메뉴 건너뛰기




Volumn 343, Issue 1, 2004, Pages 213-222

The reconstitution and activity of the small multidrug transporter EmrE is modulated by non-bilayer lipid composition

Author keywords

folding; lipid lateral pressure; membrane protein; multi drug transport; reconstitution

Indexed keywords

GLYCOPROTEIN P; MEMBRANE PROTEIN; SMALL MULTIDRUG TRANSPOTER EMRE; UNCLASSIFIED DRUG;

EID: 4444282465     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.032     Document Type: Article
Times cited : (39)

References (48)
  • 1
    • 0025392644 scopus 로고
    • Cloning of the ethidium efflux gene from Escherichia coli
    • A. Purewal, I. Jones, and M. Midgley Cloning of the ethidium efflux gene from Escherichia coli FEMS Microbiol. Letters 68 1990 73 76
    • (1990) FEMS Microbiol. Letters , vol.68 , pp. 73-76
    • Purewal, A.1    Jones, I.2    Midgley, M.3
  • 2
    • 0029925159 scopus 로고    scopus 로고
    • The SMR family: A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
    • I. Paulsen, R. Skurray, R. Tam, M. Saier, R. Turner, and R. Weiner The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs Mol. Microbiol. 19 1996 1167 1175
    • (1996) Mol. Microbiol. , vol.19 , pp. 1167-1175
    • Paulsen, I.1    Skurray, R.2    Tam, R.3    Saier, M.4    Turner, R.5    Weiner, R.6
  • 4
    • 0029999396 scopus 로고    scopus 로고
    • Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle
    • I.T. Arkin, W.P. Russ, M. Lebendiker, and S. Schuldiner Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle Biochemistry 35 1996 7233 7238
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4
  • 5
    • 0035863057 scopus 로고    scopus 로고
    • The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 resolution
    • C.G. Tate, E.R. Kunji, M. Lebendiker, and S. Schuldiner The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 resolution EMBO J. 20 2001 77 81
    • (2001) EMBO J. , vol.20 , pp. 77-81
    • Tate, C.G.1    Kunji, E.R.2    Lebendiker, M.3    Schuldiner, S.4
  • 6
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • T.R. Muth, and S. Schuldiner A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE EMBO J. 19 2000 234 240
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 7
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • I. Ubarretxena-Belandia, J.M. Baldwin, S. Schuldiner, and C.G. Tate Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer EMBO J. 22 2003 6175 6181
    • (2003) EMBO J. , vol.22 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 8
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Y. Elbaz, S. Steiner-Mordoch, T. Danieli, and S. Schuldiner In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state Proc. Natl Acad. Sci. USA 2004 EPub
    • (2004) Proc. Natl Acad. Sci. USA
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 9
    • 2942511249 scopus 로고    scopus 로고
    • Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli
    • C. Ma, and G. Chang Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli Proc. Natl Acad. Sci. USA 101 2004 2852 2857
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2852-2857
    • Ma, C.1    Chang, G.2
  • 10
    • 0035918237 scopus 로고    scopus 로고
    • A single carboxyl mutant of the multidrug transporter EmrE is fully functional
    • H. Yerushalmi, S.S. Mordoch, and S. Schuldiner A single carboxyl mutant of the multidrug transporter EmrE is fully functional J. Biol. Chem. 276 2001 12744 12748
    • (2001) J. Biol. Chem. , vol.276 , pp. 12744-12748
    • Yerushalmi, H.1    Mordoch, S.S.2    Schuldiner, S.3
  • 11
    • 0037507278 scopus 로고    scopus 로고
    • An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli
    • N. Gutman, S. Steiner-Mordoch, and S. Schuldiner An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli J. Biol. Chem. 278 2003 16082 16087
    • (2003) J. Biol. Chem. , vol.278 , pp. 16082-16087
    • Gutman, N.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 14
    • 0036306814 scopus 로고    scopus 로고
    • The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition
    • W. Meijberg, and P. Booth The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition J. Mol. Biol. 319 2002 839 853
    • (2002) J. Mol. Biol. , vol.319 , pp. 839-853
    • Meijberg, W.1    Booth, P.2
  • 15
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane composition: A role for nonbilayer lipids
    • S. Gruner Intrinsic curvature hypothesis for biomembrane composition: a role for nonbilayer lipids Proc. Natl Acad. Sci. USA 82 1985 3665 3669
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.1
  • 16
    • 0033522435 scopus 로고    scopus 로고
    • Correlation between the free energy of a channel-forming voltage-gated peptide and the spontaneous curvature of bilayer lipids
    • J. Lewis, and D. Cafiso Correlation between the free energy of a channel-forming voltage-gated peptide and the spontaneous curvature of bilayer lipids Biochemistry 38 1999 5932 5938
    • (1999) Biochemistry , vol.38 , pp. 5932-5938
    • Lewis, J.1    Cafiso, D.2
  • 17
