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Volumn 1668, Issue 1, 2005, Pages 87-98

Study of structure and orientation of mesentericin Y105, a bacteriocin from Gram-positive Leuconostoc mesenteroides, and its Trp-substituted analogues in phospholipid environments

Author keywords

Bacteriocin; Fluorescence; Lipid bound structure; Mesentericin; Peptide orientation; PMIRRAS

Indexed keywords

BACTERIOCIN; BUFFER; MESENTERICIN; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLSERINE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 12844270575     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.11.008     Document Type: Article
Times cited : (17)

References (48)
  • 2
    • 0029094242 scopus 로고
    • Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105
    • C. Fremeaux, Y. Héchard, and Y. Cenatiempo Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105 Microbiology 141 1995 1637 1645
    • (1995) Microbiology , vol.141 , pp. 1637-1645
    • Fremeaux, C.1    Héchard, Y.2    Cenatiempo, Y.3
  • 3
    • 0027080504 scopus 로고
    • Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconstoc mesenteroides
    • Y. Héchard, B. Dérijard, F. Letellier, and Y. Cenatiempo Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconstoc mesenteroides J. Gen. Microbiol. 138 1992 2725 2731
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2725-2731
    • Héchard, Y.1    Dérijard, B.2    Letellier, F.3    Cenatiempo, Y.4
  • 5
    • 0029891059 scopus 로고    scopus 로고
    • Covalent structure, synthesis and structure-function studies of Mesentericin Y105, a defensive peptide from gram-positive bacteria
    • Y. Fleury, M.A. Dayem, J.J. Montagne, E. Chamboiseau, J.P. Le Caer, P. Nicolas, and A. Delfour Covalent structure, synthesis and structure-function studies of Mesentericin Y105, a defensive peptide from gram-positive bacteria J. Biol. Chem. 271 1996 14421 14429
    • (1996) J. Biol. Chem. , vol.271 , pp. 14421-14429
    • Fleury, Y.1    Dayem, M.A.2    Montagne, J.J.3    Chamboiseau, E.4    Le Caer, J.P.5    Nicolas, P.6    Delfour, A.7
  • 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
    • Y. Chen, R.D. Ludescher, and T.J. Montville 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 1997 4770 4777
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4770-4777
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 7
    • 0031717018 scopus 로고    scopus 로고
    • Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles
    • Y. Chen, R.D. Ludescher, and T.J. Montville Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles Appl. Environ. Microbiol. 64 1998 3530 3532
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3530-3532
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 8
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of Leucocin a in TFE and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • N.L. Fregeau-Gallacher, M. Sailer, W.P. Niemczura, T.T. Nakashima, M.E. Stiles, and J.C. Verderas Three-dimensional structure of Leucocin A in TFE and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria Biochemistry 36 1997 15062 15072
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau-Gallacher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Verderas, J.C.6
  • 9
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of Carnobactericin B2 and its implication for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria
    • Y. Wang, M.E. Henz, N.L. Fregeau-Gallacher, S. Chai, A.C. Gibbs, L.Z. Yan, M.E. Stiles, D.S. Wishart, and J.C. Vederas Solution structure of Carnobactericin B2 and its implication for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria Biochemistry 38 1999 15438 15447
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.1    Henz, M.E.2    Fregeau-Gallacher, N.L.3    Chai, S.4    Gibbs, A.C.5    Yan, L.Z.6    Stiles, M.E.7    Wishart, D.S.8    Vederas, J.C.9
  • 10
    • 0035316822 scopus 로고    scopus 로고
    • Biological activities and structural properties of the atypical bacteriocins mesenterocin 52B and leucocin B-TA-33a
    • C. Corbier, F. Krier, G. Mulliert, B. Vitoux, and A.M. Revol-Junelles Biological activities and structural properties of the atypical bacteriocins mesenterocin 52B and leucocin B-TA-33a Appl. Environ. Microbiol. 67 2001 1418 1422
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1418-1422
    • Corbier, C.1    Krier, F.2    Mulliert, G.3    Vitoux, B.4    Revol-Junelles, A.M.5
  • 11
    • 0028829183 scopus 로고
    • Peptides as weapons against microorganisms in the chemical defense system of vertebrates
    • P. Nicolas, and A. Mor Peptides as weapons against microorganisms in the chemical defense system of vertebrates Annu. Rev. Microbiol. 49 1995 277 304
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 277-304
    • Nicolas, P.1    Mor, A.2
  • 12
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR
    • B. Bechinger The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR Biochim. Biophys. Acta 1462 1999 157 183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 13
    • 0032693639 scopus 로고    scopus 로고
    • Why and how peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462 1999 1 10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 14
