • Peschel, A.1    Schnell, N.2    Hille, M.3    Entian, K.-D.4    Götz, F.5
  • 26
    • 0027931272 scopus 로고
    • Producer immunity towards the lantibiotic Pep5: Identification of the immunity gene pepI and localization and functional analysis of its gene product
    • Reis, M., M. Eschbach-Bludau, M. I. Iglesias-Wind, T. Kupke, and H.-G. Sahl. 1994. Producer immunity towards the lantibiotic Pep5: identification of the immunity gene pepI and localization and functional analysis of its gene product. Appl. Environ. Microbiol. 60:2876-2883.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2876-2883
    • Reis, M.1    Eschbach-Bludau, M.2    Iglesias-Wind, M.I.3    Kupke, T.4    Sahl, H.-G.5
  • 27
    • 0024458146 scopus 로고
    • Trimethoprim resistance transposon Tn4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257
    • Rouch, D. A., L. J. Messerotti, L. S. Loo, C. A. Jackson, and R, A. Skurray. 1989. Trimethoprim resistance transposon Tn4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257. Mol. Microbiol. 3:161-175.
    • (1989) Mol. Microbiol. , vol.3 , pp. 161-175
    • Rouch, D.A.1    Messerotti, L.J.2    Loo, L.S.3    Jackson, C.A.4    Skurray, R.A.5
  • 28
    • 0019801262 scopus 로고
    • Production, purification and chemical properties of an antistaphylococcal agent produced by Staphylococcus epi- Dermidis
    • Sahl, H.-G., and H. Brandis. 1981. Production, purification and chemical properties of an antistaphylococcal agent produced by Staphylococcus epi- dermidis. J. Gen. Microbiol. 127:377-384.
    • (1981) J. Gen. Microbiol. , vol.127 , pp. 377-384
    • Sahl, H.-G.1    Brandis, H.2
  • 29
  • 30
    • 0023491341 scopus 로고
    • Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin
    • Sahl, H.-G., M. Kordel, and R. Benz. 1987. Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch. Microbiol. 149:120-124.
    • (1987) Arch. Microbiol. , vol.149 , pp. 120-124
    • Sahl, H.-G.1    Kordel, M.2    Benz, R.3
  • 31
    • 0003107982 scopus 로고
    • Pore formation in bacterial membranes by cationic Iantibiotics
    • G. Jung and H.-G. Sahl (ed.), Escom, Leiden, The Netherlands
    • Sahl, H.-G. 1991. Pore formation in bacterial membranes by cationic Iantibiotics, p, 347-358: In G. Jung and H.-G. Sahl (ed.), Nisin and novel lantibiotics, Escom, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 347-358
    • Sahl, H.-G.1
  • 32
    • 0029055380 scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of peptides with unique posttranslational modifications
    • Sahl, H.-G., R. W. Jack, and G. Bierbaum. 1995. Lantibiotics: biosynthesis and biological activities of peptides with unique posttranslational modifications. Eur. J. Biochem. 230:827-853.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 827-853
    • Sahl, H.-G.1    Jack, R.W.2    Bierbaum, G.3
  • 33
    • 0020265937 scopus 로고
    • Description of a new species of the genus Staphylococcus: Staphylococcus carnosus
    • Schleifer, K. H., and U. Fischer. 1982. Description of a new species of the genus Staphylococcus: Staphylococcus carnosus. Int. J. Syst. Bacteriol. 32: 153-156.
    • (1982) Int. J. Syst. Bacteriol. , vol.32 , pp. 153-156
    • Schleifer, K.H.1    Fischer, U.2
  • 34
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesised antibiotic with four sulfide rings
    • Schnell, N., K.-D. Entian, U. Schneider, F. Götz, H. Zähner, R. Kellner, and G. Jung. 1988. Prepeptide sequence of epidermin, a ribosomally synthesised antibiotic with four sulfide rings. Nature 333:276-278.
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.-D.2    Schneider, U.3    Götz, F.4    Zähner, H.5    Kellner, R.6    Jung, G.7
  • 35
    • 0028966278 scopus 로고
    • Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3
    • Siegers, K., and K.-D. Entian. 1995. Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3. Appl. Environ. Microbiol. 61:1082-1089.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1082-1089
    • Siegers, K.1    Entian, K.-D.2
  • 36
    • 0030046733 scopus 로고    scopus 로고
    • Comparison of the lantibiotic gene clusters and encoded proteins
    • Siezen, R. J., O. P. Kuipers, aad W. M. De Vos. 1996. Comparison of the lantibiotic gene clusters and encoded proteins. Antonie Leeuwenhoek 69: 171-184.
