메뉴 건너뛰기




Volumn 44, Issue 15, 2005, Pages 5713-5721

Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: Studies with the mechanosensitive channel MscL

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; FLUORESCENCE; HYDROCARBONS; HYDROPHOBICITY; LIPIDS; MUTAGENESIS; ORGANIC SOLVENTS; PERMITTIVITY;

EID: 17144391476     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047338g     Document Type: Article
Times cited : (48)

References (38)
  • 3
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. (2003) Lipid-protein interactions in biological membranes: a structural perspective, Biochim. Biophys. Acta 1612, 1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 5
    • 0036789731 scopus 로고    scopus 로고
    • Interactions of phospholipids with the potassium channel KcsA
    • Williamson, I. M., Alvis, S. J., East, J. M., and Lee, A. G. (2002) Interactions of phospholipids with the potassium channel KcsA, Biophys. J. 83, 2026-2038.
    • (2002) Biophys. J. , vol.83 , pp. 2026-2038
    • Williamson, I.M.1    Alvis, S.J.2    East, J.M.3    Lee, A.G.4
  • 6
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of Type 1 single span membrane proteins
    • Landolt-Marticorena, C., Williams, K. A., Deber, C. M., and Reithmeier, R. A. F. (1993) Non-random distribution of amino acids in the transmembrane segments of Type 1 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
  • 7
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider, M. D., and Sansom, M. S. P. (2001) Amino acid distributions in integral membrane protein structures, Biochim. Biophys. Acta 1512, 1-14.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 1-14
    • Ulmschneider, M.D.1    Sansom, M.S.P.2
  • 8
    • 0033609498 scopus 로고    scopus 로고
    • The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane
    • Braun, P., and von Heijne, G. (1999) The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 38, 9778-9782.
    • (1999) Biochemistry , vol.38 , pp. 9778-9782
    • Braun, P.1    Von Heijne, G.2
  • 9
    • 0030738720 scopus 로고    scopus 로고
    • Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
    • Ren, J. H., Lew, S., Wang, Z. W., and London, E. (1997) Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration, Biochemistry 36, 10213-10220.
    • (1997) Biochemistry , vol.36 , pp. 10213-10220
    • Ren, J.H.1    Lew, S.2    Wang, Z.W.3    London, E.4
  • 10
    • 0141431014 scopus 로고    scopus 로고
    • The role of tryptophan residues in an integral membrane protein: Diacylglycerol kinase
    • Clark, E. H., East, J. M., and Lee, A. G. (2003) The role of tryptophan residues in an integral membrane protein: diacylglycerol kinase, Biochemistry 42, 11065-11073.
    • (2003) Biochemistry , vol.42 , pp. 11065-11073
    • Clark, E.H.1    East, J.M.2    Lee, A.G.3
  • 14
    • 0347988157 scopus 로고    scopus 로고
    • Destabilizing mutations promote membrane protein misfolding
    • Nagy, J. K., and Sanders, C. R. (2004) Destabilizing mutations promote membrane protein misfolding, Biochemistry 43, 19-25.
    • (2004) Biochemistry , vol.43 , pp. 19-25
    • Nagy, J.K.1    Sanders, C.R.2
  • 15
    • 0023652259 scopus 로고
    • Parallax method for direct measurements of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay, A., and London, E. (1987) Parallax method for direct measurements of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids, Biochemistry 26, 39-45.
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 16
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • Perozo, E., Cortes, D. M., Sompornpisut, P., and Martinac, B. (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels, Nature 418, 942-948.
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Martinac, B.4
  • 17
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., Spencer, R. H., Lee, A. T., Barclay, M. T., and Rees, D. C. (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel, Science 282, 2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 18
    • 0345492016 scopus 로고    scopus 로고
    • Lipid-protein interactions studied by introduction of a tryptophan residue: The mechanosensitive channel MscL
    • Powl, A. M., East, J. M., and Lee, A. G. (2003) Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL, Biochemistry 42, 14306-14317.
    • (2003) Biochemistry , vol.42 , pp. 14306-14317
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 19
    • 0032935824 scopus 로고    scopus 로고
    • Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL
    • Sukharev, S. I., Sigurdson, W. J., Kung, C., and Sachs, F. (1999) Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL, J. Gen. Physiol. 113, 525-539.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 525-539
    • Sukharev, S.I.1    Sigurdson, W.J.2    Kung, C.3    Sachs, F.4
  • 20
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill, O. P., and Martinac, B. (2001) Molecular basis of mechanotransduction in living cells, Physiol. Rev. 81, 685-740.
    • (2001) Physiol. Rev. , vol.81 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 21
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., Kloda, A., Cortes, D. M., and Martinac, B. (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating, Nat. Struct. Biol. 9, 696-703.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 22
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina, N., Totemeyer, S., Stokes, N. R., Louis, P., Jones, M. A., and Booth, I. R. (1999) Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity, EMBOJ. 18, 1730-1737.
    • (1999) EMBOJ , vol.18 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 23