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of binding, insertion and destabilization of phospholipid bilayer membranes by antibacterial and cell non-selective membrane lytic peptides
    • Y. Shai Mechanism of binding, insertion and destabilization of phospholipid bilayer membranes by antibacterial and cell non-selective membrane lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 16
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • G.B. Fields, and R.L. Noble Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids Int. J. Pept. Protein Res. 35 1990 161 214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 17
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • D.S. King, C.G. Fields, and G.B. Fields A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis Int. J. Pept. Protein Res. 36 1990 255 266
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 18
    • 12844281592 scopus 로고
    • Thèse Université Bordeaux I
    • E. Thiaudière, Thèse Université Bordeaux I (1990).
    • (1990)
    • Thiaudière, E.1
  • 19
    • 0342601541 scopus 로고    scopus 로고
    • Structural characterisation of the natural membrane bound state of melittin: A fluorescence study of a dansylated analogue
    • E. Perez-Paya, J. Dufourcq, L. Braco, and C. Abad Structural characterisation of the natural membrane bound state of melittin: a fluorescence study of a dansylated analogue Biochim. Biophys. Acta 1323 1997 223 236
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 223-236
    • Perez-Paya, E.1    Dufourcq, J.2    Braco, L.3    Abad, C.4
  • 20
    • 0023456819 scopus 로고
    • Myotoxin a-phospholipid interactions, an attempt by intrinsic fluorescence to define a possible mode of action for the toxin on membranes
    • J. Dufourcq, F. Dousseau, J.F. Faucon, and A.T. Tu Myotoxin a-phospholipid interactions, an attempt by intrinsic fluorescence to define a possible mode of action for the toxin on membranes Appl. Spectrosc. 41 1987 1410 1417
    • (1987) Appl. Spectrosc. , vol.41 , pp. 1410-1417
    • Dufourcq, J.1    Dousseau, F.2    Faucon, J.F.3    Tu, A.T.4
  • 21
    • 0021671706 scopus 로고
    • Role of peptide structure in lipid-peptide interactions: A fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles
    • W.K. Surewicz, and R.M. Epand Role of peptide structure in lipid-peptide interactions: a fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles Biochemistry 23 1984 6072 6077
    • (1984) Biochemistry , vol.23 , pp. 6072-6077
    • Surewicz, W.K.1    Epand, R.M.2
  • 24
    • 0004110727 scopus 로고
    • Peptide-membrane interactions: A fluorescence study of the binding of di- and tri-peptide containing Lys and Tyr or Trp residues to phospholipid vesicles
    • J. Dufourcq, J.F. Faucon, R. Maget-Dana, M.P. Pileni, and C. Helene Peptide-membrane interactions: a fluorescence study of the binding of di- and tri-peptide containing Lys and Tyr or Trp residues to phospholipid vesicles Biochim. Biophys. Acta 649 1981 67 76
    • (1981) Biochim. Biophys. Acta , vol.649 , pp. 67-76
    • Dufourcq, J.1    Faucon, J.F.2    Maget-Dana, R.3    Pileni, M.P.4    Helene, C.5
  • 25
    • 0019497821 scopus 로고
    • Design, synthesis, and characterization of a cytotoxic peptide with melittin-like activity
    • W.F. De Grado, F.J. Kézdy, and E.T. Kaiser Design, synthesis, and characterization of a cytotoxic peptide with melittin-like activity J. Am. Chem. Soc. 103 1981 679 681
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 679-681
    • De Grado, W.F.1    Kézdy, F.J.2    Kaiser, E.T.3
  • 27
    • 0342601541 scopus 로고    scopus 로고
    • Structural characterization of the natural membrane-bound state of melittin: A fluorescence study of a dansylated analogue
    • E. Perez-Paya, J. Dufourcq, L. Braco, and C. Abad Structural characterization of the natural membrane-bound state of melittin: a fluorescence study of a dansylated analogue Biochim. Biophys. Acta 1329 1997 223 236
    • (1997) Biochim. Biophys. Acta , vol.1329 , pp. 223-236
    • Perez-Paya, E.1    Dufourcq, J.2    Braco, L.3    Abad, C.4
  • 28
    • 0025977855 scopus 로고
    • Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers
    • K. Matsuzaki, M. Harada, S. Funakoshi, N. Fujii, and K. Miyajima Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers Biochim. Biophys. Acta 1063 1991 162 170
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 162-170
    • Matsuzaki, K.1    Harada, M.2    Funakoshi, S.3    Fujii, N.4    Miyajima, K.5
  • 32
    • 0026731378 scopus 로고
    • Does Fourier-transform infrared spectroscopy provide useful information on protein structure?
    • P.I. Haris, and D. Chapman Does Fourier-transform infrared spectroscopy provide useful information on protein structure? TIBS 17 1992 328 333
    • (1992) TIBS , vol.17 , pp. 328-333
    • Haris, P.I.1    Chapman, D.2
  • 33
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • W.K. Surewicz, H.H. Mantsch, and D. Chapman Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment Biochemistry 32 1993 389 394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 34
