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Volumn 158, Issue 12, 2012, Pages 2927-2935

Identification of the genes involved in the secretion and self-immunity of lacticin Q, an unmodified leaderless bacteriocin from Lactococcus lactis QU 5

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BACTERIOCIN; LACTICIN Q; LACTICIN Z; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84870320132     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.062943-0     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 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., Koga, H., Okuda, K., Kanemasa, Y., Sashihara, T., Nakayama, J. & Sonomoto, K. (2004). 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, 429-436.
    • (2004) J Biosci Bioeng , vol.98 , pp. 429-436
    • Aso, Y.1    Nagao, J.2    Koga, H.3    Okuda, K.4    Kanemasa, Y.5    Sashihara, T.6    Nakayama, J.7    Sonomoto, K.8
  • 2
    • 64749101378 scopus 로고    scopus 로고
    • Development of bacteriocinogenic strains of Saccharomyces cerevisiae heterologously expressing and secreting the leaderless enterocin L50 peptides L50A and L50B from Enterococcus faecium L50
    • Basanta, A., Herranz, C., Gutiérrez, J., Criado, R., Hernández, P. E. & Cintas, L. M. (2009). Development of bacteriocinogenic strains of Saccharomyces cerevisiae heterologously expressing and secreting the leaderless enterocin L50 peptides L50A and L50B from Enterococcus faecium L50. Appl Environ Microbiol 75, 2382-2392.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2382-2392
    • Basanta, A.1    Herranz, C.2    Gutiérrez, J.3    Criado, R.4    Hernández, P.E.5    Cintas, L.M.6
  • 3
    • 77952279826 scopus 로고    scopus 로고
    • Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50
    • Basanta, A., Gómez-Sala, B., Sánchez, J., Diep, D. B., Herranz, C., Hernández, P. E. & Cintas, L. M. (2010). Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50. Appl Environ Microbiol 76, 3314-3324.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3314-3324
    • Basanta, A.1    Gómez-Sala, B.2    Sánchez, J.3    Diep, D.B.4    Herranz, C.5    Hernández, P.E.6    Cintas, L.M.7
  • 4
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C., Paul, M., Xie, L. & van der Donk, W. A. (2005). Biosynthesis and mode of action of lantibiotics. Chem Rev 105, 633-684.
    • (2005) Chem Rev , vol.105 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    van der Donk, W.A.4
  • 5
    • 0031922351 scopus 로고    scopus 로고
    • Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins
    • Cintas, L. M., Casaus, P., Holo, H., Hernandez, P. E., Nes, I. F. & Håvarstein, L. S. (1998). Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins. J Bacteriol 180, 1988-1994.
    • (1998) J Bacteriol , vol.180 , pp. 1988-1994
    • Cintas, L.M.1    Casaus, P.2    Holo, H.3    Hernandez, P.E.4    Nes, I.F.5    Håvarstein, L.S.6
  • 6
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D., Hill, C. & Ross, R. P. (2005). Bacteriocins: developing innate immunity for food. Nat Rev Microbiol 3, 777-788.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 7
    • 33750071105 scopus 로고    scopus 로고
    • Complete sequence of the enterocin Qencoding plasmid pCIZ2 from the multiple bacteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity
    • Criado, R., Diep, D. B., Aakra, A., Gutiérrez, J., Nes, I. F., Hernández, P. E. & Cintas, L. M. (2006). Complete sequence of the enterocin Qencoding plasmid pCIZ2 from the multiple bacteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity. Appl Environ Microbiol 72, 6653-6666.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6653-6666
    • Criado, R.1    Diep, D.B.2    Aakra, A.3    Gutiérrez, J.4    Nes, I.F.5    Hernández, P.E.6    Cintas, L.M.7
  • 8
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter, P. G., Kuipers, O. P. & de Vos, W. M. (1996). Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol 62, 3662-3667.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • de Ruyter, P.G.1    Kuipers, O.P.2    de Vos, W.M.3
  • 9
    • 0035829346 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for production of enterocins A and B by Enterococcus faecium WHE 81
    • Ennahar, S., Asou, Y., Zendo, T., Sonomoto, K. & Ishizaki, A. (2001). Biochemical and genetic evidence for production of enterocins A and B by Enterococcus faecium WHE 81. Int J Food Microbiol 70, 291-301.
