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Volumn 1694, Issue 1-3 SPEC.ISS., 2004, Pages 97-109

The role of lipids in membrane insertion and translocation of bacterial proteins

Author keywords

Lipid protein interaction; Membrane phospholipid; Membrane protein assembly; Protein insertion; Protein secretion

Indexed keywords

BACTERIAL PROTEIN; COAT PROTEIN;

EID: 9144247030     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.03.007     Document Type: Review
Times cited : (58)

References (135)
  • 2
    • 0036663201 scopus 로고    scopus 로고
    • Bacterial secretome: The assembly manual and operating instructions
    • Economou A. Bacterial secretome: the assembly manual and operating instructions. Mol. Membr. Biol. 19:2002;159-169
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 159-169
    • Economou, A.1
  • 3
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly
    • Luirink J., Samuelson T., de Gier J. YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly. FEBS Lett. 501:2001;1-5
    • (2001) FEBS Lett. , vol.501 , pp. 1-5
    • Luirink, J.1    Samuelson, T.2    De Gier, J.3
  • 4
    • 0035201578 scopus 로고    scopus 로고
    • Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
    • Müller M., Koch H.G., Beck K., Schaefer U. Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog. Nucl. Acid Res. Mol. Biol. 66:2001;107-157
    • (2001) Prog. Nucl. Acid Res. Mol. Biol. , vol.66 , pp. 107-157
    • Müller, M.1    Koch, H.G.2    Beck, K.3    Schaefer, U.4
  • 5
    • 0034193232 scopus 로고    scopus 로고
    • Role of lipids in the translocation of proteins across membranes
    • van Voorst F., de Kruijff B. Role of lipids in the translocation of proteins across membranes. Biochem. J. 347:2000;601-612
    • (2000) Biochem. J. , vol.347 , pp. 601-612
    • Van Voorst, F.1    De Kruijff, B.2
  • 6
    • 0018135125 scopus 로고
    • Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli
    • Raetz C.R. Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli. Microbiol. Rev. 42:1978;614-659
    • (1978) Microbiol. Rev. , vol.42 , pp. 614-659
    • Raetz, C.R.1
  • 7
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. U. S. A. 82:1985;3665-3669
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 8
    • 0031566307 scopus 로고    scopus 로고
    • Lipids beyond the bilayer
    • de Kruijff B. Lipids beyond the bilayer. Nature. 386:1997;129-130
    • (1997) Nature , vol.386 , pp. 129-130
    • De Kruijff, B.1
  • 9
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: A mechanism for modulation of protein function
    • Cantor R.S. Lateral pressures in cell 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.S.1
  • 10
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • Cantor R.S. Lipid composition and the lateral pressure profile in bilayers. Biophys. J. 76:1999;2625-2639
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 11
    • 0027225477 scopus 로고
    • Polymorphic regulation of membrane phospholipid composition in Escherichia coli
    • Rietveld A.G., Killian J.A., Dowhan W., de Kruijff B. Polymorphic regulation of membrane phospholipid composition in Escherichia coli. J. Biol. Chem. 268:1993;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
  • 12
    • 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., Andersson A., Rilfors L., Lindblom G. Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures. J. Biol. Chem. 271:1996;6801-6809
    • (1996) J. Biol. Chem. , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.2    Rilfors, L.3    Lindblom, G.4
  • 13
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan W. Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66:1997;199-232
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 15
    • 0036425599 scopus 로고    scopus 로고
    • Phospholipid flip-flop in biogenic membranes: What is needed to connect opposite sides
    • Kol M.A., de Kruijff B., de Kroon A.I. Phospholipid flip-flop in biogenic membranes: what is needed to connect opposite sides. Semin. Cell Dev. Biol. 13:2002;163-170
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 163-170
    • Kol, M.A.1    De Kruijff, B.2    De Kroon, A.I.3
  • 16
    • 0025881880 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability
    • DeChavigny A., Heacock P.N., Dowhan W. Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability. J. Biol. Chem. 266:1991;5323-5332
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • Dechavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 17
    • 0027999523 scopus 로고
