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Volumn 94, Issue 11, 2008, Pages 4348-4357

Interactions of fluorinated surfactants with diphtheria toxin T-domain: Testing new media for studies of membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIPHTHERIA TOXIN; FLUORINE DERIVATIVE; PHOSPHOLIPID; SURFACTANT;

EID: 44849136504     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.126235     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U. 2001. Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11:397-402.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 4
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C., R. Audebert, and J.-L. Popot. 1996. Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl. Acad. Sci. USA. 93:15047-15050.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 6
    • 0032075801 scopus 로고    scopus 로고
    • Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants
    • Chabaud, E., P. Barthelemy, N. Mora, J. L. Popot, and B. Pucci. 1998.Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants. Biochimie. 80:515-530.
    • (1998) Biochimie , vol.80 , pp. 515-530
    • Chabaud, E.1    Barthelemy, P.2    Mora, N.3    Popot, J.L.4    Pucci, B.5
  • 7
    • 0033518067 scopus 로고    scopus 로고
    • Synthesis and preliminary assessments of ethyl-terminated perfluoroalkyl nonionic surfactants derived from tris(hydroxymethyl) acrylamidomethane
    • Barthelemy, P., B. Ameduri, E. Chabaud, J. L. Popot, and B. Pucci. 1999. Synthesis and preliminary assessments of ethyl-terminated perfluoroalkyl nonionic surfactants derived from tris(hydroxymethyl) acrylamidomethane. Org. Lett. 1:1689-1692.
    • (1999) Org. Lett , vol.1 , pp. 1689-1692
    • Barthelemy, P.1    Ameduri, B.2    Chabaud, E.3    Popot, J.L.4    Pucci, B.5
  • 8
    • 1942532324 scopus 로고    scopus 로고
    • Hemifluorinated surfactants: A non-dissociating environment for handling membrane proteins in aqueous solutions?
    • Breyton, C., E. Chabaud, Y. Chaudier, B. Pucci, and J.-L. Popot. 2004. Hemifluorinated surfactants: a non-dissociating environment for handling membrane proteins in aqueous solutions? FEBS Lett. 564:312-318.
    • (2004) FEBS Lett , vol.564 , pp. 312-318
    • Breyton, C.1    Chabaud, E.2    Chaudier, Y.3    Pucci, B.4    Popot, J.-L.5
  • 9
    • 33644530973 scopus 로고    scopus 로고
    • Chaperoning of insertion of membrane proteins into lipid bilayers by hemifluorinated surfactants: Application to diphtheria toxin
    • Palchevskyy, S. S., Y. O. Posokhov, B. Olivier, J. L. Popot, B. Pucci, and A. S. Ladokhin. 2006. Chaperoning of insertion of membrane proteins into lipid bilayers by hemifluorinated surfactants: application to diphtheria toxin. Biochemistry. 45:2629-2635.
    • (2006) Biochemistry , vol.45 , pp. 2629-2635
    • Palchevskyy, S.S.1    Posokhov, Y.O.2    Olivier, B.3    Popot, J.L.4    Pucci, B.5    Ladokhin, A.S.6
  • 10
    • 0000483941 scopus 로고    scopus 로고
    • Trans- location of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain
    • Oh, K. J., L. Senzel, R. J. Collier, and A. Finkelstein. 1999. Trans- location of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain. Proc. Natl. Acad. Sci. USA. 96:8467-8470.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8467-8470
    • Oh, K.J.1    Senzel, L.2    Collier, R.J.3    Finkelstein, A.4
  • 11
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • Miller, C. J., J. L. Elliott, and R. J. Collier. 1999. Anthrax protective antigen: prepore-to-pore conversion. Biochemistry. 38:10432-10441.
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 12
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • Shatursky, O., A. P. Heuck, L. A. Shepard, J. Rossjohn, M. W. Parker, A. E. Johnson, and R. K. Tweten. 1999. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell. 99:293-299.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 14
    • 0033621164 scopus 로고    scopus 로고
    • Kinetic description of structural changes linked to membrane import of the colicin E1 channel protein
    • Zakharov, S. D., M. Lindeberg, and W. A. Cramer. 1999. Kinetic description of structural changes linked to membrane import of the colicin E1 channel protein. Biochemistry. 38:11325-11332.
    • (1999) Biochemistry , vol.38 , pp. 11325-11332
    • Zakharov, S.D.1    Lindeberg, M.2    Cramer, W.A.3
  • 15
    • 0033609909 scopus 로고    scopus 로고
    • Adventures in membrane protein topology: A study of the membrane-bound state of colicin E1
    • Tory, M. C., and A. R. Merrill. 1999. Adventures in membrane protein topology: a study of the membrane-bound state of colicin E1. J. Biol. Chem. 274:24539-24549.
