메뉴 건너뛰기




Volumn 1788, Issue 2, 2009, Pages 390-401

Effects of temperature and pressure on the lateral organization of model membranes with functionally reconstituted multidrug transporter LmrA

Author keywords

Fluorescence spectroscopy; High hydrostatic pressure; Lipid phase transition; LmrA; Phospholipid; Raft mixture

Indexed keywords

CHOLESTEROL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; GLYCOLIPID; GLYCOPROTEIN P; LIPID; ORTEIN LMRA; UNCLASSIFIED DRUG;

EID: 59249086209     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.09.017     Document Type: Article
Times cited : (19)

References (56)
  • 5
    • 0004224163 scopus 로고
    • Cevc G. (Ed), Marcel Dekker, Inc, New York
    • In: Cevc G. (Ed). Phospholipids Handbook (1993), Marcel Dekker, Inc, New York
    • (1993) Phospholipids Handbook
  • 6
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim. Biophys. Acta 1595 (2002) 160-184
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 160-184
    • Winter, R.1
  • 7
    • 21644459337 scopus 로고    scopus 로고
    • Temperature-pressure configurational landscape of lipid bilayers and proteins
    • Winter R., and Dzwolak W. Temperature-pressure configurational landscape of lipid bilayers and proteins. Cell. Mol. Biol. 50 (2004) 397-417
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 397-417
    • Winter, R.1    Dzwolak, W.2
  • 9
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamics in the pressure-temperature plane
    • Meersman F., Smeller L., and Heremans K. Protein stability and dynamics in the pressure-temperature plane. Biochim. Biophys. Acta 1764 (2006) 346-354
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 10
    • 0003577553 scopus 로고
    • Pressure effects on biochemical systems
    • Kelm H. (Ed), Reidel Publishing Company, Dordrecht, Netherlands
    • Heremans K. Pressure effects on biochemical systems. In: Kelm H. (Ed). High Pressure Chemistry (1978), Reidel Publishing Company, Dordrecht, Netherlands 467-487
    • (1978) High Pressure Chemistry , pp. 467-487
    • Heremans, K.1
  • 11
    • 33745713605 scopus 로고    scopus 로고
    • Temperature and pressure effects on structural and conformational properties of POPC/SM/Cholesterol model raft mixtures - a FT-IR, SAXS, DSC, PPC and Laurdan fluorescence spectroscopy study
    • Nicolini C., Kraineva J., Khurana M., Periasamy N., Funari S.S., and Winter R. Temperature and pressure effects on structural and conformational properties of POPC/SM/Cholesterol model raft mixtures - a FT-IR, SAXS, DSC, PPC and Laurdan fluorescence spectroscopy study. Biochim. Biophys. Acta 1758 (2006) 248-258
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 248-258
    • Nicolini, C.1    Kraineva, J.2    Khurana, M.3    Periasamy, N.4    Funari, S.S.5    Winter, R.6
  • 13
    • 33749046141 scopus 로고    scopus 로고
    • Origins of life and biochemistry under high pressure conditions
    • Daniel I., Oger P., and Winter R. Origins of life and biochemistry under high pressure conditions. Chem. Soc. Rev. 35 (2006) 858-875
    • (2006) Chem. Soc. Rev. , vol.35 , pp. 858-875
    • Daniel, I.1    Oger, P.2    Winter, R.3
  • 14
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., and Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 26 (2001) 612-618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 16
    • 0022379140 scopus 로고
    • Mechanisms of inhibition of (Na,K)-ATPase by hydrostatic pressure studied with fluorescent probes
    • Chong P.L.G., Fortes P.A.G., and Jameson D.A. Mechanisms of inhibition of (Na,K)-ATPase by hydrostatic pressure studied with fluorescent probes. J. Biol. Chem. 260 (1985) 14484-14490
    • (1985) J. Biol. Chem. , vol.260 , pp. 14484-14490
    • Chong, P.L.G.1    Fortes, P.A.G.2    Jameson, D.A.3
  • 19
    • 0014976167 scopus 로고
    • High hydrostatic pressure and enzymic activity: inhibition of multimeric enzymes by dissociation
    • Penniston J.T. High hydrostatic pressure and enzymic activity: inhibition of multimeric enzymes by dissociation. Arch. Biochem. Biophys. 142 (1971) 322-332
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 322-332
    • Penniston, J.T.1
  • 20
    • 0036196009 scopus 로고    scopus 로고
    • Effects of pressure-induced membrane phase transitions on inactivation of HorA, an ATP-dependent multidrug resistance transporter, in Lactobacillus plantarum
    • Ulmer H.M., Herberhold H., Fahsel S., Gänzle M.G., Winter R., and Vogel R.F. Effects of pressure-induced membrane phase transitions on inactivation of HorA, an ATP-dependent multidrug resistance transporter, in Lactobacillus plantarum. Appl. Environ. Microbiol. 68 (2002) 1088-1095
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1088-1095
    • Ulmer, H.M.1    Herberhold, H.2    Fahsel, S.3    Gänzle, M.G.4    Winter, R.5    Vogel, R.F.6
  • 23
    • 1542461687 scopus 로고    scopus 로고
    • Winter R. (Ed), Springer-Verlag, Heidelberg, Germany