    • Regulation of lipid polymorphism is essential for the viability of phosphatidylethanolamine-deficient Escherichia coli cells
    • Rietveld A.G., Chupin V.V., Koorengevel M.C., Wienk H.L., Dowhan W., de Kruijff B. Regulation of lipid polymorphism is essential for the viability of phosphatidylethanolamine-deficient Escherichia coli cells. J. Biol. Chem. 269:1994;28670-28675
    • (1994) J. Biol. Chem. , vol.269 , pp. 28670-28675
    • Rietveld, A.G.1    Chupin, V.V.2    Koorengevel, M.C.3    Wienk, H.L.4    Dowhan, W.5    De Kruijff, B.6
  • 18
    • 0024462213 scopus 로고
    • Alteration of the phospholipid composition of Escherichia coli through genetic manipulation
    • Heacock P.N., Dowhan W. Alteration of the phospholipid composition of Escherichia coli through genetic manipulation. J. Biol. Chem. 264:1989;14972-14977
    • (1989) J. Biol. Chem. , vol.264 , pp. 14972-14977
    • Heacock, P.N.1    Dowhan, W.2
  • 19
    • 0033988057 scopus 로고    scopus 로고
    • Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin
    • Kikuchi S., Shibuya I., Matsumoto K. Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin. J. Bacteriol. 182:2000;371-376
    • (2000) J. Bacteriol. , vol.182 , pp. 371-376
    • Kikuchi, S.1    Shibuya, I.2    Matsumoto, K.3
  • 20
    • 0028785891 scopus 로고
    • Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli
    • Rietveld A.G., Koorengevel M.C., de Kruijff B. Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J. 14:1995;5506-5513
    • (1995) EMBO J. , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 21
    • 0034723287 scopus 로고    scopus 로고
    • Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase
    • van der Does C., Swaving J., van Klompenburg W., Driessen A.J.M. Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase. J. Biol. Chem. 275:2000;2472-2478
    • (2000) J. Biol. Chem. , vol.275 , pp. 2472-2478
    • Van Der Does, C.1    Swaving, J.2    Van Klompenburg, W.3    Driessen, A.J.M.4
  • 22
    • 0034161573 scopus 로고    scopus 로고
    • SecYEG assembles into a tetramer to form the active protein translocation channel
    • Manting E.H., vanderDoes C., Remiy H., Engel A., Driessen A.J.M. SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19:2000;852-861
    • (2000) EMBO J. , vol.19 , pp. 852-861
    • Manting, E.H.1    Vanderdoes, C.2    Remiy, H.3    Engel, A.4    Driessen, A.J.M.5
  • 23
    • 0345196631 scopus 로고    scopus 로고
    • The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
    • Meyer T.H., Menetret J.F., Breitling R., Miller K.R., Akey C.W., Rapoport T.A. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J. Mol. Biol. 285:1999;1789-1800
    • (1999) J. Mol. Biol. , vol.285 , pp. 1789-1800
    • Meyer, T.H.1    Menetret, J.F.2    Breitling, R.3    Miller, K.R.4    Akey, C.W.5    Rapoport, T.A.6
  • 25
    • 0032555499 scopus 로고    scopus 로고
    • Effects of nonlamellar-prone lipids on the ATPase activity of SecA bound to model membranes
    • Ahn T., Kim H. Effects of nonlamellar-prone lipids on the ATPase activity of SecA bound to model membranes. J. Biol. Chem. 273:1998;21692-21698
    • (1998) J. Biol. Chem. , vol.273 , pp. 21692-21698
    • Ahn, T.1    Kim, H.2
  • 26
    • 0023878031 scopus 로고
    • Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
    • de Vrije T., de Swart R.I., Dowhan W., Tommassen J., de Kruijff B. Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes. Nature. 334:1988;173-175
    • (1988) Nature , vol.334 , pp. 173-175
    • De Vrije, T.1    De Swart, R.I.2    Dowhan, W.3    Tommassen, J.4    De Kruijff, B.5
  • 27
    • 0025835871 scopus 로고
    • Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes
    • Kusters R., Dowhan W., de Kruijff B. Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes. J. Biol. Chem. 266:1991;8659-8662
    • (1991) J. Biol. Chem. , vol.266 , pp. 8659-8662
    • Kusters, R.1    Dowhan, W.2    De Kruijff, B.3
  • 28
    • 0026514429 scopus 로고
    • SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: A monolayer study
    • Breukink E., Demel R.A., de Korte-Kool G., de Kruijff B. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study. Biochemistry. 31:1992;1119-1124
    • (1992) Biochemistry , vol.31 , pp. 1119-1124
    • Breukink, E.1    Demel, R.A.2    De Korte-Kool, G.3    De Kruijff, B.4
  • 29
    • 0026777830 scopus 로고
    • Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding
    • Ulbrandt N.D., London E., Oliver D.B. Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding. J. Biol. Chem. 267:1992;15184-15192