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy: Assignments and model compounds
    • H.J. Hilderson G.B. Ralston Plenum Press New York
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy: assignments and model compounds H.J. Hilderson G.B. Ralston Subcellular Biochemistry: Physicochemical Methods in the Study of Biomembranes 1994 Plenum Press New York 329 362
    • (1994) Subcellular Biochemistry: Physicochemical Methods in the Study of Biomembranes , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 35
    • 0030048902 scopus 로고    scopus 로고
    • In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air/water interface
    • I. Cornut, B. Desbat, J.M. Turlet, and J. Dufourcq In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air/water interface Biophys. J. 70 1996 305 312
    • (1996) Biophys. J. , vol.70 , pp. 305-312
    • Cornut, I.1    Desbat, B.2    Turlet, J.M.3    Dufourcq, J.4
  • 37
    • 0029909789 scopus 로고    scopus 로고
    • Purification and amino-acid sequences of piscicocins V1a and V1B, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity
    • P. Bhugaloo-Vial, X. Dousset, A. Metivier, O. Sorokine, P. Anglade, P. Boyaval, and D. Marion Purification and amino-acid sequences of piscicocins V1a and V1B, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity Appl. Environ. Microbiol. 62 1996 4410 4416
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4410-4416
    • Bhugaloo-Vial, P.1    Dousset, X.2    Metivier, A.3    Sorokine, O.4    Anglade, P.5    Boyaval, P.6    Marion, D.7
  • 38
  • 40
    • 0018100287 scopus 로고
    • Specific binding of a cardiotoxin from Naja mossambica mossambica to charged phopholipids detected by intrinsic fluorescence
    • J. Dufourcq, and J.F. Faucon Specific binding of a cardiotoxin from Naja mossambica mossambica to charged phopholipids detected by intrinsic fluorescence Biochemistry 17 1978 1770 1776
    • (1978) Biochemistry , vol.17 , pp. 1770-1776
    • Dufourcq, J.1    Faucon, J.F.2
  • 42
    • 0019316475 scopus 로고
    • A NMR study of the ionization of fatty acids, fatty amines and N-acylamino acids incorporated in phosphatidylcholine vesicles
    • M. Ptak, M. Egret-Charlier, A. Sanson, and O. Bouloussa A NMR study of the ionization of fatty acids, fatty amines and N-acylamino acids incorporated in phosphatidylcholine vesicles Biochim. Biophys. Acta 600 1980 387 397
    • (1980) Biochim. Biophys. Acta , vol.600 , pp. 387-397
    • Ptak, M.1    Egret-Charlier, M.2    Sanson, A.3    Bouloussa, O.4
  • 43
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of α helix
    • D. Eisenberg, R.M. Weiss, and T.C. Terwilliger The helical hydrophobic moment: a measure of the amphiphilicity of α helix Nature 299 1982 371 374
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 44
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determinating the energetics of peptide-bilayers interactions
    • S.H. White, W.C. Wimley, A.S. Ladokhin, and K. Hristova Protein folding in membranes: determinating the energetics of peptide-bilayers interactions Methods Enzymol. 295B 1998 62 87
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 45
    • 0020584333 scopus 로고
    • Abolition of the thermotropic transition of charged phospholipids induced by a cardiotoxin from Naja mossambica mossambica as detected by fluorescence polarization, differential scanning calorimetry and Raman spectroscopy
    • J.F. Faucon, J. Dufourcq, E. Bernard, L. Ducheneau, and M. Pézolet Abolition of the thermotropic transition of charged phospholipids induced by a cardiotoxin from Naja mossambica mossambica as detected by fluorescence polarization, differential scanning calorimetry and Raman spectroscopy Biochemistry 22 1983 2180 2185
    • (1983) Biochemistry , vol.22 , pp. 2180-2185
    • Faucon, J.F.1    Dufourcq, J.2    Bernard, E.3    Ducheneau, L.4    Pézolet, M.5
  • 46
    • 0020488236 scopus 로고
    • Phase separations induced by melittin in negatively charged phospholipid bilayers as detected by fluorescence polarization and differential scanning calorimetry
    • E. Bernard, J.F. Faucon, and J. Dufourcq Phase separations induced by melittin in negatively charged phospholipid bilayers as detected by fluorescence polarization and differential scanning calorimetry Biochim. Biophys. Acta 688 1982 152 162
    • (1982) Biochim. Biophys. Acta , vol.688 , pp. 152-162
    • Bernard, E.1    Faucon, J.F.2    Dufourcq, J.3
  • 47
    • 0026760920 scopus 로고
    • Glycine and beta-branched residues support and modulate peptide helicity in membrane environments
    • S.C. Li, and C.M. Deber Glycine and beta-branched residues support and modulate peptide helicity in membrane environments FEBS Lett. 311 1992 217 220
    • (1992) FEBS Lett. , vol.311 , pp. 217-220
    • Li, S.C.1    Deber, C.M.2
  • 48
    • 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
    • Y. Chen, R. Shapira, M. Eisenstein, and T. Montville 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 1997 524 531
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 524-531
    • Chen, Y.1    Shapira, R.2    Eisenstein, M.3    Montville, T.4


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