메뉴 건너뛰기




Volumn 78, Issue 5, 2000, Pages 2475-2485

The effect of peptide/lipid hydrophobic mismatch on the phase behavior of model membranes mimicking the lipid composition in Escherichia coli membranes

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DIOLEOYLPHOSPHATIDYLETHANOLAMINE; DIOLEOYLPHOSPHATIDYLGLYCEROL; LEUCINE; MEMBRANE PHOSPHOLIPID; MEMBRANE PROTEIN; TRYPTOPHAN;

EID: 0034108440     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76792-0     Document Type: Article
Times cited : (53)

References (48)
  • 1
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M. S., and S. Munro. 1993. Cholesterol and the Golgi apparatus Science. 261:1280-1288.
    • (1993) Science , vol.261 , pp. 1280-1288
    • Bretscher, M.S.1    Munro, S.2
  • 2
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. 3. Relationship between calcium adenosine triphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey, M., and G. W. Feigenson. 1981. Fluorescence quenching in model membranes. 3. Relationship between calcium adenosine triphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry. 20:1949-1961.
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 3
    • 0028203898 scopus 로고
    • Effects of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase activity
    • Cornea, R. L., and D. D. Thomas. 1994. Effects of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase activity. Biochemistry. 33:2912-2920.
    • (1994) Biochemistry , vol.33 , pp. 2912-2920
    • Cornea, R.L.1    Thomas, D.D.2
  • 7
    • 0030823233 scopus 로고    scopus 로고
    • Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoylphosphatidylcholine lipid bilayers
    • Dumas, F., M. M. Sperotto, M.-C. Lebrun, J.-F. Tocanne, and O. G. Mouritsen. 1997. Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoylphosphatidylcholine lipid bilayers. Biophys. J. 73:1940-1953.
    • (1997) Biophys. J. , vol.73 , pp. 1940-1953
    • Dumas, F.1    Sperotto, M.M.2    Lebrun, M.-C.3    Tocanne, J.-F.4    Mouritsen, O.G.5
  • 8
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand, R. M. 1998. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta. 1376:353-368.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 9
    • 33845281853 scopus 로고
    • Physical properties of surfactant bilayer membranes: Thermal transitions, elasticity, rigidity, cohesion, and colloidal interactions
    • Evans, E., and D. Needham. 1987. Physical properties of surfactant bilayer membranes: thermal transitions, elasticity, rigidity, cohesion, and colloidal interactions. J. Phys. Chem. 91:4219-4228.
    • (1987) J. Phys. Chem. , vol.91 , pp. 4219-4228
    • Evans, E.1    Needham, D.2
  • 10
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S. M. 1985. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA. 82:3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 13
    • 0000616967 scopus 로고
    • Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy
    • Huschilt, J. C., R. S. Hodges, and J. H. Davis. 1985. Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy. Biochemistry. 24:1377-1386.
    • (1985) Biochemistry , vol.24 , pp. 1377-1386
    • Huschilt, J.C.1    Hodges, R.S.2    Davis, J.H.3
  • 14
    • 0002650761 scopus 로고    scopus 로고
    • Cytoplasmic membrane
    • F. C. Neidhart, editor. American Society of Microbiology Press, Washington, DC
    • Kadner, R. J. 1996. Cytoplasmic membrane. In Escherichia coli and Salmonella. Cellular and Molecular Biology. F. C. Neidhart, editor. American Society of Microbiology Press, Washington, DC. 58-87.
    • (1996) Escherichia Coli and Salmonella. Cellular and Molecular Biology , pp. 58-87
    • Kadner, R.J.1
  • 15
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 18
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian, J. A., I. Salemink, M. R. R. de Planque, G. Lindblom, R. E. Koeppe, II, and D. V. Greathouse. 1996. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 35:1037-1045.
    • (1996) Biochemistry , vol.35 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    De Planque, M.R.R.3    Lindblom, G.4    Koeppe II, R.E.5    Greathouse, D.V.6
  • 19
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membranes proteins
    • Landau, E. M., and J. P. Rosenbusch. 1996. Lipidic cubic phases: a novel concept for the crystallization of membranes proteins. Proc. Natl. Acad. Sci. USA. 93:14532-14535.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 20
    • 0029156582 scopus 로고
    • From entangled membranes to eclectic morphologies: Cubic membranes as subcellular space organizers