    • 0032826458 scopus 로고    scopus 로고
    • Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity
    • Yoshimura, K., Batiza, A., Schroeder, M., Blount, P., and Kung, C. (1999) Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity, Biophys. J. 77, 1960-1972.
    • (1999) Biophys. J. , vol.77 , pp. 1960-1972
    • Yoshimura, K.1    Batiza, A.2    Schroeder, M.3    Blount, P.4    Kung, C.5
  • 24
    • 0020485872 scopus 로고
    • Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid
    • East, J. M., and Lee, A. G. (1982) Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid, Biochemistry 21, 4144-4151.
    • (1982) Biochemistry , vol.21 , pp. 4144-4151
    • East, J.M.1    Lee, A.G.2
  • 25
    • 0016312487 scopus 로고
    • Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes
    • Warren, G. B., Toon, P. A., Birdsall, N. J. M., Lee, A. G., and Metcalfe, J. C. (1974) Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes, Biochemistry 13, 5501-5507.
    • (1974) Biochemistry , vol.13 , pp. 5501-5507
    • Warren, G.B.1    Toon, P.A.2    Birdsall, N.J.M.3    Lee, A.G.4    Metcalfe, J.C.5
  • 26
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membrane properly, and why bother?
    • Ladokhin, A. S., Jayasinghe, S., and White, S. H. (2000) How to measure and analyze tryptophan fluorescence in membrane properly, and why bother?, Anal. Biochem. 285, 235-245.
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 27
    • 84945799762 scopus 로고
    • Fluorescence quantum yields of tryptophan and tyrosine
    • Chen, R. F. (1967) Fluorescence quantum yields of tryptophan and tyrosine, Anal. Lett. 1, 35-42.
    • (1967) Anal. Lett. , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 28
    • 0038080063 scopus 로고    scopus 로고
    • Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL - Implications for channel gating and evolutionary design
    • Maurer, J. A., and Dougherty, D. A. (2003) Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL - Implications for channel gating and evolutionary design. J. Biol. Chem. 278, 21076-21082.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21076-21082
    • Maurer, J.A.1    Dougherty, D.A.2
  • 29
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J., and Holloway, P. W. (1990) Quenching of tryptophan fluorescence by brominated phospholipid, Biochemistry 29, 9638-9643.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 30
    • 0033032331 scopus 로고    scopus 로고
    • Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: Theoretical considerations
    • Ladokhin, A. S. (1999) Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: Theoretical considerations, Biophys. J. 76, 946-955.
    • (1999) Biophys. J. , vol.76 , pp. 946-955
    • Ladokhin, A.S.1
  • 31
    • 0037465698 scopus 로고    scopus 로고
    • Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic α-helix locations within membranes
    • Caputo, G. A., and London, E. (2003) Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic α-helix locations within membranes, Biochemistry 42, 3265-3274.
    • (2003) Biochemistry , vol.42 , pp. 3265-3274
    • Caputo, G.A.1    London, E.2
  • 32
    • 0026787997 scopus 로고
    • Polarity of lipid bilayers. A fluorescence investigation
    • Perochon, E., Lopez, A., and Tocanne, J. F. (1992) Polarity of lipid bilayers. A fluorescence investigation, Biochemistry 31, 7672-7682.
    • (1992) Biochemistry , vol.31 , pp. 7672-7682
    • Perochon, E.1    Lopez, A.2    Tocanne, J.F.3
  • 33
    • 0019881824 scopus 로고
    • Time-resolved emission spectroscopy of the dansyl fluorescence probe
    • Ghiggino, K. P., Lee, A. G., Meech, S. R., O'Connor, D. V., and Phillips, D. (1981) Time-resolved emission spectroscopy of the dansyl fluorescence probe, Biochemistry 20, 5381-5389.
    • (1981) Biochemistry , vol.20 , pp. 5381-5389
    • Ghiggino, K.P.1    Lee, A.G.2    Meech, S.R.3    O'Connor, D.V.4    Phillips, D.5
  • 34
    • 0034884665 scopus 로고    scopus 로고
    • Site-directed spin-labeling analysis of reconstituted MscL in the closed state
    • Perozo, E., Kloda, A., Cortes, D. M., and Martinac, B. (2001) Site-directed spin-labeling analysis of reconstituted MscL in the closed state, J. Gen. Physiol. 118, 193-205.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 193-205
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 35
    • 0041320859 scopus 로고    scopus 로고
    • Investigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations
    • Elmore, D. E., and Dougherty, D. A. (2003) Investigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations, Biophys. J. 85, 1512-1524.
    • (2003) Biophys. J. , vol.85 , pp. 1512-1524
    • Elmore, D.E.1    Dougherty, D.A.2
  • 36
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee, A. G. (2004) How lipids affect the activities of integral membrane proteins, Biochim. Biophys. Acta 1666, 62-87.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 37
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R. M. (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps, Acta Crystallogr., Sect. D 55, 938-940.
    • (1999) Acta Crystallogr., Sect. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 38
    • 0001724013 scopus 로고
    • The dielectric constant of dioxane-water mixtures between 0 and 80°
    • Akerlof, G., and Short, O. A. (1936) The dielectric constant of dioxane-water mixtures between 0 and 80°, J. Am. Chem. Soc. 58, 1241-1243.
    • (1936) J. Am. Chem. Soc. , vol.58 , pp. 1241-1243
    • Akerlof, G.1    Short, O.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.