    • In: Winter R. (Ed). High Pressure Bioscience and Biotechnology II (2003), Springer-Verlag, Heidelberg, Germany
    • (2003) High Pressure Bioscience and Biotechnology II
  • 24
    • 0030273002 scopus 로고    scopus 로고
    • Tetracycline resistance determinants: mechanisms of action, regulation of expression, genetic mobility, and distribution
    • Roberts M.C. Tetracycline resistance determinants: mechanisms of action, regulation of expression, genetic mobility, and distribution. FEMS Microbiol. Rev. 19 (1996) 1-24
    • (1996) FEMS Microbiol. Rev. , vol.19 , pp. 1-24
    • Roberts, M.C.1
  • 25
    • 4644222866 scopus 로고    scopus 로고
    • Energetics of wild-type and mutant multidrug resistance secondary transporter LmrP of Lactococcus lactis
    • Mazurkiewicz P., Driessen A.J., and Konings W.N. Energetics of wild-type and mutant multidrug resistance secondary transporter LmrP of Lactococcus lactis. Biochim. Biophys. Acta 1658 (2004) 252-261
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 252-261
    • Mazurkiewicz, P.1    Driessen, A.J.2    Konings, W.N.3
  • 26
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • Margolles A., Putman M., van Veen H.W., and Konings W.N. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry 38 (1999) 16298-16306
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    van Veen, H.W.3    Konings, W.N.4
  • 27
    • 0034870399 scopus 로고    scopus 로고
    • Hop resistance in the beer spoilage bacterium Lactobacillus brevis is mediated by the ATP-binding cassette multidrug transporter HorA
    • Sakamoto K., Margolles A., van Veen H.W., and Konings W.N. Hop resistance in the beer spoilage bacterium Lactobacillus brevis is mediated by the ATP-binding cassette multidrug transporter HorA. J. Bacteriol. 183 (2001) 5371-5375
    • (2001) J. Bacteriol. , vol.183 , pp. 5371-5375
    • Sakamoto, K.1    Margolles, A.2    van Veen, H.W.3    Konings, W.N.4
  • 29
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • Bolhuis H., van Veen H.W., Molenaar D., Poolman B., Driessen A.J., and Konings W.N. Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J. 15 (1996) 4239-4245
    • (1996) EMBO J. , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    van Veen, H.W.2    Molenaar, D.3    Poolman, B.4    Driessen, A.J.5    Konings, W.N.6
  • 30
  • 31
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 32
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • van Veen H.W., Margolles A., Müller M., Higgins C.F., and Konings W.N. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J. 19 (2000) 2503-2514
    • (2000) EMBO J. , vol.19 , pp. 2503-2514
    • van Veen, H.W.1    Margolles, A.2    Müller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 33
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins
    • Rigaud J.L., Pitard B., and Levy D. Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim. Biophys. Acta 1231 (1995) 223-246
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 34
    • 36849115843 scopus 로고
    • Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetimes
    • Spencer R.D., and Weber G. Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetimes. J. Chem. Phys. 52 (1970) 1654-1663
    • (1970) J. Chem. Phys. , vol.52 , pp. 1654-1663
    • Spencer, R.D.1    Weber, G.2
  • 35
    • 0022647019 scopus 로고
    • Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry
    • Parasassi T., Conti F., and Gratton E. Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry. Cell Mol. Biol. 32 (1986) 103-108
    • (1986) Cell Mol. Biol. , vol.32 , pp. 103-108
    • Parasassi, T.1    Conti, F.2    Gratton, E.3
  • 36
    • 0030048608 scopus 로고    scopus 로고
    • Fluorescence generalized polarization of cell membranes: a two-photon scanning microscopy approach
    • Yu W., So P.T.C., French T., and Gratton E. Fluorescence generalized polarization of cell membranes: a two-photon scanning microscopy approach. Biophys. J. 70 (1996) 626-636
    • (1996) Biophys. J. , vol.70 , pp. 626-636
    • Yu, W.1    So, P.T.C.2    French, T.3    Gratton, E.4
  • 37
    • 0020997959 scopus 로고
    • A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution
    • Gratton E., and Limkeman M.M. A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution. Biophys. J. 44 (1983) 315-324
    • (1983) Biophys. J. , vol.44 , pp. 315-324
    • Gratton, E.1    Limkeman, M.M.2
  • 38
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi T., De Stasio G., Ravagnan G., Rusch R.M., and Gratton E. Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophys. J. 60 (1991) 179-189
    • (1991) Biophys. J. , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 39
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • Parasassi T., De Stasio G., d'Ubaldo A., and Gratton E. Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence. Biophys. J. 57 (1990) 1179-1186
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    d'Ubaldo, A.3    Gratton, E.4
  • 40