    • Landh, T. 1995. From entangled membranes to eclectic morphologies: cubic membranes as subcellular space organizers. FEBS Lett. 369:13-17.
    • (1995) FEBS Lett. , vol.369 , pp. 13-17
    • Landh, T.1
  • 21
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. F. Reithmeier. 1993. Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 229:602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.F.4
  • 22
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M. A., and D. M. Engelman. 1994. Specificity and promiscuity in membrane helix interactions. Q. Rev. Biophys. 27:157-218.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 23
    • 0002334276 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy and lipid phase behaviour and lipid diffusion
    • W. W. Christine, editor. Oily Press, Dundee, Scotland
    • Lindblom, G. 1996. Nuclear magnetic resonance spectroscopy and lipid phase behaviour and lipid diffusion. In Advances in Lipid Methology, Vol. 3. W. W. Christine, editor. Oily Press, Dundee, Scotland. 133-209.
    • (1996) Advances in Lipid Methology , vol.3 , pp. 133-209
    • Lindblom, G.1
  • 24
    • 0023052449 scopus 로고
    • Phase equilibria of membrane lipids from Acholeplasma laidlawii: Importance of a single lipid forming nonlamellar phases
    • Lindblom, G., I. Brentel, M. Sjölund, G. Wikander, and Å. Wieslander. 1986. Phase equilibria of membrane lipids from Acholeplasma laidlawii: importance of a single lipid forming nonlamellar phases. Biochemistry. 25:7502-7510.
    • (1986) Biochemistry , vol.25 , pp. 7502-7510
    • Lindblom, G.1    Brentel, I.2    Sjölund, M.3    Wikander, G.4    Wieslander, Å.5
  • 25
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance
    • Lindblom, G., and L. Rilfors. 1989. Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance. Biochim. Biophys. Acta. 988:221-256.
    • (1989) Biochim. Biophys. Acta. , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 28
    • 0029975929 scopus 로고    scopus 로고
    • Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures
    • Morein, S., A.-S. Andersson, L. Rilfors, and G. Lindblom. 1996. Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures. J. Biol. Chem. 271:6801-6809.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.-S.2    Rilfors, L.3    Lindblom, G.4
  • 29
    • 0030835044 scopus 로고    scopus 로고
    • Influence of membrane-spanning α-helical peptides on the phase behaviour of dioleoylphos-phatidylcholine/water system
    • Morein, S., E. Strandberg, J. A. Killian, S. Persson, G. Arvidson, R. E. Koeppe, II, and G. Lindblom. 1997. Influence of membrane-spanning α-helical peptides on the phase behaviour of dioleoylphos-phatidylcholine/water system. Biophys. J. 73:3078-3088.
    • (1997) Biophys. J. , vol.73 , pp. 3078-3088
    • Morein, S.1    Strandberg, E.2    Killian, J.A.3    Persson, S.4    Arvidson, G.5    Koeppe II, R.E.6    Lindblom, G.7
  • 30
    • 0022399766 scopus 로고
    • Simultaneous modelling of phase and calorimetric behavior in an amphiphilic peptide/ phospholipid model membrane
    • Morrow, M. R., J. C. Huschilt, and J. H. Davis. 1985. Simultaneous modelling of phase and calorimetric behavior in an amphiphilic peptide/ phospholipid model membrane. Biochemistry. 24:5396-5406.
    • (1985) Biochemistry , vol.24 , pp. 5396-5406
    • Morrow, M.R.1    Huschilt, J.C.2    Davis, J.H.3
  • 31
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen, O. G., and M. Bloom. 1984. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46:141-153.
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 32
    • 0027489133 scopus 로고
    • Sorting of membrane proteins in the secretory pathway
    • Pelham, H. R., and S. Munro. 1993. Sorting of membrane proteins in the secretory pathway. Cell. 75:603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.1    Munro, S.2
  • 33
    • 0031681279 scopus 로고    scopus 로고
    • Molecular ordering of interfacially located tryptophan analogs in ester- And ether-lipid bilayers
    • Persson, S., J. A. Killian, and G. Lindblom. 1998. Molecular ordering of interfacially located tryptophan analogs in ester- and ether-lipid bilayers. Biophys. J. 75:1365-1371.
    • (1998) Biophys. J. , vol.75 , pp. 1365-1371
    • Persson, S.1    Killian, J.A.2    Lindblom, G.3
  • 34
    • 0001913674 scopus 로고
    • Folding and assembly of integral membrane proteins: An introduction
    • S. H. White, editor. Oxford University Press, New York
    • Popot, J.-L., C. de Vitry, and A. Atteia. 1994. Folding and assembly of integral membrane proteins: an introduction. In Membrane Protein Structure: Experimental Approaches. S. H. White, editor. Oxford University Press, New York. 41-96.