    • (1992) J. Biol. Chem. , vol.267 , pp. 15184-15192
    • Ulbrandt, N.D.1    London, E.2    Oliver, D.B.3
  • 31
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F.U., Lecker S., Schiebel E., Hendrick J.P., Wickner W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell. 63:1990;269-279
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 32
    • 0026344236 scopus 로고
    • SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane
    • Hendrick J.P., Wickner W. SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane. J. Biol. Chem. 266:1991;24596-24600
    • (1991) J. Biol. Chem. , vol.266 , pp. 24596-24600
    • Hendrick, J.P.1    Wickner, W.2
  • 33
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill R., Dowhan W., Wickner W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell. 60:1990;271-280
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 34
    • 0030922143 scopus 로고    scopus 로고
    • The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase
    • Eichler J., Brunner J., Wickner W. The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase. EMBO J. 16:1997;2188-2196
    • (1997) EMBO J. , vol.16 , pp. 2188-2196
    • Eichler, J.1    Brunner, J.2    Wickner, W.3
  • 35
    • 0027769773 scopus 로고
    • SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
    • Driessen A.J. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer. Biochemistry. 32:1993;13190-13197
    • (1993) Biochemistry , vol.32 , pp. 13190-13197
    • Driessen, A.J.1
  • 36
    • 0025959111 scopus 로고
    • SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
    • Akita M., Shinkai A., Matsuyama S., Mizushima S. SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer. Biochem. Biophys. Res. Commun. 174:1991;211-216
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 211-216
    • Akita, M.1    Shinkai, A.2    Matsuyama, S.3    Mizushima, S.4
  • 38
    • 0037009514 scopus 로고    scopus 로고
    • Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
    • Or E., Navon A., Rapoport T. Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane. EMBO J. 21:2002;4470-4479
    • (2002) EMBO J. , vol.21 , pp. 4470-4479
    • Or, E.1    Navon, A.2    Rapoport, T.3
  • 40
    • 0028241570 scopus 로고
    • Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature
    • Nishiyama K., Hanada M., Tokuda H. Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature. EMBO J. 13:1994;3272-3277
    • (1994) EMBO J. , vol.13 , pp. 3272-3277
    • Nishiyama, K.1    Hanada, M.2    Tokuda, H.3
  • 41
    • 0030029447 scopus 로고    scopus 로고
    • SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature
    • Hanada M., Nishiyama K., Tokuda H. SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature. FEBS Lett. 381:1996;25-28
    • (1996) FEBS Lett. , vol.381 , pp. 25-28
    • Hanada, M.1    Nishiyama, K.2    Tokuda, H.3
  • 42
    • 0028906150 scopus 로고
    • Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature
    • Kontinen V.P., Tokuda H. Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature. FEBS Lett. 364:1995;157-160
    • (1995) FEBS Lett. , vol.364 , pp. 157-160
    • Kontinen, V.P.1    Tokuda, H.2
  • 43
    • 0032724657 scopus 로고    scopus 로고
    • Increases in acidic phospholipid contents specifically restore protein translocation in a cold-sensitive secA or secG null mutant
    • Suzuki H., Nishiyama K., Tokuda H. Increases in acidic phospholipid contents specifically restore protein translocation in a cold-sensitive secA or secG null mutant. J. Biol. Chem. 274:1999;31020-31024
    • (1999) J. Biol. Chem. , vol.274 , pp. 31020-31024
    • Suzuki, H.1    Nishiyama, K.2    Tokuda, H.3
  • 44
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • Nishiyama K., Suzuki T., Tokuda H. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell. 85:1996;71-81
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 45
    • 0036775559 scopus 로고    scopus 로고
    • Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA
    • Nagamori S., Nishiyama K., Tokuda H. Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA. J. Biochem. 132:2002;629-634
    • (2002) J. Biochem. , vol.132 , pp. 629-634
    • Nagamori, S.1    Nishiyama, K.2    Tokuda, H.3
  • 46
    • 0023730553 scopus 로고
    • Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization
    • Batenburg A.M., Demel R.A., Verkleij A.J., de Kruijff B. Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization. Biochemistry. 27:1988;5678-5685
    • (1988) Biochemistry , vol.27 , pp. 5678-5685
