메뉴 건너뛰기




Volumn 458, Issue A, 2009, Pages 559-574

Chapter 22 Whole-Cell Generation of Lantibiotic Variants

Author keywords

[No Author keywords available]

Indexed keywords

ACTAGARDIN; EPIDERMIN; GALLIDERMIN; LACTICIN 3147; LANTHIOPEPTIN; LANTIBIOTIC; MERSACIDIN; MUTACIN 2; NISIN; NUKACIN; PEP5 LANTIBIOTIC; SUBTILIN; UNCLASSIFIED DRUG;

EID: 64249162751     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)04822-8     Document Type: Review
Times cited : (23)

References (47)
  • 1
    • 33748781971 scopus 로고    scopus 로고
    • Lysine-oriented charges trigger the membrane binding and activity of Nukacin ISK-1
    • Asaduzzaman S.M., Nagao J.-I., Aso Y., Nakayama J., and Sonomoto K. Lysine-oriented charges trigger the membrane binding and activity of Nukacin ISK-1. Appl. Environ. Microbiol. 72 9 (2006) 6012-6017
    • (2006) Appl. Environ. Microbiol. , vol.72 , Issue.9 , pp. 6012-6017
    • Asaduzzaman, S.M.1    Nagao, J.-I.2    Aso, Y.3    Nakayama, J.4    Sonomoto, K.5
  • 2
    • 12444307516 scopus 로고    scopus 로고
    • Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic nukacin ISK-1
    • Aso Y., Nagao J.-I., Koga H., Okuda K.-I., Kanemasa Y., Sashihara T., Nakayama J., and Sonomoto K. Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic nukacin ISK-1. J. Biosci. Bioeng. 98 6 (2004) 429-436
    • (2004) J. Biosci. Bioeng. , vol.98 , Issue.6 , pp. 429-436
    • Aso, Y.1    Nagao, J.-I.2    Koga, H.3    Okuda, K.-I.4    Kanemasa, Y.5    Sashihara, T.6    Nakayama, J.7    Sonomoto, K.8
  • 4
    • 0028007534 scopus 로고
    • Construction of an expression system for engineering of the lantibiotic Pep5
    • Bierbaum G., Reis M., Szekat C., and Sahl H.G. Construction of an expression system for engineering of the lantibiotic Pep5. Appl. Environ. Microbiol. 60 12 (1994) 4332-4338
    • (1994) Appl. Environ. Microbiol. , vol.60 , Issue.12 , pp. 4332-4338
    • Bierbaum, G.1    Reis, M.2    Szekat, C.3    Sahl, H.G.4
  • 5
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman M., Logan R., O'Brien K., Seno E.T., Rao R.N., and Schoner B.E. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116 (1992) 43-49
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 7
    • 0343052949 scopus 로고    scopus 로고
    • Gene replacement in Staphylococcus carnosus and Staphylococcus xylosus
    • Brückner R. Gene replacement in Staphylococcus carnosus and Staphylococcus xylosus. FEMS Microbiol. Lett. 151 (1997) 1-8
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 1-8
    • Brückner, R.1
  • 10
  • 11
    • 0031842742 scopus 로고    scopus 로고
    • Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy
    • Chen P., Novak J., Kirk M., Barnes S., Qi F., and Caufield P.W. Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy. Appl. Environ. Microbiol. 64 7 (1998) 2335-2340
    • (1998) Appl. Environ. Microbiol. , vol.64 , Issue.7 , pp. 2335-2340
    • Chen, P.1    Novak, J.2    Kirk, M.3    Barnes, S.4    Qi, F.5    Caufield, P.W.6
  • 12
    • 0344837858 scopus 로고    scopus 로고
    • Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtilisin (AprE), WprA, and Vpr
    • Corvey C., Stein T., Dusterhus S., Karas M., and Entian K.D. Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtilisin (AprE), WprA, and Vpr. Biochem. Biophys. Res. Commun. 304 (2003) 48-54
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 48-54
    • Corvey, C.1    Stein, T.2    Dusterhus, S.3    Karas, M.4    Entian, K.D.5
  • 13
    • 0037227138 scopus 로고    scopus 로고
    • A food-grade approach for functional analysis and modification of native plasmids in Lactococcus lactis
    • Cotter P.D., Hill C., and Ross R.P. A food-grade approach for functional analysis and modification of native plasmids in Lactococcus lactis. Appl. Environ. Microbiol. 69 1 (2003) 702-706
    • (2003) Appl. Environ. Microbiol. , vol.69 , Issue.1 , pp. 702-706
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 14
    • 33749999203 scopus 로고    scopus 로고