    • (1996) Antonie Leeuwenhoek , vol.69 , pp. 171-184
    • Siezen, R.J.1    Kuipers, O.P.2    De Vos, W.M.3
  • 38
    • 0030964778 scopus 로고    scopus 로고
    • Organization and expression of a gene cluster involved in the biosynthesis of the lantibiotic lactocin
    • Skaugen, M., C. I. M. Abildgaard, and I. F. Nes. 1997. Organization and expression of a gene cluster involved in the biosynthesis of the lantibiotic lactocin S. Mol. Gen. Genet. 253:674-686.
    • (1997) S. Mol. Gen. Genet. , vol.253 , pp. 674-686
    • Skaugen, M.1    Abildgaard, C.I.M.2    Nes, I.F.3
  • 39
    • 0029034856 scopus 로고
    • Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphyhcoccus epidermidis K7. Cloning and characterization of the epilancin K7 encoding gene and NMR analysis of mature epilancin K7
    • Van de Kamp, M., H. W. Van den Hooven, R. N. H. Konings, G. Bierhaum, H.-G. Sahl, O. P. Kuipers, R. J. Siezen, W. M. De Vos, C. W. Hilbers, and F. J. M. Van de Ven. 1995. Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphyhcoccus epidermidis K7. Cloning and characterization of the epilancin K7 encoding gene and NMR analysis of mature epilancin K7. Eur. J. Biochem. 230:587-600.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 587-600
    • Van de Kamp, M.1    Van Den Hooven, H.W.2    Konings, R.N.H.3    Bierhaum, G.4    Sahl, H.-G.5    Kuipers, O.P.6    Siezen, R.J.7    De Vos, W.M.8    Hilbers, C.W.9    Van de Ven, F.J.M.10
  • 40
    • 0030059436 scopus 로고    scopus 로고
    • Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate
    • Van den Hooven, H. W., C. A. E. Doeland, M. Van de Kamp, R. N. H. Konings, C. W. Hilbers, and F. J. M. Van de Ven. 1996. Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate. Eur. J. Biochem. 235:382-393.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 382-393
    • Van den Hooven, H.W.1    Doeland, C.A.E.2    Van de Kamp, M.3    Konings, R.N.H.4    Hilbers, C.W.5    Van de Ven, F.J.M.6
  • 41
    • 0030067073 scopus 로고    scopus 로고
    • Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate
    • Van den Hooven, H. W., C. A. E. M. Spronk, M. Van de Kamp, R. N. H. Konings, C. W. Hilbers, and F. J. M. Van de Ven. 1996. Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate. Eur. J. Biochem. 235:394-403.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 394-403
    • Van den Hooven, H.W.1    Spronk, C.A.E.M.2    Van de Kamp, M.3    Konings, R.N.H.4    Hilbers, C.W.5    Van De Ven, F.J.M.6
  • 42
    • 0028017962 scopus 로고
    • Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis
    • Van der Meer, J. R., H. S. Rollenia, R. J. Siezen, M. M. Beerthuyzen, O. P. Kuipers, and W. M. De Vos. 1994. Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis. J. Biol. Chem. 269:3555-3562.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3555-3562
    • Van der Meer, J.R.1    Rollenia, H.S.2    Siezen, R.J.3    Beerthuyzen, M.M.4    Kuipers, O.P.5    De Vos, W.M.6
  • 43
  • 44
    • 0025245731 scopus 로고
    • Biosynthesis of the lantibiotic Pep5. Isolation and characterization of a prepeptide containing dehydroamino acids
    • Weil, H.-P., A. G. Beck-Sickinger, J. Metzger, S. Stevanovic, G. Jung, M. Josten, and H.-G. Sahl. 1990. Biosynthesis of the lantibiotic Pep5. Isolation and characterization of a prepeptide containing dehydroamino acids. Eur. J. Biochem. 194:217-223.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 217-223
    • Weil, H.-P.1    Beck-Sickinger, A.G.2    Metzger, J.3    Stevanovic, S.4    Jung, G.5    Josten, M.6    Sahl, H.-G.7
  • 46
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-109.
    • (1985) Gene , vol.33 , pp. 103-109
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.