    • Batenburg, A.M.1    Demel, R.A.2    Verkleij, A.J.3    De Kruijff, B.4
  • 47
    • 0025180750 scopus 로고
    • Lipid and peptide specificities in signal peptide-lipid interactions in model membranes
    • Demel R.A., Goormaghtigh E., de Kruijff B. Lipid and peptide specificities in signal peptide-lipid interactions in model membranes. Biochim. Biophys. Acta. 1027:1990;155-162
    • (1990) Biochim. Biophys. Acta , vol.1027 , pp. 155-162
    • Demel, R.A.1    Goormaghtigh, E.2    De Kruijff, B.3
  • 48
    • 0027248503 scopus 로고
    • OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidylglycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane
    • Phoenix D.A., Kusters R., Hikita C., Mizushima S., de Kruijff B. OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidylglycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane. J. Biol. Chem. 268:1993;17069-17073
    • (1993) J. Biol. Chem. , vol.268 , pp. 17069-17073
    • Phoenix, D.A.1    Kusters, R.2    Hikita, C.3    Mizushima, S.4    De Kruijff, B.5
  • 49
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath K., Mothes W., Wilkinson B.M., Stirling C.J., Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell. 94:1998;795-807
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 50
    • 0026573926 scopus 로고
    • Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles
    • Keller R.C., Killian J.A., de Kruijff B. Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles. Biochemistry. 31:1992;1672-1677
    • (1992) Biochemistry , vol.31 , pp. 1672-1677
    • Keller, R.C.1    Killian, J.A.2    De Kruijff, B.3
  • 51
    • 0024971493 scopus 로고
    • Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties
    • McKnight C.J., Briggs M.S., Gierasch L.M. Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties. J. Biol. Chem. 264:1989;17293-17297
    • (1989) J. Biol. Chem. , vol.264 , pp. 17293-17297
    • McKnight, C.J.1    Briggs, M.S.2    Gierasch, L.M.3
  • 53
    • 0027769981 scopus 로고
    • Membrane-bound conformation of a signal peptide: A transferred nuclear Overhauser effect analysis
    • Wang Z., Jones J.D., Rizo J., Gierasch L.M. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 32:1993;13991-13999
    • (1993) Biochemistry , vol.32 , pp. 13991-13999
    • Wang, Z.1    Jones, J.D.2    Rizo, J.3    Gierasch, L.M.4
  • 54
    • 0037135542 scopus 로고    scopus 로고
    • The phase property of membrane phospholipids is affected by the functionality of signal peptides from the Escherichia coli ribose-binding protein
    • Ahn T., Oh D.-B., Kim H., Park C. The phase property of membrane phospholipids is affected by the functionality of signal peptides from the Escherichia coli ribose-binding protein. J. Biol. Chem. 277:2002;26157-26162
    • (2002) J. Biol. Chem. , vol.277 , pp. 26157-26162
    • Ahn, T.1    Oh, D.-B.2    Kim, H.3    Park, C.4
  • 56
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian J.A. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:1998;401-416
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 57
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1998;1029-1038
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 61
    • 0033569759 scopus 로고    scopus 로고
    • SecA is not required for signal recognition particle-mediated targeting and initial membrane insertion of a nascent inner membrane protein
    • Scotti P.A., Valent Q.A., Manting E.H., Urbanus M.L., Driessen A.J.M., Oudega B., Luirink J. SecA is not required for signal recognition particle-mediated targeting and initial membrane insertion of a nascent inner membrane protein. J. Biol. Chem. 274:1999;29883-29888
    • (1999) J. Biol. Chem. , vol.274 , pp. 29883-29888
    • Scotti, P.A.1    Valent, Q.A.2    Manting, E.H.3    Urbanus, M.L.4    Driessen, A.J.M.5    Oudega, B.6    Luirink, J.7
  • 63
    • 0035854809 scopus 로고    scopus 로고
    • FtsY binds to the Escherichia coli inner membrane via interactions with phosphatidylethanolamine and membrane proteins
    • Millman J.S., Qi H.Y., Vulcu F., Bernstein H.D., Andrews D.W. FtsY binds to the Escherichia coli inner membrane via interactions with phosphatidylethanolamine and membrane proteins. J. Biol. Chem. 276:2001;25982-25989
    • (2001) J. Biol. Chem. , vol.276 , pp. 25982-25989
    • Millman, J.S.1    Qi, H.Y.2    Vulcu, F.3    Bernstein, H.D.4    Andrews, D.W.5
  • 64
    • 0034618026 scopus 로고    scopus 로고
    • Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon
    • Koch H.G., Müller M. Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon. J. Cell Biol. 150:2000;689-694