    • Complete alanine scanning of the two-component lantibiotic lacticin 3147: Generating a blueprint for rational drug design
    • Cotter P.D., Deegan L.H., Lawton E.M., Draper L.A., O'Connor P.M., Hill C., and Ross R.P. Complete alanine scanning of the two-component lantibiotic lacticin 3147: Generating a blueprint for rational drug design. Mol. Microbiol. 62 (2006) 735-747
    • (2006) Mol. Microbiol. , vol.62 , pp. 735-747
    • Cotter, P.D.1    Deegan, L.H.2    Lawton, E.M.3    Draper, L.A.4    O'Connor, P.M.5    Hill, C.6    Ross, R.P.7
  • 17
    • 0026473125 scopus 로고
    • A lactococcal expression system for engineered nisins
    • Dodd H.M., Horn N., Hao Z., and Gasson M.J. A lactococcal expression system for engineered nisins. Appl. Environ. Microbiol. 58 11 (1992) 3683-3693
    • (1992) Appl. Environ. Microbiol. , vol.58 , Issue.11 , pp. 3683-3693
    • Dodd, H.M.1    Horn, N.2    Hao, Z.3    Gasson, M.J.4
  • 18
    • 34548498172 scopus 로고    scopus 로고
    • A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: Analysis of mutants producing reduced antibacterial activities
    • Field D., Collins B., Cotter H., and Ross R.P. A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: Analysis of mutants producing reduced antibacterial activities. J. Mol. Microbiol. Biotechnol. 13 (2007) 226-234
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 226-234
    • Field, D.1    Collins, B.2    Cotter, H.3    Ross, R.P.4
  • 19
    • 45149121558 scopus 로고    scopus 로고
    • The generation of nisin variants with enhanced activity against specific gram-positive pathogens
    • Field D., O'Connor P.M., Cotter P.D., Hill C., and Ross R.P. The generation of nisin variants with enhanced activity against specific gram-positive pathogens. Mol. Microbiol. 69 (2008) 218-230
    • (2008) Mol. Microbiol. , vol.69 , pp. 218-230
    • Field, D.1    O'Connor, P.M.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 20
    • 0022348417 scopus 로고
    • High copy number plasmid vectors for use in lactic streptococci
    • Gasson M.J., and Anderson P.H. High copy number plasmid vectors for use in lactic streptococci. FEMS Microbiol. Lett. 30 (1985) 193-196
    • (1985) FEMS Microbiol. Lett. , vol.30 , pp. 193-196
    • Gasson, M.J.1    Anderson, P.H.2
  • 21
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust B., Challis G.L., Fowler K., Kieser T., and Chater K.F. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. USA 100 4 (2003) 1541-1546
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.4 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 22
    • 25444499680 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin
    • Kluskens L.D., Kuipers A., Rink R., de Boef E., Fekken S., Driessen A.J., Kuipers O.P., and Moll G.N. Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin. Biochemistry 44 38 (2005) 12827-12834
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12827-12834
    • Kluskens, L.D.1    Kuipers, A.2    Rink, R.3    de Boef, E.4    Fekken, S.5    Driessen, A.J.6    Kuipers, O.P.7    Moll, G.N.8
  • 24
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers O.P., Beerthuyzen M.M., Siezen R.J., and de Vos W.M. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. Eur. J. Biochem. 216 (1993) 281-291
    • (1993) Eur. J. Biochem. , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    de Vos, W.M.4
  • 25
    • 0028858480 scopus 로고
    • Autoregulation of nisin biosynthesis in Lactococcus lactis by signal transduction
    • Kuipers O.P., Beerthuyzen M.M., de Ruyter P.G., Luesink E.J., and de Vos W.M. Autoregulation of nisin biosynthesis in Lactococcus lactis by signal transduction. J. Biol. Chem. 270 45 (1995) 27299-27304
    • (1995) J. Biol. Chem. , vol.270 , Issue.45 , pp. 27299-27304
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    de Ruyter, P.G.3    Luesink, E.J.4    de Vos, W.M.5
  • 26