    • (2001) Int J Food Microbiol , vol.70 , pp. 291-301
    • Ennahar, S.1    Asou, Y.2    Zendo, T.3    Sonomoto, K.4    Ishizaki, A.5
  • 10
    • 0031767745 scopus 로고    scopus 로고
    • Purification and genetic characterization of enterocin I from Enterococcus faecium 6T1a, a novel antilisterial plasmid-encoded bacteriocin which does not belong to the pediocin family of bacteriocins
    • Floriano, B., Ruiz-Barba, J. L. & Jiménez-Díaz, R. (1998). Purification and genetic characterization of enterocin I from Enterococcus faecium 6T1a, a novel antilisterial plasmid-encoded bacteriocin which does not belong to the pediocin family of bacteriocins. Appl Environ Microbiol 64, 4883-4890.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4883-4890
    • Floriano, B.1    Ruiz-Barba, J.L.2    Jiménez-Díaz, R.3
  • 11
    • 34248172307 scopus 로고    scopus 로고
    • Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of Gram-positive bacteria
    • Fujita, K., Ichimasa, S., Zendo, T., Koga, S., Yoneyama, F., Nakayama, J. & Sonomoto, K. (2007). Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of Gram-positive bacteria. Appl Environ Microbiol 73, 2871-2877.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2871-2877
    • Fujita, K.1    Ichimasa, S.2    Zendo, T.3    Koga, S.4    Yoneyama, F.5    Nakayama, J.6    Sonomoto, K.7
  • 12
    • 0141557576 scopus 로고    scopus 로고
    • Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins
    • Gajic, O., Buist, G., Kojic, M., Topisirovic, L., Kuipers, O. P. & Kok, J. (2003). Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. J Biol Chem 278, 34291-34298.
    • (2003) J Biol Chem , vol.278 , pp. 34291-34298
    • Gajic, O.1    Buist, G.2    Kojic, M.3    Topisirovic, L.4    Kuipers, O.P.5    Kok, J.6
  • 13
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by electroporation
    • Holo, H. & Nes, I. F. (1995). Transformation of Lactococcus by electroporation. Methods Mol Biol 47, 195-199.
    • (1995) Methods Mol Biol , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 14
    • 27444437741 scopus 로고    scopus 로고
    • Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin
    • Hyink, O., Balakrishnan, M. & Tagg, J. R. (2005). Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin. FEMS Microbiol Lett 252, 235-241.
    • (2005) FEMS Microbiol Lett , vol.252 , pp. 235-241
    • Hyink, O.1    Balakrishnan, M.2    Tagg, J.R.3
  • 15
    • 36148934877 scopus 로고    scopus 로고
    • Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14
    • Iwatani, S., Zendo, T., Yoneyama, F., Nakayama, J. & Sonomoto, K. (2007). Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14. Biosci Biotechnol Biochem 71, 1984-1992.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 1984-1992
    • Iwatani, S.1    Zendo, T.2    Yoneyama, F.3    Nakayama, J.4    Sonomoto, K.5
  • 16
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer, T. R. (1993). Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol Rev 12, 39-85.
    • (1993) FEMS Microbiol Rev , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 19
    • 24644468692 scopus 로고    scopus 로고
    • Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli
    • Nagao, J., Harada, Y., Shioya, K., Aso, Y., Zendo, T., Nakayama, J. & Sonomoto, K. (2005). Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli. Biochem Biophys Res Commun 336, 507-513.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 507-513
    • Nagao, J.1    Harada, Y.2    Shioya, K.3    Aso, Y.4    Zendo, T.5    Nakayama, J.6    Sonomoto, K.7
  • 20
    • 84857089795 scopus 로고    scopus 로고
    • Genes involved in immunity to and secretion of aureocin A53, an atypical class II bacteriocin produced by Staphylococcus aureus A53
    • Nascimento, J. dos S., Coelho, M. L., Ceotto, H., Potter, A., Fleming, L. R., Salehian, Z., Nes, I. F. & Bastos, M. C. (2012). Genes involved in immunity to and secretion of aureocin A53, an atypical class II bacteriocin produced by Staphylococcus aureus A53. J Bacteriol 194, 875-883.