    • (2000) J. Cell Biol. , vol.150 , pp. 689-694
    • Koch, H.G.1    Müller, M.2
  • 65
    • 0027473683 scopus 로고
    • Sec dependent and sec independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
    • Andersson H., von Heijne G. Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length. EMBO J. 12:1993;683-691
    • (1993) EMBO J. , vol.12 , pp. 683-691
    • Andersson, H.1    Von Heijne, G.2
  • 66
    • 0022001799 scopus 로고
    • Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli
    • Wolfe P.B., Rice M., Wickner W. Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. J. Biol. Chem. 260:1985;1836-1841
    • (1985) J. Biol. Chem. , vol.260 , pp. 1836-1841
    • Wolfe, P.B.1    Rice, M.2    Wickner, W.3
  • 67
    • 0025675488 scopus 로고
    • The function of a leader peptide in translocating charged amino acyl residues across a membrane
    • Rohrer J., Kuhn A. The function of a leader peptide in translocating charged amino acyl residues across a membrane. Science. 250:1990;1418-1421
    • (1990) Science , vol.250 , pp. 1418-1421
    • Rohrer, J.1    Kuhn, A.2
  • 68
    • 0032430831 scopus 로고    scopus 로고
    • Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli
    • de Gier J.W.L., Scotti P.A., Sääf A., Valent Q.A., Kuhn A., Luirink J., von Heijne G. Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 95:1998;14646-14651
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14646-14651
    • De Gier, J.W.L.1    Scotti, P.A.2    Sääf, A.3    Valent, Q.A.4    Kuhn, A.5    Luirink, J.6    Von Heijne, G.7
  • 69
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • Cao G., Kuhn A., Dalbey R.E. The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism. EMBO J. 14:1995;866-875
    • (1995) EMBO J. , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 70
    • 0030953689 scopus 로고    scopus 로고
    • Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane
    • Kiefer D., Hu X., Dalbey R., Kuhn A. Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane. EMBO J. 16:1997;2197-2204
    • (1997) EMBO J. , vol.16 , pp. 2197-2204
    • Kiefer, D.1    Hu, X.2    Dalbey, R.3    Kuhn, A.4
  • 71
    • 0033571246 scopus 로고    scopus 로고
    • Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control
    • Kiefer D., Kuhn A. Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control. EMBO J. 18:1999;6299-6306
    • (1999) EMBO J. , vol.18 , pp. 6299-6306
    • Kiefer, D.1    Kuhn, A.2
  • 72
    • 0033548545 scopus 로고    scopus 로고
    • Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins
    • Schuenemann T.A., Delgado-Nixon V.M., Dalbey R.E. Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins. J. Biol. Chem. 274:1999;6855-6864
    • (1999) J. Biol. Chem. , vol.274 , pp. 6855-6864
    • Schuenemann, T.A.1    Delgado-Nixon, V.M.2    Dalbey, R.E.3
  • 73
    • 0025142363 scopus 로고
    • Initial steps in protein membrane insertion. Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction
    • Gallusser A., Kuhn A. Initial steps in protein membrane insertion. Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction. EMBO J. 9:1990;2723-2729
    • (1990) EMBO J. , vol.9 , pp. 2723-2729
    • Gallusser, A.1    Kuhn, A.2
  • 74
    • 0028047348 scopus 로고
    • A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane
    • Kusters R., Breukink E., Gallusser A., Kuhn A., de Kruijff B. A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane. J. Biol. Chem. 269:1994;1560-1563
    • (1994) J. Biol. Chem. , vol.269 , pp. 1560-1563
    • Kusters, R.1    Breukink, E.2    Gallusser, A.3    Kuhn, A.4    De Kruijff, B.5
  • 75
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat are required to initiate membrane insertion
    • Kuhn A., Kreil G., Wickner W. Both hydrophobic domains of M13 procoat are required to initiate membrane insertion. EMBO J. 5:1986;3681-3685
    • (1986) EMBO J. , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 76
    • 0030050901 scopus 로고    scopus 로고
    • Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence
    • Soekarjo M., Eisenhawer M., Kuhn A., Vogel H. Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence. Biochemistry. 35:1996;1232-1241
    • (1996) Biochemistry , vol.35 , pp. 1232-1241
    • Soekarjo, M.1    Eisenhawer, M.2    Kuhn, A.3    Vogel, H.4
  • 77
    • 0022398528 scopus 로고
    • M13 procoat inserts into liposomes in the absence of other membrane proteins
    • Geller B.L., Wickner W. M13 procoat inserts into liposomes in the absence of other membrane proteins. J. Biol. Chem. 260:1985;13281-13285