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers A., de Boef E., Rink R., Fekken S., Kluskens L.D., Driessen A.J., Leenhouts K., Kuipers O.P., and Moll G.N. NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides. J. Biol. Chem. 279 21 (2004) 22176-22182
    • (2004) J. Biol. Chem. , vol.279 , Issue.21 , pp. 22176-22182
    • Kuipers, A.1    de Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.6    Leenhouts, K.7    Kuipers, O.P.8    Moll, G.N.9
  • 27
    • 55049131364 scopus 로고    scopus 로고
    • Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin
    • Kuipers A., Meijer-Wierenga J., Rink R., Kluskens L.D., and Moll G.N. Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin. Appl. Environ. Microbiol. 74 21 (2008) 6591-6597
    • (2008) Appl. Environ. Microbiol. , vol.74 , Issue.21 , pp. 6591-6597
    • Kuipers, A.1    Meijer-Wierenga, J.2    Rink, R.3    Kluskens, L.D.4    Moll, G.N.5
  • 28
    • 0029074409 scopus 로고
    • Oxidative decarboxylation of peptides catalyzed by flavoprotein EpiD. Determination of substrate specificity using peptide libraries and neutral loss mass spectrometry
    • Kupke T., Kempter C., Jung G., and Götz F. Oxidative decarboxylation of peptides catalyzed by flavoprotein EpiD. Determination of substrate specificity using peptide libraries and neutral loss mass spectrometry. J. Biol. Chem. 270 19 (1995) 11282-11289
    • (1995) J. Biol. Chem. , vol.270 , Issue.19 , pp. 11282-11289
    • Kupke, T.1    Kempter, C.2    Jung, G.3    Götz, F.4
  • 29
    • 0026491208 scopus 로고
    • Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis
    • Liu W., and Hansen N. Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis. J. Biol. Chem. 267 35 (1992) 25078-25085
    • (1992) J. Biol. Chem. , vol.267 , Issue.35 , pp. 25078-25085
    • Liu, W.1    Hansen, N.2
  • 30
    • 0026575735 scopus 로고
    • Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector
    • MacNeil D.J., Gewain K.M., Ruby C.L., Dezeny G., Gibbons P.H., and MacNeil T. Analysis of Streptomyces avermitilis genes required for avermectin biosynthesis utilizing a novel integration vector. Gene 111 1 (1992) 61-68
    • (1992) Gene , vol.111 , Issue.1 , pp. 61-68
    • MacNeil, D.J.1    Gewain, K.M.2    Ruby, C.L.3    Dezeny, G.4    Gibbons, P.H.5    MacNeil, T.6
  • 31
    • 0036178887 scopus 로고    scopus 로고
    • The flavoprotein MrsD catalyses the oxidative decarboxylation reaction involved in formation of the peptidoglycan synthesis inhibitor mersacidin
    • Majer F., Schmid D.G., Altena K., Bierbaum G., and Kupke T. The flavoprotein MrsD catalyses the oxidative decarboxylation reaction involved in formation of the peptidoglycan synthesis inhibitor mersacidin. J. Bacteriol. 184 5 (2002) 1234-1243
    • (2002) J. Bacteriol. , vol.184 , Issue.5 , pp. 1234-1243
    • Majer, F.1    Schmid, D.G.2    Altena, K.3    Bierbaum, G.4    Kupke, T.5
  • 32
    • 1542743956 scopus 로고    scopus 로고
    • Structural characterization of Lacticin 3147, a two-peptide lantibiotic with synergistic activity
    • Martin N.I., Spules T., Carpenter M.R., Cotter P.D., Hill C., Ross P., and Vederas J.J. Structural characterization of Lacticin 3147, a two-peptide lantibiotic with synergistic activity. Biochemistry 43 (2004) 3049-3056
    • (2004) Biochemistry , vol.43 , pp. 3049-3056
    • Martin, N.I.1    Spules, T.2    Carpenter, M.R.3    Cotter, P.D.4    Hill, C.5    Ross, P.6    Vederas, J.J.7
  • 33
    • 0028007156 scopus 로고
    • Sequence analysis of lantibiotics: Chemical derivatization procedures allow a fast access to complete edman degradation
    • Meyer H.E., Heber M., Eisermann B., Korte H., Metzger J.W., and Jung G. Sequence analysis of lantibiotics: Chemical derivatization procedures allow a fast access to complete edman degradation. Anal. Biochem. 223 (1994) 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
  • 34
    • 0029875689 scopus 로고    scopus 로고
    • Detection of modified amino acids in lantibiotic peptide Mutacin II by chemical derivatization and electrospray ionization-Mass spectroscopic analysis