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by nonlamellar-forming lipids
    • A. Bothelo, N. Gibson, R. Thurmond, Y. Wang, and M. Brown Conformational energetics of rhodopsin modulated by nonlamellar-forming lipids Biochemistry 41 2002 6354 6368
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Bothelo, A.1    Gibson, N.2    Thurmond, R.3    Wang, Y.4    Brown, M.5
  • 18
    • 0033587549 scopus 로고    scopus 로고
    • Modulation of folding and assembly of the membrane protein bacteriorhodopsin by intermolecular forces within the lipid bilayer
    • A. Curran, R. Templer, and P. Booth Modulation of folding and assembly of the membrane protein bacteriorhodopsin by intermolecular forces within the lipid bilayer Biochemistry 38 1999 9328 9336
    • (1999) Biochemistry , vol.38 , pp. 9328-9336
    • Curran, A.1    Templer, R.2    Booth, P.3
  • 19
    • 0034255144 scopus 로고    scopus 로고
    • Modulation of CTP:phosphocholine cytidylyltranferase by membrane curvature elastic stress
    • G. Attard, R. Templer, W. Smith, A. Hunt, and S. Jackowski Modulation of CTP:phosphocholine cytidylyltranferase by membrane curvature elastic stress Proc. Natl Acad. Sci. USA 97 2000 9032 9036
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9032-9036
    • Attard, G.1    Templer, R.2    Smith, W.3    Hunt, A.4    Jackowski, S.5
  • 21
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • V. Daggett, and A. Fersht The present view of the mechanism of protein folding Nature Rev. Mol. Cell. Biol. 4 2003 497 502
    • (2003) Nature Rev. Mol. Cell. Biol. , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 22
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • C. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.1
  • 23
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Y. Elbaz, S. Steiner-Mordoch, T. Danieli, and S. Schuldiner In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state Proc. Natl Acad. Sci. USA 101 2004 1519 1524
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 25
    • 0041735000 scopus 로고    scopus 로고
    • Conformational changes in the multidrug transporter EmrE associated with substrate binding
    • C.G. Tate, I. Ubarretxena-Belandia, and J.M. Baldwin Conformational changes in the multidrug transporter EmrE associated with substrate binding J. Mol. Biol. 332 2003 229 242
    • (2003) J. Mol. Biol. , vol.332 , pp. 229-242
    • Tate, C.G.1    Ubarretxena-Belandia, I.2    Baldwin, J.M.3
  • 26
    • 0026443063 scopus 로고
    • Colorimetric quantitation of trace amounts of sodium lauryl sulphate in the presence of nucleic acids and proteins
    • M. Arand, T. Friedberg, and F. Oesch Colorimetric quantitation of trace amounts of sodium lauryl sulphate in the presence of nucleic acids and proteins Anal. Biochem. 207 1992 73 75
    • (1992) Anal. Biochem. , vol.207 , pp. 73-75
    • Arand, M.1    Friedberg, T.2    Oesch, F.3
  • 27
    • 0035930510 scopus 로고    scopus 로고
    • In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit
    • D. Rotem, N. Sal-man, and S. Schuldiner In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit J. Biol. Chem. 276 2001 48243 48249
    • (2001) J. Biol. Chem. , vol.276 , pp. 48243-48249
    • Rotem, D.1    Sal-Man, N.2    Schuldiner, S.3
  • 28
    • 0037378077 scopus 로고    scopus 로고
    • Purified human MDR1 modulates membrane potential in reconstituted proteoliposomes
    • E. Howard, and P. Roepe Purified human MDR1 modulates membrane potential in reconstituted proteoliposomes Biochemistry 42 2003 3544 3555
    • (2003) Biochemistry , vol.42 , pp. 3544-3555
    • Howard, E.1    Roepe, P.2
  • 29
    • 0032541971 scopus 로고    scopus 로고
    • Detergent-mediated reconstitution of membrane proteins
    • J. Knol, K. Sjollema, and B. Poolman Detergent-mediated reconstitution of membrane proteins Biochemistry 37 1998 16410 16415
    • (1998) Biochemistry , vol.37 , pp. 16410-16415
    • Knol, J.1    Sjollema, K.2    Poolman, B.3
  • 30
    • 0034695044 scopus 로고    scopus 로고
    • ATPase activity and transport by a cGMP transporter in human erythrocyte ghosts and proteoliposome-reconstituted membrane extracts
    • E. Boadu, and G. Sager ATPase activity and transport by a cGMP transporter in human erythrocyte ghosts and proteoliposome-reconstituted membrane extracts Biochim. Biophys. Acta 1509 2000 467 474
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 467-474
    • Boadu, E.1    Sager, G.2
  • 31
    • 0019888608 scopus 로고
    • Purification and reconstitution of functional lactose carrier from Escherichia coli
    • M. Newman, D. Foster, T. Wilson, and H. Kaback Purification and reconstitution of functional lactose carrier from Escherichia coli J. Biol. Chem. 256 1981 11804 11808
    • (1981) J. Biol. Chem. , vol.256 , pp. 11804-11808
    • Newman, M.1    Foster, D.2    Wilson, T.3    Kaback, H.4
  • 33
    • 0033729495 scopus 로고    scopus 로고
    • Functional consequences of lipid packing stress
    • S. Bezrukov Functional consequences of lipid packing stress Curr. Opin. Colloid Interface Sci. 5 2000 237 243
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 237-243