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm G., Muhr R., and Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5 (1992) 191-195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 42
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis
    • Vigano C., Margolles A., van Veen H.W., Konings W.N., and Ruysschaert J.M. Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis. J. Biol. Chem. 275 (2000) 10962-10967
    • (2000) J. Biol. Chem. , vol.275 , pp. 10962-10967
    • Vigano, C.1    Margolles, A.2    van Veen, H.W.3    Konings, W.N.4    Ruysschaert, J.M.5
  • 43
    • 33947388784 scopus 로고    scopus 로고
    • Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance
    • Siarheyeva A., Lopez J.J., Lehner I., Hellmich U.A., van Veen H.W., and Glaubitz C. Probing the molecular dynamics of the ABC multidrug transporter LmrA by deuterium solid-state nuclear magnetic resonance. Biochemistry 46 (2007) 3075-3083
    • (2007) Biochemistry , vol.46 , pp. 3075-3083
    • Siarheyeva, A.1    Lopez, J.J.2    Lehner, I.3    Hellmich, U.A.4    van Veen, H.W.5    Glaubitz, C.6
  • 44
    • 21244451188 scopus 로고    scopus 로고
    • Direct visualization of asymmetric behavior in supported lipid bilayers at the gel-fluid phase transition
    • Feng Z.V., Spurlin T.A., and Gewirth A.A. Direct visualization of asymmetric behavior in supported lipid bilayers at the gel-fluid phase transition. Biophys. J. 88 (2005) 2154-2164
    • (2005) Biophys. J. , vol.88 , pp. 2154-2164
    • Feng, Z.V.1    Spurlin, T.A.2    Gewirth, A.A.3
  • 45
    • 17144401112 scopus 로고    scopus 로고
    • Single-molecule measurements of the impact of lipid phase behavior on anchor strengths
    • Wieland J.A., Gewirth A.A., and Leckband D.E. Single-molecule measurements of the impact of lipid phase behavior on anchor strengths. J. Phys. Chem. B 109 (2005) 5985-5993
    • (2005) J. Phys. Chem. B , vol.109 , pp. 5985-5993
    • Wieland, J.A.1    Gewirth, A.A.2    Leckband, D.E.3
  • 46
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch S.L., and Keller S.L. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 85 (2003) 3074-3083
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 47
    • 33646012953 scopus 로고    scopus 로고
    • The effects of temperature, pressure and peptide incorporation on ternary model raft mixtures - a Laurdan fluorescence spectroscopy study
    • Periasamy N., and Winter R. The effects of temperature, pressure and peptide incorporation on ternary model raft mixtures - a Laurdan fluorescence spectroscopy study. Biochim. Biophys. Acta 1764 (2006) 398-404
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 398-404
    • Periasamy, N.1    Winter, R.2
  • 48
    • 0141939627 scopus 로고    scopus 로고
    • Differential properties of the sterols cholesterol, ergosterol, β-sitosterol, trans-7-dehydrocholesterol, stigmasterol and lanosterol on DPPC bilayer order
    • Bernsdorff C., and Winter R. Differential properties of the sterols cholesterol, ergosterol, β-sitosterol, trans-7-dehydrocholesterol, stigmasterol and lanosterol on DPPC bilayer order. J. Phys. Chem. B 107 (2003) 10658-10664
    • (2003) J. Phys. Chem. B , vol.107 , pp. 10658-10664
    • Bernsdorff, C.1    Winter, R.2
  • 49
    • 59249107231 scopus 로고    scopus 로고
    • H. Teichert, Behaviour of membrane transport proteins under high hydrostatic pressure, Dissertation, Technische Universität München, 2008.
    • H. Teichert, Behaviour of membrane transport proteins under high hydrostatic pressure, Dissertation, Technische Universität München, 2008.
  • 53
    • 0033230717 scopus 로고    scopus 로고
    • Pressure-regulated metabolism in microorganisms
    • Abe F., Kato C., and Horikoshi K. Pressure-regulated metabolism in microorganisms. Trends Microbiol. 447 (1999) 447-453
    • (1999) Trends Microbiol. , vol.447 , pp. 447-453
    • Abe, F.1    Kato, C.2    Horikoshi, K.3
  • 54
    • 36148983058 scopus 로고    scopus 로고
    • Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: perspectives from piezophysiology
    • Abe F. Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: perspectives from piezophysiology. Biosci. Biotechnol. Biochem. 71 (2007) 2347-2357
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2347-2357
    • Abe, F.1
  • 55
    • 22144450237 scopus 로고    scopus 로고
    • Determination of the activation volume of PLCβ by Gβγ-subunits through the use of high hydrostatic pressure
    • Scarlata S. Determination of the activation volume of PLCβ by Gβγ-subunits through the use of high hydrostatic pressure. Biophys. J. 88 (2005) 2867-2874
    • (2005) Biophys. J. , vol.88 , pp. 2867-2874
    • Scarlata, S.1
  • 56
    • 0037171143 scopus 로고    scopus 로고
    • Experiments on ion channels at high pressure
    • Macdonald A.G. Experiments on ion channels at high pressure. Biochim. Biophys. Acta 1595 (2002) 387-389
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 387-389
    • Macdonald, A.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.