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Volumn 43, Issue 36, 2004, Pages 11567-11575

Assembly and stability of nisin-Lipid II pores

Author keywords

[No Author keywords available]

Indexed keywords

CELL-WALL SYNTHESIS; NISIN PORE FORMATIONS; PEPTIDE ANTIBIOTIC NISINS; PERMEABILIZATION;

EID: 4444277132     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049476b     Document Type: Article
Times cited : (229)

References (32)
  • 1
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • Sahl, H. G., Jack, R. W., and Bierbaum, G. (1995) Biosynthesis and biological activities of lantibiotics with unique post-translational 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
  • 2
    • 0034117808 scopus 로고    scopus 로고
    • Lantibiotics and microcins: Polypeptides with unusual chemical diversity
    • Jack, R. W., and Jung, G. (2000) Lantibiotics and microcins: Polypeptides with unusual chemical diversity, Curr. Opin. Chem. Biol. 4, 310-317.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 310-317
    • Jack, R.W.1    Jung, G.2
  • 3
    • 0030043503 scopus 로고    scopus 로고
    • Post-translational modifications of lantibiotics
    • Kupke, T., and Gotz, F. (1996) Post-translational modifications of lantibiotics, Antonie van Leeuwenhoek 69, 139-150.
    • (1996) Antonie van Leeuwenhoek , vol.69 , pp. 139-150
    • Kupke, T.1    Gotz, F.2
  • 4
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria
    • Sahl, H. G., and Bierbaum, G. (1998) Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria, Annu. Rev. Microbiol 52, 41-79.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 7
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin, and other lantibiotics
    • Brotz, H., Josten, M., Wiedemann, L, Schneider, U., Gotz, F., Bierbaum, G., and Sahl, H. G. (1998) Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin, and other lantibiotics, Mol. Microbiol. 30, 317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brotz, H.1    Josten, M.2    Wiedemann, L.3    Schneider, U.4    Gotz, F.5    Bierbaum, G.6    Sahl, H.G.7
  • 8
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic
    • Breukink, E., Wiedemann, I., van Kraaij, C., Kuipers, O. P., Sahl, H., and de Kruijff, B. (1999) Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic, Science 286, 2361-2364.
    • (1999) Science , vol.286 , pp. 2361-2364
    • Breukink, E.1    Wiedemann, I.2    Van Kraaij, C.3    Kuipers, O.P.4    Sahl, H.5    De Kruijff, B.6
  • 9
    • 0001786686 scopus 로고
    • (Hakenbeck, R., Ed.), Elsevier, Amsterdam, The Netherlands
    • van Heijenoort, J. (1994) in Bacterial Cell Wall (Hakenbeck, R., Ed.) pp 39-72, Elsevier, Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 39-72
    • Van Heijenoort, J.1
  • 10
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I., Breukink, E., van Kraaij, C., Kuipers, O. P., Bierbaum, G., de Kruijff, B., and Sahl, H. G. (2001) Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity, J. Biol. Chem. 276, 1772-1779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 11
    • 0037129973 scopus 로고    scopus 로고
    • Mapping the targeted membrane pore formation mechanism by solution NMR: The nisin Z and lipid II interaction in SDS micelles
    • Hsu, S. T., Breukink, E., de Kruijff, B., Kaptein, R., Bonvin, A. M., and van Nuland, N. A. (2002) Mapping the targeted membrane pore formation mechanism by solution NMR: The nisin Z and lipid II interaction in SDS micelles, Biochemistry 41, 7670-7676.
    • (2002) Biochemistry , vol.41 , pp. 7670-7676
    • Hsu, S.T.1    Breukink, E.2    De Kruijff, B.3    Kaptein, R.4    Bonvin, A.M.5    Van Nuland, N.A.6
  • 12
    • 0037044318 scopus 로고    scopus 로고
    • Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin
    • Van Heusden, H. E., De Kruijff, B., and Breukink, E. (2002) Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin, Biochemistry 41, 12171-12178.
    • (2002) Biochemistry , vol.41 , pp. 12171-12178
    • Van Heusden, H.E.1    De Kruijff, B.2    Breukink, E.3
  • 15
    • 0026496892 scopus 로고
    • Engineering dehydrated amino acid residues in the antimicrobial peptide nisin
    • Kuipers, O. P., Rollema, H. S., Yap, W. M., Boot, H. J., Siezen, R. J., and de Vos, W. M. (1992) Engineering dehydrated amino acid residues in the antimicrobial peptide nisin, J. Biol. Chem. 267, 24340-24346.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24340-24346
    • Kuipers, O.P.1    Rollema, H.S.2    Yap, W.M.3    Boot, H.J.4    Siezen, R.J.5    De Vos, W.M.6
  • 16
    • 0014779155 scopus 로고
    • Two-dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., Fkeischer, S., and Yamamoto, A. (1970) Two-dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots, Lipids 5, 494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 18
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume, and ability to maintain a membrane potential
    • Hope, M., Bally, M. B., Webb, G., and Cullis, P. R. (1985) Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume, and ability to maintain a membrane potential, Biochim. Biophys. Acta 812, 55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 19
    • 0003320620 scopus 로고    scopus 로고
    • (Lakowicz, J. R., Ed.), Kluwer Academic/Plenum Publishers, New York
    • Lakowicz, J. R. (1999) in Principles of Fluorescence Spectroscopy (Lakowicz, J. R., Ed.) pp 445-486, Kluwer Academic/Plenum Publishers, New York.
    • (1999) Principles of Fluorescence Spectroscopy , pp. 445-486
    • Lakowicz, J.R.1
  • 20
    • 0029618211 scopus 로고
    • Effective detergent/chlorophyll ratio and detergent concentration in the aqueous phase during solubilization of Phormidium laminosum membranes
    • Ochoa de Aida, J. A., Llama, M. J., and Serra, J. L. (1995) Effective detergent/chlorophyll ratio and detergent concentration in the aqueous phase during solubilization of Phormidium laminosum membranes, Biochim. Biophys. Acta 1240, 209-215.
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 209-215
    • Ochoa De Aida, J.A.1    Llama, M.J.2    Serra, J.L.3
  • 21
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. (1995) Circular dichroism, Methods Enzymol. 246, 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 22
    • 0034612303 scopus 로고    scopus 로고
    • Pyrene excimer fluorescence: A spatially sensitive probe to monitor lipid-induced helical rearrangement of apolipophorin III
    • Sahoo, D., Narayanaswami, V., Kay, C. M., and Ryan, R. O. (2000) Pyrene excimer fluorescence: A spatially sensitive probe to monitor lipid-induced helical rearrangement of apolipophorin III, Biochemistry 39, 6594-6601.
    • (2000) Biochemistry , vol.39 , pp. 6594-6601
    • Sahoo, D.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 23
    • 0029202621 scopus 로고
    • Pyrene excimer fluorescence as a probe of protein conformational change
    • Lehrer, S. S. (1995) Pyrene excimer fluorescence as a probe of protein conformational change, Subcell. Biochem. 24, 115-132.
    • (1995) Subcell. Biochem. , vol.24 , pp. 115-132
    • Lehrer, S.S.1
  • 24
    • 0033535984 scopus 로고    scopus 로고
    • Proximity between Glu 126 and Arg 144 in the lactose permease of Escherichia coli
    • Zhao, M., Zen, K. C., Hubbell, W. L., and Kaback, H. R. (1999) Proximity between Glu 126 and Arg 144 in the lactose permease of Escherichia coli, Biochemistry 38, 7407-7412.
    • (1999) Biochemistry , vol.38 , pp. 7407-7412
    • Zhao, M.1    Zen, K.C.2    Hubbell, W.L.3    Kaback, H.R.4
  • 25
    • 0034767060 scopus 로고    scopus 로고
    • Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin
    • Zhao, H., Mattila, J. P., Holopainen, J. M., and Kinnunen, P. K. (2001) Comparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin, Biophys. J. 81, 2979-2991.
    • (2001) Biophys. J. , vol.81 , pp. 2979-2991
    • Zhao, H.1    Mattila, J.P.2    Holopainen, J.M.3    Kinnunen, P.K.4
  • 26
    • 0030919291 scopus 로고    scopus 로고
    • Intramolecular pyrene excimer fluorescence: A probe of proximity and protein conformational change
    • Lehrer, S. S. (1997) Intramolecular pyrene excimer fluorescence: A probe of proximity and protein conformational change, Methods Enzymol 278, 286-295.
    • (1997) Methods Enzymol. , vol.278 , pp. 286-295
    • Lehrer, S.S.1
  • 27
    • 0035807045 scopus 로고    scopus 로고
    • Membrane-spanning peptides induce phospholipid flop: A model for phospholipid translocation across the inner membrane of E. coli
    • Kol, M. A., de Kroon, A. L, Rijkers, D. T., Killian, J. A., and de Kruijff, B. (2001) Membrane-spanning peptides induce phospholipid flop: A model for phospholipid translocation across the inner membrane of E. coli, Biochemistry 40, 10500-10506.
    • (2001) Biochemistry , vol.40 , pp. 10500-10506
    • Kol, M.A.1    De Kroon, A.L.2    Rijkers, D.T.3    Killian, J.A.4    De Kruijff, B.5
  • 28
    • 0041589300 scopus 로고    scopus 로고
    • Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
    • Kol, M. A., van Dalen, A., de Kroon, A. I., and de Kruijff, B. (2003) Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane, J. Biol. Chem. 278, 24586-24593.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24586-24593
    • Kol, M.A.1    Van Dalen, A.2    De Kroon, A.I.3    De Kruijff, B.4
  • 29
    • 0032577918 scopus 로고    scopus 로고
    • Structural variations in nisin associated with different membrane mimicking and pH environments
    • Dykes, G. A., Hancock, R. E., and Hastings, J. W. (1998) Structural variations in nisin associated with different membrane mimicking and pH environments, Biochem. Biophys. Res. Commun. 247, 723-727.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 723-727
    • Dykes, G.A.1    Hancock, R.E.2    Hastings, J.W.3
  • 30
    • 2342498649 scopus 로고    scopus 로고
    • Lipid II-mediated pore formation by the peptide antibioitic nisin-A black lipid membrane study
    • in press
    • Wiedemann, I., Benz, R., and Sahl, H. (2004) Lipid II-mediated pore formation by the peptide antibioitic nisin-A black lipid membrane study, J. Bacteriol, in press.
    • (2004) J. Bacteriol.
    • Wiedemann, I.1    Benz, R.2    Sahl, H.3
  • 31
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • -Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1995) Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore, Biochemistry 34, 6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 32
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He, K., Ludtke, S. J., Huang, H. W., and Worcester, D. L. (1995) Antimicrobial peptide pores in membranes detected by neutron in-plane scattering, Biochemistry 34, 15614-15618.
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4


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