    • Novák J., Kirk M., Caufield P.W., Barnes S., Morrison K., and Baker J. Detection of modified amino acids in lantibiotic peptide Mutacin II by chemical derivatization and electrospray ionization-Mass spectroscopic analysis. Anal. Biochem. 236 (1996) 358-360
    • (1996) Anal. Biochem. , vol.236 , pp. 358-360
    • Novák, J.1    Kirk, M.2    Caufield, P.W.3    Barnes, S.4    Morrison, K.5    Baker, J.6
  • 37
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • Pascalle G., de Ruyter G.A., Kuipers O.P., and de Vos W.M. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62 10 (1996) 3662-3667
    • (1996) Appl. Environ. Microbiol. , vol.62 , Issue.10 , pp. 3662-3667
    • Pascalle, G.1    de Ruyter, G.A.2    Kuipers, O.P.3    de Vos, W.M.4
  • 38
    • 20544436705 scopus 로고    scopus 로고
    • Lantibiotic structures as guidelines for the deign of peptides that can be modified by lantibiotic enzymes
    • Rink R., Kuipers A., de Boef E., Leenhouts K.J., Driessen A.J., Moll G.N., and Kuipers O.P. Lantibiotic structures as guidelines for the deign of peptides that can be modified by lantibiotic enzymes. Biochemistry 44 24 (2005) 8873-8882
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8873-8882
    • Rink, R.1    Kuipers, A.2    de Boef, E.3    Leenhouts, K.J.4    Driessen, A.J.5    Moll, G.N.6    Kuipers, O.P.7
  • 39
    • 36048994654 scopus 로고    scopus 로고
    • NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed non-lantibiotic peptides
    • Rink R., Kluskens L.D., Kuipers A., Driessen A.J., Kuipers O.P., and Moll G.N. NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed non-lantibiotic peptides. Biochemistry 46 45 (2007) 13179-13189
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13179-13189
    • Rink, R.1    Kluskens, L.D.2    Kuipers, A.3    Driessen, A.J.4    Kuipers, O.P.5    Moll, G.N.6
  • 40
    • 0033621484 scopus 로고    scopus 로고
    • Extensive post-translational modification, including serine to d-alanine conversion, in the two-component lantibiotic, lacticin 3147
    • Ryan M.P., Jack R.W., Josten M., Sahl H.G., Jung G., Ross R.P., and Hill C. Extensive post-translational modification, including serine to d-alanine conversion, in the two-component lantibiotic, lacticin 3147. J. Biol. Chem. 274 53 (1999) 37544-37550
    • (1999) J. Biol. Chem. , vol.274 , Issue.53 , pp. 37544-37550
    • Ryan, M.P.1    Jack, R.W.2    Josten, M.3    Sahl, H.G.4    Jung, G.5    Ross, R.P.6    Hill, C.7
  • 42
    • 0023992075 scopus 로고
    • Construction of a plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon D., and Chopin A. Construction of a plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70 (1988) 559-566
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 44
    • 0038155138 scopus 로고    scopus 로고
    • Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin
    • Szekat C., Jack R.W., Skutlarek D., Farber H., and Bierbaum G. Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin. Appl. Environ. Microbiol. 69 7 (2003) 3777-3783
    • (2003) Appl. Environ. Microbiol. , vol.69 , Issue.7 , pp. 3777-3783
    • Szekat, C.1    Jack, R.W.2    Skutlarek, D.3    Farber, H.4    Bierbaum, G.5
  • 46
    • 0031050298 scopus 로고    scopus 로고
    • A novel methodology for assignment of disulfide bond pairings in proteins
    • Wu J., and Watson J.T. A novel methodology for assignment of disulfide bond pairings in proteins. Protein Sci. 6 (1997) 391-398
    • (1997) Protein Sci. , vol.6 , pp. 391-398
    • Wu, J.1    Watson, J.T.2
  • 47
    • 0028955428 scopus 로고
    • The tetracyclic lantibiotic actagardine 1H-NMR and 13C-NMR assignments and revised primary structure
    • Zimmerman N., Metzger J.W., and Jung G. The tetracyclic lantibiotic actagardine 1H-NMR and 13C-NMR assignments and revised primary structure. Eur. J. Biochem. 228 3 (1995) 786-797
    • (1995) Eur. J. Biochem. , vol.228 , Issue.3 , pp. 786-797
    • Zimmerman, N.1    Metzger, J.W.2    Jung, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.