    • (1999) J. Biol. Chem , vol.274 , pp. 24539-24549
    • Tory, M.C.1    Merrill, A.R.2
  • 17
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson, A. E., and M. A. van Waes. 1999. The translocon: a dynamic gateway at the ER membrane. Annu. Rev. Cell Dev. Biol. 15:799-842.
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 799-842
    • Johnson, A.E.1    van Waes, M.A.2
  • 18
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • Alder, N. N., and A. E. Johnson. 2004. Cotranslational membrane protein biogenesis at the endoplasmic reticulum. J. Biol. Chem. 279:22787-22790.
    • (2004) J. Biol. Chem , vol.279 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 19
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • Rapoport, T. A., V. Goder, S. U. Heinrich, and K. E. S. Matlack. 2004. Membrane-protein integration and the role of the translocation channel. Trends Cell Biol. 14:568-575.
    • (2004) Trends Cell Biol , vol.14 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.S.4
  • 21
    • 27844476903 scopus 로고    scopus 로고
    • Do protein-lipid interactions determine the recognition of transmembrane helices at the ER trans- locon?
    • White, S. H., and G. von Heijne. 2005. Do protein-lipid interactions determine the recognition of transmembrane helices at the ER trans- locon? Biochem. Soc. Trans. 33:1012-1015.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1012-1015
    • White, S.H.1    von Heijne, G.2
  • 22
    • 13444274461 scopus 로고    scopus 로고
    • Border crossing
    • Bowie, J. U. 2005. Border crossing. Nature. 433:367-369.
    • (2005) Nature , vol.433 , pp. 367-369
    • Bowie, J.U.1
  • 23
    • 2942627354 scopus 로고    scopus 로고
    • Reversible refolding of the diphtheria toxin T-domain on lipid membranes
    • Ladokhin, A. S., R. Legmann, R. J. Collier, and S. H. White. 2004. Reversible refolding of the diphtheria toxin T-domain on lipid membranes. Biochemistry. 43:7451-7458.
    • (2004) Biochemistry , vol.43 , pp. 7451-7458
    • Ladokhin, A.S.1    Legmann, R.2    Collier, R.J.3    White, S.H.4
  • 24
    • 14644429004 scopus 로고    scopus 로고
    • Reversible transition between the surface trimer and membrane-inserted monomer of annexin 12
    • Ladokhin, A. S., and H. T. Haigler. 2005. Reversible transition between the surface trimer and membrane-inserted monomer of annexin 12. Biochemistry. 44:3402-3409.
    • (2005) Biochemistry , vol.44 , pp. 3402-3409
    • Ladokhin, A.S.1    Haigler, H.T.2
  • 25
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2.0 A resolution
    • Bennett, M. J., S. Choe, and D. Eisenberg. 1994. Refined structure of dimeric diphtheria toxin at 2.0 A resolution. Protein Sci. 3:1444-1463.
    • (1994) Protein Sci , vol.3 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 26
    • 0032939820 scopus 로고    scopus 로고
    • Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes
    • Zhan, H., J. L. Elliott, W. H. Shen, P. D. Huynh, A. Finkelstein, and R. J. Collier. 1999. Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes. J. Membr. Biol. 167:173-181.
    • (1999) J. Membr. Biol , vol.167 , pp. 173-181
    • Zhan, H.1    Elliott, J.L.2    Shen, W.H.3    Huynh, P.D.4    Finkelstein, A.5    Collier, R.J.6
  • 27
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer, L. D., M. J. Hope, and P. R. Cullis. 1986. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta. 858:161-168.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 29
    • 0031008251 scopus 로고    scopus 로고
    • Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching
    • Ladokhin, A. S., W. C. Wimley, K. Hristova, and S. H. White. 1997. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching. Methods Enzymol. 278:474-486.
    • (1997) Methods Enzymol , vol.278 , pp. 474-486
    • Ladokhin, A.S.1    Wimley, W.C.2    Hristova, K.3    White, S.H.4
  • 30
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin, A. S., S. Jayasinghe, and S. H. White. 2000. How to measure and analyze tryptophan fluorescence in membranes 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
  • 31
    • 42949116926 scopus 로고    scopus 로고
    • Membrane insertion pathway of Annexin B12: Thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching
    • Posokhov, Y. O., M. V. Rodnin, L. Lu, and A. S. Ladokhin. 2008. Membrane insertion pathway of Annexin B12: thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching. Biochemistry. 47:5078-5087.
    • (2008) Biochemistry , vol.47 , pp. 5078-5087
    • Posokhov, Y.O.1    Rodnin, M.V.2    Lu, L.3    Ladokhin, A.S.4
  • 32
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:482-501.
    • (1994) Biophys. J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 33
    • 0037331059 scopus 로고    scopus 로고
    • Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy
    • Haustein, E., and P. Schwille. 2003. Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy. Methods. 29:153-166.