    • (1985) J. Biol. Chem. , vol.260 , pp. 13281-13285
    • Geller, B.L.1    Wickner, W.2
  • 78
    • 0023644197 scopus 로고
    • Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure
    • Kuhn A. Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure. Science. 238:1987;1413-1415
    • (1987) Science , vol.238 , pp. 1413-1415
    • Kuhn, A.1
  • 79
    • 0025697080 scopus 로고
    • Bacteriophages M13 and Pf3 tell us how proteins insert into the membrane
    • Kuhn A., Rohrer J., Gallusser A. Bacteriophages M13 and Pf3 tell us how proteins insert into the membrane. J. Struct. Biol. 104:1990;38-43
    • (1990) J. Struct. Biol. , vol.104 , pp. 38-43
    • Kuhn, A.1    Rohrer, J.2    Gallusser, A.3
  • 80
    • 0027942129 scopus 로고
    • Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly
    • Cao G., Cheng S., Whitley P., von-Heijne G., Kuhn A., Dalbey R.E. Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly. J. Biol. Chem. 269:1994;26898-26903
    • (1994) J. Biol. Chem. , vol.269 , pp. 26898-26903
    • Cao, G.1    Cheng, S.2    Whitley, P.3    Von-Heijne, G.4    Kuhn, A.5    Dalbey, R.E.6
  • 82
    • 0034732952 scopus 로고    scopus 로고
    • Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins
    • Ridder A.N.J.A., Morein S., Stam J.G., Kuhn A., de Kruijff B., Killian J.A. Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins. Biochemistry. 39:2000;6521-6528
    • (2000) Biochemistry , vol.39 , pp. 6521-6528
    • Ridder, A.N.J.A.1    Morein, S.2    Stam, J.G.3    Kuhn, A.4    De Kruijff, B.5    Killian, J.A.6
  • 83
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena C., Williams K.A., Deber C.M., Reithmeier R.A. Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 229:1993;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.4
  • 84
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:1996;842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 85
    • 0032406838 scopus 로고    scopus 로고
    • Statistical analysis of predicted transmembrane alpha-helices
    • Arkin I.T., Brunger A.T. Statistical analysis of predicted transmembrane alpha-helices. Biochim. Biophys. Acta. 1429:1998;113-128
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 113-128
    • Arkin, I.T.1    Brunger, A.T.2
  • 86
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne G. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:1986;3021-3027
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 87
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G., Gavel Y. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:1988;671-678
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 88
    • 0025285274 scopus 로고
    • Positively charged residues are important determinants of membrane protein topology
    • Dalbey R.E. Positively charged residues are important determinants of membrane protein topology. Trends Biochem. Sci. 15:1990;253-257
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 253-257
    • Dalbey, R.E.1
  • 89
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • van Klompenburg W., Nilsson I., von Heijne G., de Kruijff B. Anionic phospholipids are determinants of membrane protein topology. EMBO J. 16:1997;4261-4266
    • (1997) EMBO J. , vol.16 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 90
    • 0034986771 scopus 로고    scopus 로고
    • Anionic lipids stimulate Sec-independent insertion of a membrane protein lacking charged amino acid side chains
    • Ridder A.N.J.A., Kuhn A., Killian J.A., de Kruijff B. Anionic lipids stimulate Sec-independent insertion of a membrane protein lacking charged amino acid side chains. EMBO Rep. 2:2001;403-408
    • (2001) EMBO Rep. , vol.2 , pp. 403-408
    • Ridder, A.N.J.A.1    Kuhn, A.2    Killian, J.A.3    De Kruijff, B.4
  • 91
    • 0037117758 scopus 로고    scopus 로고
    • Importance of hydrophobic matching for spontaneous insertion of a single-spanning membrane protein
    • Ridder A.N.J.A., van de Hoef W., Stam J.G., Kuhn A., de Kruijff B., Killian J.A. Importance of hydrophobic matching for spontaneous insertion of a single-spanning membrane protein. Biochemistry. 41:2002;4946-4952
    • (2002) Biochemistry , vol.41 , pp. 4946-4952
    • Ridder, A.N.J.A.1    Van De Hoef, W.2    Stam, J.G.3    Kuhn, A.4    De Kruijff, B.5    Killian, J.A.6
  • 94
    • 0037040894 scopus 로고    scopus 로고
    • Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion
    • Chen M., Samuelson J.C., Jiang F., Müller M., Kuhn A., Dalbey R.E. Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion. J. Biol. Chem. 277:2002;7670-7675
