메뉴 건너뛰기




Volumn 235, Issue 1-2, 1996, Pages 207-214

Influence of the signal sequence and chaperone SecB on the interaction between precursor protein prePhoE and phospholipids

Author keywords

lipid monolayer; lipid protein interaction; precursor; SecB; signal sequence

Indexed keywords

OUTER MEMBRANE PROTEIN; PHOSPHOLIPID; PROTEIN PRECURSOR;

EID: 0030041516     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00207.x     Document Type: Article
Times cited : (8)

References (41)
  • 1
    • 58149208032 scopus 로고
    • