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Volumn 64, Issue 6, 1998, Pages 1997-2005

Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHIMERIC PROTEIN; DNA; MALTOSE BINDING PROTEIN; PEDIOCIN;

EID: 0031745937     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.6.1997-2005.1998     Document Type: Article
Times cited : (90)

References (36)
  • 1
    • 0021019879 scopus 로고
    • Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli
    • Amann, E., J. Brosius, and M. Ptashne. 1983. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli. Gene 25:167-178.
    • (1983) Gene , vol.25 , pp. 167-178
    • Amann, E.1    Brosius, J.2    Ptashne, M.3
  • 2
    • 0025960702 scopus 로고
    • Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial strains
    • Bhunia, A. K., M. C. Johnson, B. Ray, and N. Kalchayanand. 1991. Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial strains. J. Appl. Bacteriol. 70:25-30.
    • (1991) J. Appl. Bacteriol. , vol.70 , pp. 25-30
    • Bhunia, A.K.1    Johnson, M.C.2    Ray, B.3    Kalchayanand, N.4
  • 3
    • 0025752512 scopus 로고
    • Influence of growth conditions on the production of bacteriocin, pediocin AcH, by Pediococcus acidilactici H
    • Biswas, S. R., P. Ray, M. C. Johnson, and B. Ray. 1991. Influence of growth conditions on the production of bacteriocin, pediocin AcH, by Pediococcus acidilactici H. Appl. Environ. Microbiol. 57:1265-1267.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1265-1267
    • Biswas, S.R.1    Ray, P.2    Johnson, M.C.3    Ray, B.4
  • 4
    • 0028037952 scopus 로고
    • Analysis of the pediocin AcH gene cluster from plasmid pSMB74 and its expression in a pediocin-negative Pediococcus acidilactici strain
    • Bukhtiyarova, M., R. Yang, and B. Ray. 1994. Analysis of the pediocin AcH gene cluster from plasmid pSMB74 and its expression in a pediocin-negative Pediococcus acidilactici strain. Appl. Environ. Microbiol. 60:3405-3408.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3405-3408
    • Bukhtiyarova, M.1    Yang, R.2    Ray, B.3
  • 5
    • 0030999249 scopus 로고    scopus 로고
    • Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure
    • Chen, Y., R. Shapira, M. Eisenstein, and T. J. Montville. 1997. Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure. Appl. Environ. Microbiol. 63:524-531.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 524-531
    • Chen, Y.1    Shapira, R.2    Eisenstein, M.3    Montville, T.J.4
  • 6
    • 0030833912 scopus 로고    scopus 로고
    • Electrostatic interactions, but not the YGNGV consensus motif, govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles
    • Chen, Y., R. D. Ludescher, and T. J. Montville. 1997. Electrostatic interactions, but not the YGNGV consensus motif, govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles. Appl. Environ. Microbiol. 63:4770-4777.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4770-4777
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 8
    • 0028229579 scopus 로고
    • Folding pattern diversity of integral membrane proteins
    • Cowan, S. W., and J. P. Rosenbusch. 1994. Folding pattern diversity of integral membrane proteins. Science 264:914-916.
    • (1994) Science , vol.264 , pp. 914-916
    • Cowan, S.W.1    Rosenbusch, J.P.2
  • 9
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., E. Schwarz, M. Komaroray, and R. Wall. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaroray, M.3    Wall, R.4
  • 10
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman, D. M., and T. A. Steitz. 1981. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23:79-88.
    • (1981) Cell , vol.23 , pp. 79-88
    • Engelman, D.M.1    Steitz, T.A.2
  • 11
    • 0027132575 scopus 로고
    • ABC-transporters: Bacterial exporters
    • Fath, M. J., and R. Kolter. 1993. ABC-transporters: bacterial exporters. Microbiol. Rev. 57:995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 12
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland, G., O. R. Blingsmo, K. Sletten, G. Jung, I. F. Nes, and J. Nissen-Meyer. 1996. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: the C-terminal region is important for determining specificity. Appl. Environ. Microbiol. 62:3313-3318.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 13
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings, J. W., M. Sailer, K. Johnson, K. L. Roy, J. C. Vederas, and M. E. Stiles. 1991. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173:7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 14
    • 0026724915 scopus 로고
    • Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0
    • Henderson, J. T., A. L. Chopko, and P. D. van Wassenaar. 1992. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys. 295:5-12.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 5-12
    • Henderson, J.T.1    Chopko, A.L.2    Van Wassenaar, P.D.3
  • 15
    • 0001823786 scopus 로고
    • Recombinant PCR
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), Academic Press, Inc., San Diego, Calif.
    • Higuchi, R. 1990. Recombinant PCR, p. 177-183. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), PCR protocols. A guide to methods and applications. Academic Press, Inc., San Diego, Calif.
    • (1990) PCR Protocols. A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 16
    • 0027077825 scopus 로고
    • Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake LB706
    • Holck, A., L. Axelsson, S.-E. Birkeland, T. Aukrust, and H. Bloom. 1992. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake LB706. J. Gen. Microbiol. 138:2715-2720.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2715-2720
    • Holck, A.1    Axelsson, L.2    Birkeland, S.-E.3    Aukrust, T.4    Bloom, H.5
  • 17
    • 0028140093 scopus 로고
    • Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sake LB674
    • Holck, A., L. Axelsson, K. Huhne, and L. Krockel. 1994. Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sake LB674. FEMS Microbiol. Lett. 115:143-150.