    • (2002) J. Biol. Chem. , vol.277 , pp. 7670-7675
    • Chen, M.1    Samuelson, J.C.2    Jiang, F.3    Müller, M.4    Kuhn, A.5    Dalbey, R.E.6
  • 95
    • 0038268750 scopus 로고    scopus 로고
    • Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: Different YidC structural requirements for membrane protein insertion
    • Chen M., Xie K., Nouwen N., Driessen A.J., Dalbey R.E. Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YidC structural requirements for membrane protein insertion. J. Biol. Chem. 278:2003;23295-23300
    • (2003) J. Biol. Chem. , vol.278 , pp. 23295-23300
    • Chen, M.1    Xie, K.2    Nouwen, N.3    Driessen, A.J.4    Dalbey, R.E.5
  • 97
    • 0026516666 scopus 로고
    • Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion
    • Lee J.I., Kuhn A., Dalbey R.E. Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion. J. Biol. Chem. 267:1992;938-943
    • (1992) J. Biol. Chem. , vol.267 , pp. 938-943
    • Lee, J.I.1    Kuhn, A.2    Dalbey, R.E.3
  • 98
    • 0030803823 scopus 로고    scopus 로고
    • In vitro membrane integration of leader peptidase depends on the Sec machinery and anionic phospholipids and can occur post-translationally
    • van Klompenburg W., Ridder A.N.J.A., van Raalte A.L.J., Killian J.A., von Heijne G., de Kruijff B. In vitro membrane integration of leader peptidase depends on the Sec machinery and anionic phospholipids and can occur post-translationally. FEBS Lett. 413:1997;109-114
    • (1997) FEBS Lett. , vol.413 , pp. 109-114
    • Van Klompenburg, W.1    Ridder, A.N.J.A.2    Van Raalte, A.L.J.3    Killian, J.A.4    Von Heijne, G.5    De Kruijff, B.6
  • 100
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature. 341:1989;456-458
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 101
    • 0026529067 scopus 로고
    • Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli
    • Andersson H., Bakker E., von Heijne G. Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli. J. Biol. Chem. 267:1992;1491-1495
    • (1992) J. Biol. Chem. , vol.267 , pp. 1491-1495
    • Andersson, H.1    Bakker, E.2    Von Heijne, G.3
  • 102
    • 0028364507 scopus 로고
    • + on the translocation of charged residues explain the 'positive inside' rule
    • + on the translocation of charged residues explain the 'positive inside' rule. EMBO J. 13:1994;2267-2272
    • (1994) EMBO J. , vol.13 , pp. 2267-2272
    • Andersson, H.1    Von Heijne, G.2
  • 104
    • 0029385475 scopus 로고
    • A quantitative assay to determine the amount of signal peptidase I in E. coli and the orientation of membrane vesicles
    • vanKlompenburg W., Whitley P., Diemel R., von Heijne G., de Kruijff B. A quantitative assay to determine the amount of signal peptidase I in E. coli and the orientation of membrane vesicles. Mol. Membr. Biol. 12:1995;349-353
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 349-353
    • Vanklompenburg, W.1    Whitley, P.2    Diemel, R.3    Von Heijne, G.4    De Kruijff, B.5
  • 106
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel M., Dalbey R.E., Strynadka N.C.J. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature. 396:1998;186-190
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 107
    • 0035859890 scopus 로고    scopus 로고
    • Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase
    • van den Brink-van der Laan E., Dalbey R.E., Demel R.A., Killian J.A., de Kruijff B. Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase. Biochemistry. 40:2001;9677-9684
    • (2001) Biochemistry , vol.40 , pp. 9677-9684
    • Van Den Brink-Van Der Laan, E.1    Dalbey, R.E.2    Demel, R.A.3    Killian, J.A.4    De Kruijff, B.5
  • 108
  • 111
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA-Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes D.M., Cuello L.G., Perozo E. Molecular architecture of full-length KcsA-Role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117:2001;165-180
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 112
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu Y.S., Sompornpisut P., Perozo E. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8:2001;883-887
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.1    Sompornpisut, P.2    Perozo, E.3
  • 115
    • 0034303479 scopus 로고    scopus 로고
    • Efficient membrane assembly of the KcsA potassium channel in Escherichia coli requires the protonmotive force
    • van Dalen A., Schrempf H., Killian J.A., de Kruijff B. Efficient membrane assembly of the KcsA potassium channel in Escherichia coli requires the protonmotive force. EMBO Rep. 1:2000;340-346