    • Bezrukov, S.1
  • 34
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in membranes: A mechanism for modulation of protein function
    • R. Cantor Lateral pressures in membranes: a mechanism for modulation of protein function J. Phys. Chem. B 101 1997 1723 1725
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1723-1725
    • Cantor, R.1
  • 35
    • 0030992795 scopus 로고    scopus 로고
    • Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels
    • J. Lundbaek, A. Maer, and O. Andersen Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels Biochemistry 36 1997 5695 5701
    • (1997) Biochemistry , vol.36 , pp. 5695-5701
    • Lundbaek, J.1    Maer, A.2    Andersen, O.3
  • 36
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • J.S. Patzlaff, T. van der Heide, and B. Poolman The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA J. Biol. Chem. 278 2003 29546 29551
    • (2003) J. Biol. Chem. , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 37
    • 0037449746 scopus 로고    scopus 로고
    • Drug binding in human P-glycoprotein causes conformational changes in both nucleotide binding domains
    • T. Loo, M. Bartlett, and D. Clarke Drug binding in human P-glycoprotein causes conformational changes in both nucleotide binding domains J. Biol. Chem. 278 2003 1575 1578
    • (2003) J. Biol. Chem. , vol.278 , pp. 1575-1578
    • Loo, T.1    Bartlett, M.2    Clarke, D.3
  • 38
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • E. Yu, G. McDermott, H. Zgurskaya, H. Nikaido, and D. Koshland Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump Science 300 2003 976 980
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.1    McDermott, G.2    Zgurskaya, H.3    Nikaido, H.4    Koshland, D.5
  • 40
    • 0034467682 scopus 로고    scopus 로고
    • Structure-function relationships of integral membrane proteins: Membrane transporters vs channels
    • J. le Coutre, and H. Kaback Structure-function relationships of integral membrane proteins: membrane transporters vs channels Biopolymers 55 2000 297 307
    • (2000) Biopolymers , vol.55 , pp. 297-307
    • Le Coutre, J.1    Kaback, H.2
  • 41
    • 0034609525 scopus 로고    scopus 로고
    • Sensitive monitoring of the dynamics of a membrane-bound transport protein by tryptophan phosphorescence spectroscopy
    • J. Broos, G. Strambini, M. Gonnelli, E. Vos, M. Koolhof, and G. Robillard Sensitive monitoring of the dynamics of a membrane-bound transport protein by tryptophan phosphorescence spectroscopy Biochemistry 39 2000 10877 10883
    • (2000) Biochemistry , vol.39 , pp. 10877-10883
    • Broos, J.1    Strambini, G.2    Gonnelli, M.3    Vos, E.4    Koolhof, M.5    Robillard, G.6
  • 42
    • 0036845373 scopus 로고    scopus 로고
    • Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition
    • X. Wang, M. Bogdanov, and W. Dowhan Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition EMBO J. 21 2002 5673 5681
    • (2002) EMBO J. , vol.21 , pp. 5673-5681
    • Wang, X.1    Bogdanov, M.2    Dowhan, W.3
  • 43
    • 0037126033 scopus 로고    scopus 로고
    • Crosslinking of embedded cysteines reveals contact points in the EmrE oligomer
    • M. Soskine, S. Steiner-Mordoch, and S. Schuldiner Crosslinking of embedded cysteines reveals contact points in the EmrE oligomer Proc. Natl Acad. Sci. USA 99 2002 12043 12048
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12043-12048
    • Soskine, M.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 44
    • 0026565917 scopus 로고
    • +-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles
    • +-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles Biochem. J. 281 1992 95 102
    • (1992) Biochem. J. , vol.281 , pp. 95-102
    • Doyle, F.1    McGivan, J.2
  • 45
    • 0034707090 scopus 로고    scopus 로고
    • Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents
    • F. Goni, and A. Alonso Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents Biochim. Biophys. Acta 1508 2000 51 68
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 51-68
    • Goni, F.1    Alonso, A.2
  • 46
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • M. le Maire, P. Champeil, and J. Moller Interaction of membrane proteins and lipids with solubilizing detergents Biochim. Biophys. Acta 1508 2000 86 111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Moller, J.3
  • 47
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • M. Dubois, K. Gilles, J. Hamilton, P. Rebers, and F. Smith Colorimetric method for determination of sugars and related substances Anal. Biochem. 28 1956 350 356
    • (1956) Anal. Biochem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.2    Hamilton, J.3    Rebers, P.4    Smith, F.5
  • 48
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • M. Markwell, S. Haas, L. Bieber, and N. Tolbert A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples Anal. Biochem. 87 1978 206 210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.1    Haas, S.2    Bieber, L.3    Tolbert, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.