    • (1994) FEMS Microbiol. Lett. , vol.115 , pp. 143-150
    • Holck, A.1    Axelsson, L.2    Huhne, K.3    Krockel, L.4
  • 18
    • 0028566270 scopus 로고
    • A revised set of potentials for β-turn formation in proteins
    • Hutchinson, E. G., and J. M. Thornton. 1994. A revised set of potentials for β-turn formation in proteins. Protein Sci. 3:2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 19
    • 0028990155 scopus 로고
    • Bacteriocins of gram-positive bacteria
    • Jack, R. W., J. R. Tagg, and B. Ray. 1995. Bacteriocins of gram-positive bacteria. Microbiol. Rev. 59:171-200.
    • (1995) Microbiol. Rev. , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 20
    • 0021352840 scopus 로고
    • Amphiphilic secondary structure: Design of peptide hormones
    • Kaiser, E. T., and F. J. Kezdy. 1984. Amphiphilic secondary structure: design of peptide hormones. Science 223:249-255.
    • (1984) Science , vol.223 , pp. 249-255
    • Kaiser, E.T.1    Kezdy, F.J.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D. W., E. Chen, and D. V. Goeddel. 1989. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1:11-15.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 23
    • 0030956720 scopus 로고    scopus 로고
    • Anionic phospholipids modulate peptide insertion into membranes
    • Liu, L.-P., and C. M. Deber. 1997. Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36:5476-5482.
    • (1997) Biochemistry , vol.36 , pp. 5476-5482
    • Liu, L.-P.1    Deber, C.M.2
  • 25
    • 0031985197 scopus 로고    scopus 로고
    • Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon
    • Miller, K. W., R. Schamber, Y. Chen, and B. Ray. 1998. Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon. Appl. Environ. Microbiol. 64:14-20.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 14-20
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 26
    • 0028339135 scopus 로고
    • Complete nucleotide sequence of pSMB74, a plasmid encoding the production of pediocin AcH in Pediococcus acidilactici
    • Motlagh, A. M., M. Bukhtiyarova, and B. Ray. 1994. Complete nucleotide sequence of pSMB74, a plasmid encoding the production of pediocin AcH in Pediococcus acidilactici. Lett. Appl. Microbiol. 18:305-312.
    • (1994) Lett. Appl. Microbiol. , vol.18 , pp. 305-312
    • Motlagh, A.M.1    Bukhtiyarova, M.2    Ray, B.3
  • 27
    • 0008685484 scopus 로고    scopus 로고
    • Characteristics and application of pediocin(s) of Pediococcus acidilactici: Pediocin PA-1/AcH
    • T. F. Bozoglu and B. Ray (ed.), Springer, New York, N.Y.
    • Ray, B. 1996. Characteristics and application of pediocin(s) of Pediococcus acidilactici: pediocin PA-1/AcH, p. 155-203. In T. F. Bozoglu and B. Ray (ed.), Lactic acid bacteria: current advances in metabolism, genetics, and applications. Springer, New York, N.Y.
    • (1996) Lactic Acid Bacteria: Current Advances in Metabolism, Genetics, and Applications , pp. 155-203
    • Ray, B.1
  • 28
    • 0027339076 scopus 로고
    • 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin a from Leuconostoc gelidum and nisin A from Lactococcus lactis
    • 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis. Biochemistry 32:310-318.
    • (1993) Biochemistry , vol.32 , pp. 310-318
    • Sailer, M.1    Helms, G.L.2    Henkel, T.3    Niemczura, W.P.4    Stiles, M.E.5    Vederas, J.C.6
  • 30
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
    • Taylor, J. W., J. Ott, and F. Eckstein. 1985. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Res. 13:8765-8785.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8765-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 31
    • 0027326620 scopus 로고
    • Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174
    • Tichaczek, P. S., R. F. Vogel, and W. P. Hammes. 1993. Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174. Arch. Microbiol. 160:279-283.
    • (1993) Arch. Microbiol. , vol.160 , pp. 279-283
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.P.3
  • 32
    • 0028344604 scopus 로고
    • Cloning and sequencing sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH673
    • Tichaczek, P. S., R. F. Vogel, and W. Hammes. 1994. Cloning and sequencing sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH673. Microbiology 140:361-367.
    • (1994) Microbiology , vol.140 , pp. 361-367
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.3
  • 33
    • 0029074843 scopus 로고
    • Functional analysis of the pediocin operon of Pediococcus acidilactici PAC 1.0: PedB is the immunity protein and PedD is the precursor processing enzyme
    • Venema, K., J. Kok, J. D. Marugg, M. Y. Toonen, A. M. Ledeboer, G. Venema, and M. L. Chikindas. 1995. Functional analysis of the pediocin operon of Pediococcus acidilactici PAC 1.0: PedB is the immunity protein and PedD is the precursor processing enzyme. Mol. Microbiol. 17:515-522.
    • (1995) Mol. Microbiol. , vol.17 , pp. 515-522
    • Venema, K.1    Kok, J.2    Marugg, J.D.3    Toonen, M.Y.4    Ledeboer, A.M.5    Venema, G.6    Chikindas, M.L.7
  • 34
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht, T., M. Dathe, M. Beyermann, E. Krause, W. L. Maloy, D. L. MacDonald, and M. Bienert. 1997. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 36:6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 35
    • 0026800644 scopus 로고
    • Novel method to extract large amounts of bacteriocins from lactic acid bacteria
    • Yang, R., M. C. Johnson, and B. Ray. 1992. Novel method to extract large amounts of bacteriocins from lactic acid bacteria. Appl. Environ. Microbiol. 58:3355-3359.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3355-3359
    • Yang, R.1    Johnson, M.C.2    Ray, B.3
  • 36
    • 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 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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