    • (2000) EMBO Rep. , vol.1 , pp. 340-346
    • Van Dalen, A.1    Schrempf, H.2    Killian, J.A.3    De Kruijff, B.4
  • 117
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson I.M., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268:1993;5798-57801
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-57801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 120
    • 0034696954 scopus 로고    scopus 로고
    • Pore mutations affecting tetrameric assembly and functioning of the potassium channel KcsA from Streptomyces lividans
    • Splitt H., Meuser D., Borovok I., Betzler M., Schrempf H. Pore mutations affecting tetrameric assembly and functioning of the potassium channel KcsA from Streptomyces lividans. FEBS Lett. 472:2000;83-87
    • (2000) FEBS Lett. , vol.472 , pp. 83-87
    • Splitt, H.1    Meuser, D.2    Borovok, I.3    Betzler, M.4    Schrempf, H.5
  • 122
    • 85041133119 scopus 로고    scopus 로고
    • Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle
    • Herskovits A.A., Bibi E. Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4621-4626
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4621-4626
    • Herskovits, A.A.1    Bibi, E.2
  • 123
    • 0029790978 scopus 로고    scopus 로고
    • In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force
    • Bassilana M., Gwizdek C. In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force. EMBO J. 15:1996;5202-5208
    • (1996) EMBO J. , vol.15 , pp. 5202-5208
    • Bassilana, M.1    Gwizdek, C.2
  • 124
    • 0038409063 scopus 로고    scopus 로고
    • The sensor protein KdpD inserts into the Escherichia coli membrane independent of the Sec translocase and YidC
    • Facey S.J., Kuhn A. The sensor protein KdpD inserts into the Escherichia coli membrane independent of the Sec translocase and YidC. Eur. J. Biochem. 270:2003;1724-1734
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1724-1734
    • Facey, S.J.1    Kuhn, A.2
  • 125
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 126
    • 0037077723 scopus 로고    scopus 로고
    • Influence of lipids on membrane assembly and stability of the potassium channel KcsA
    • van Dalen A., Hegger S., Killian J.A., de Kruijff B. Influence of lipids on membrane assembly and stability of the potassium channel KcsA. FEBS Lett. 525:2002;33-38
    • (2002) FEBS Lett. , vol.525 , pp. 33-38
    • Van Dalen, A.1    Hegger, S.2    Killian, J.A.3    De Kruijff, B.4
  • 130
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta. 1612:2003;1-40
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 131
    • 0032530656 scopus 로고    scopus 로고
    • Phospholipid-assisted protein folding: Phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease
    • Bogdanov M., Dowhan W. Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease. EMBO J. 17:1998;5255-5264
    • (1998) EMBO J. , vol.17 , pp. 5255-5264
    • Bogdanov, M.1    Dowhan, W.2
  • 132
    • 0033617356 scopus 로고    scopus 로고
    • Phospholipid-assisted refolding of an integral membrane protein - Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone
    • Bogdanov M., Umeda M., Dowhan W. Phospholipid-assisted refolding of an integral membrane protein - Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone. J. Biol. Chem. 274:1999;12339-12345
    • (1999) J. Biol. Chem. , vol.274 , pp. 12339-12345
    • Bogdanov, M.1    Umeda, M.2    Dowhan, W.3
  • 133
    • 0036566310 scopus 로고    scopus 로고
    • A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
    • Bogdanov M., Heacock P.N., Dowhan W. A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition. EMBO J. 21:2002;2107-2116
    • (2002) EMBO J. , vol.21 , pp. 2107-2116
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 134
    • 0036845373 scopus 로고    scopus 로고
    • Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition
    • Wang X., Bogdanov M., Dowhan W. 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
  • 135
    • 0037328667 scopus 로고    scopus 로고
    • Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine biosynthetic machinery with the prohibitin complex of Saccharomyces cerevisiae
    • Birner R., Nebauer R., Schneiter R., Daum G. Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine biosynthetic machinery with the prohibitin complex of Saccharomyces cerevisiae. Mol. Biol. Cell. 14:2003;370-383
    • (2003) Mol. Biol. Cell , vol.14 , pp. 370-383
    • Birner, R.1    Nebauer, R.2    Schneiter, R.3    Daum, G.4


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