    • (2012) J Bacteriol , vol.194 , pp. 875-883
    • dos Nascimento, J.S.1    Coelho, M.L.2    Ceotto, H.3    Potter, A.4    Fleming, L.R.5    Salehian, Z.6    Nes, I.F.7    Bastos, M.C.8
  • 23
    • 0036301056 scopus 로고    scopus 로고
    • Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus
    • Netz, D. J., Pohl, R., Beck-Sickinger, A. G., Selmer, T., Pierik, A. J., Bastos, M. C. & Sahl, H. G. (2002). Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus. J Mol Biol 319, 745-756.
    • (2002) J Mol Biol , vol.319 , pp. 745-756
    • Netz, D.J.1    Pohl, R.2    Beck-Sickinger, A.G.3    Selmer, T.4    Pierik, A.J.5    Bastos, M.C.6    Sahl, H.G.7
  • 24
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., Gerber, A. S. & Hartl, D. L. (1988). Genetic applications of an inverse polymerase chain reaction. Genetics 120, 621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 27
    • 84857175322 scopus 로고    scopus 로고
    • Identification, characterization, and recombinant expression of epidermicin NI01, a novel unmodified bacteriocin produced by Staphylococcus epidermidis that displays potent activity against staphylococci
    • Sandiford, S. & Upton, M. (2012). Identification, characterization, and recombinant expression of epidermicin NI01, a novel unmodified bacteriocin produced by Staphylococcus epidermidis that displays potent activity against staphylococci. Antimicrob Agents Chemother 56, 1539-1547.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 1539-1547
    • Sandiford, S.1    Upton, M.2
  • 28
    • 77950628779 scopus 로고    scopus 로고
    • Characterization of modification enzyme NukM and engineering of a novel thioether bridge in lantibiotic nukacin ISK-1
    • Shioya, K., Harada, Y., Nagao, J., Nakayama, J. & Sonomoto, K. (2010). Characterization of modification enzyme NukM and engineering of a novel thioether bridge in lantibiotic nukacin ISK-1. Appl Microbiol Biotechnol 86, 891-899.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 891-899
    • Shioya, K.1    Harada, Y.2    Nagao, J.3    Nakayama, J.4    Sonomoto, K.5
  • 29
    • 0024493090 scopus 로고
    • Construction of a lactococcal expression vector: Expression of hen egg white lysozyme in Lactococcus lactis subsp. lactis
    • van de Guchte, M., van der Vossen, J. M., Kok, J. & Venema, G. (1989). Construction of a lactococcal expression vector: expression of hen egg white lysozyme in Lactococcus lactis subsp. lactis. Appl Environ Microbiol 55, 224-228.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 224-228
    • van de Guchte, M.1    van der Vossen, J.M.2    Kok, J.3    Venema, G.4
  • 30
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. (1982). Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 31
    • 0142136196 scopus 로고    scopus 로고
    • Purification and characterization of a novel bacteriocin produced by Enterococcus faecalis strain RJ-11
    • Yamamoto, Y., Togawa, Y., Shimosaka, M. & Okazaki, M. (2003). Purification and characterization of a novel bacteriocin produced by Enterococcus faecalis strain RJ-11. Appl Environ Microbiol 69, 5746-5753.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5746-5753
    • Yamamoto, Y.1    Togawa, Y.2    Shimosaka, M.3    Okazaki, M.4
  • 33
    • 67749135638 scopus 로고    scopus 로고
    • Peptide-lipid huge toroidal pore, a new antimicrobial mechanism mediated by a lactococcal bacteriocin, lacticin Q
    • Yoneyama, F., Imura, Y., Ohno, K., Zendo, T., Nakayama, J., Matsuzaki, K. & Sonomoto, K. (2009b). Peptide-lipid huge toroidal pore, a new antimicrobial mechanism mediated by a lactococcal bacteriocin, lacticin Q. Antimicrob Agents Chemother 53, 3211-3217.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 3211-3217
    • Yoneyama, F.1    Imura, Y.2    Ohno, K.3    Zendo, T.4    Nakayama, J.5    Matsuzaki, K.6    Sonomoto, K.7
  • 34
    • 38349133640 scopus 로고    scopus 로고
    • Bacteriocin detection by liquid chromatography/mass spectrometry for rapid identification
    • Zendo, T., Nakayama, J., Fujita, K. & Sonomoto, K. (2008). Bacteriocin detection by liquid chromatography/mass spectrometry for rapid identification. J Appl Microbiol 104, 499-507.
    • (2008) J Appl Microbiol , vol.104 , pp. 499-507
    • Zendo, T.1    Nakayama, J.2    Fujita, K.3    Sonomoto, K.4


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