    • (2003) Methods , vol.29 , pp. 153-166
    • Haustein, E.1    Schwille, P.2
  • 35
    • 21144446624 scopus 로고    scopus 로고
    • NMR study of a membrane protein in detergent-free aqueous solution
    • Zoonens, M., L. J. Catoire, F. Giusti, and J. L. Popot. 2005. NMR study of a membrane protein in detergent-free aqueous solution. Proc. Natl. Acad. Sci. USA. 102:8893-8898.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8893-8898
    • Zoonens, M.1    Catoire, L.J.2    Giusti, F.3    Popot, J.L.4
  • 37
    • 33750296008 scopus 로고    scopus 로고
    • Lactobionamide surfactants with hydrogenated, perfluorinated or hemi- fluorinated tails: Physical-chemical and biochemical characterization
    • Lebaupain, F., A. G. Salvay, B. Olivier, G. Durand, A. S. Fabiano, N. Michel, J. L. Popot, C. Ebel, C. Breyton, and B. Pucci. 2006. Lactobionamide surfactants with hydrogenated, perfluorinated or hemi- fluorinated tails: physical-chemical and biochemical characterization. Langmuir. 22:8881-8890.
    • (2006) Langmuir , vol.22 , pp. 8881-8890
    • Lebaupain, F.1    Salvay, A.G.2    Olivier, B.3    Durand, G.4    Fabiano, A.S.5    Michel, N.6    Popot, J.L.7    Ebel, C.8    Breyton, C.9    Pucci, B.10
  • 38
    • 35148874303 scopus 로고    scopus 로고
    • Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer: Implications for in vitro studies of amphipol-stabilized membrane proteins
    • Zoonens, M., F. Giusti, F. Zito, and J. L. Popot. 2007. Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer: implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry. 46:10392-10404.
    • (2007) Biochemistry , vol.46 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.L.4
  • 39
    • 43649083325 scopus 로고    scopus 로고
    • Gohon, Y., T. Dahmane, R. W. Ruigrok, P. Schuck, D. Charvolin, F. Rappaport, P. Timmins, D. M. Engelman, C. Tribet, J. L. Popot, and C. Ebel. 2008. Bacteriorhodopsin/amphipol complexes: structural and functional properties. Biophys. J. 94. In press.
    • Gohon, Y., T. Dahmane, R. W. Ruigrok, P. Schuck, D. Charvolin, F. Rappaport, P. Timmins, D. M. Engelman, C. Tribet, J. L. Popot, and C. Ebel. 2008. Bacteriorhodopsin/amphipol complexes: structural and functional properties. Biophys. J. 94. In press.
  • 40
    • 0035450348 scopus 로고    scopus 로고
    • Slow reorganization of small phosphatidylcholine vesicles upon adsorption of amphiphilic polymers
    • Ladaviere, C., M. Toustou, T. Gulik-Krzywicki, and C. Tribet. 2001. Slow reorganization of small phosphatidylcholine vesicles upon adsorption of amphiphilic polymers. J. Colloid Interface Sci. 241: 178-187.
    • (2001) J. Colloid Interface Sci , vol.241 , pp. 178-187
    • Ladaviere, C.1    Toustou, M.2    Gulik-Krzywicki, T.3    Tribet, C.4
  • 42
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining the energetics of peptide- bilayer interactions
    • White, S. H., W. C. Wimley, A. S. Ladokhin, and K. Hristova. 1998. Protein folding in membranes: determining the energetics of peptide- bilayer interactions. Methods Enzymol. 295:62-87.
    • (1998) Methods Enzymol , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 44
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 45
    • 0035827137 scopus 로고    scopus 로고
    • Protein chemistry at membrane interfaces: Non-additivity of electrostatic and hydrophobic interactions
    • Ladokhin, A. S., and S. H. White. 2001. Protein chemistry at membrane interfaces: non-additivity of electrostatic and hydrophobic interactions. J. Mol. Biol. 309:543-552.
    • (2001) J. Mol. Biol , vol.309 , pp. 543-552
    • Ladokhin, A.S.1    White, S.H.2
  • 46
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin
    • Ladokhin, A. S., and S. H. White. 1999. Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285:1363-1369.
    • (1999) J. Mol. Biol , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 47
    • 34250195381 scopus 로고    scopus 로고
    • Folding amphipathic helices into membranes: Amphiphilicity trumps hydrophobicity
    • Fernandez-Vidal, M., S. Jayasinghe, A. S. Ladokhin, and S. H. White. 2007. Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity. J. Mol. Biol. 370:459-470.
    • (2007) J. Mol. Biol , vol.370 , pp. 459-470
    • Fernandez-Vidal, M.1    Jayasinghe, S.2    Ladokhin, A.S.3    White, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.