    • (1994) Membrane Protein Structure: Experimental Approaches , pp. 41-96
    • Popot, J.-L.1    De Vitry, C.2    Atteia, A.3
  • 35
    • 0028362193 scopus 로고
    • Structural dimensions and their changes in a reentrant hexagonal-lamellar transition of phospholipids
    • Rand, R. P., and N. L. Fuller. 1994. Structural dimensions and their changes in a reentrant hexagonal-lamellar transition of phospholipids. Biophys. J. 66:2127-2138.
    • (1994) Biophys. J. , vol.66 , pp. 2127-2138
    • Rand, R.P.1    Fuller, N.L.2
  • 36
    • 0000558754 scopus 로고
    • Elastic interactions of photosynthetic reaction center proteins affecting phase transitions and protein distributions
    • Riegler, J., and H. Möhwald. 1986. Elastic interactions of photosynthetic reaction center proteins affecting phase transitions and protein distributions. Biophys. J. 49:1111-1118.
    • (1986) Biophys. J. , vol.49 , pp. 1111-1118
    • Riegler, J.1    Möhwald, H.2
  • 37
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • Reithmeier, R. A. F. 1995. Characterization and modeling of membrane proteins using sequence analysis. Curr Opin. Struct. Biol. 5:491-500.
    • (1995) Curr Opin. Struct. Biol. , vol.5 , pp. 491-500
    • Reithmeier, R.A.F.1
  • 38
    • 0027225477 scopus 로고
    • Polymorphic regulation of membrane phospholipid composition in Escherichia coli
    • Rietveld, A. G., J. A. Killian, W. Dowhan, and B. de Kruijff. 1993. Polymorphic regulation of membrane phospholipid composition in Escherichia coli. J. Biol. Chem. 268:12427-12433.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12427-12433
    • Rietveld, A.G.1    Killian, J.A.2    Dowhan, W.3    De Kruijff, B.4
  • 39
    • 0028785891 scopus 로고
    • Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli
    • Rietveld, A. G., M. C. Koorengevel, and B. de Kruijff. 1995. Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J. 14:5506-5513.
    • (1995) EMBO J. , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 40
    • 0014779155 scopus 로고
    • Two dimensional thin layer Chromatographic separation of polar lipids and determination of phospholipids by phosphorous analysis of spots
    • Rouser, G., S. Fleischer, and A. Yamamota. 1970. Two dimensional thin layer Chromatographic separation of polar lipids and determination of phospholipids by phosphorous analysis of spots. Lipids. 5:494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamota, A.3
  • 41
    • 46549104553 scopus 로고
    • Magnetic ordering of phospholipid membranes
    • Seelig, J., F. Borle, and T. A. Cross. 1985. Magnetic ordering of phospholipid membranes. Biochim. Biophys. Acta. 814:195-198.
    • (1985) Biochim. Biophys. Acta. , vol.814 , pp. 195-198
    • Seelig, J.1    Borle, F.2    Cross, T.A.3
  • 42
    • 0030783371 scopus 로고    scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: Implications for membrane fusion mechanisms
    • Siegel, D. P., and R. M. Epand. 1997. The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms. Biophys. J. 73:3089-3111.
    • (1997) Biophys. J. , vol.73 , pp. 3089-3111
    • Siegel, D.P.1    Epand, R.M.2
  • 43
    • 0023390222 scopus 로고
    • Hydrophobic molecules in lecithin-water systems. I. Formation of reversed hexagonal phases at high and low water contents
    • Sjölund, M., G. Lindblom, L. Rilfors, and G. Arvidson. 1987. Hydrophobic molecules in lecithin-water systems. I. Formation of reversed hexagonal phases at high and low water contents. Biophys. J. 52:145-153.
    • (1987) Biophys. J. , vol.52 , pp. 145-153
    • Sjölund, M.1    Lindblom, G.2    Rilfors, L.3    Arvidson, G.4
  • 44
    • 0024354092 scopus 로고
    • II) phase of phosphatidylethanolamine-containing membranes
    • II) phase of phosphatidylethanolamine-containing membranes. Biochemistry. 28:4245-4253.
    • (1989) Biochemistry , vol.28 , pp. 4245-4253
    • Tate, M.W.1    Gruner, S.M.2
  • 45
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • Von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 46
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.-M., W. C. Wimley, K. Gawrish, and S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrish, K.3    White, S.H.4
  • 47
    • 0026442901 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
    • Zhang, Y.-P., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 1992. Interaction of a peptide model of a hydrophobic transmembrane α-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry. 31:11579-11588.
    • (1992) Biochemistry , vol.31 , pp. 11579-11588
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.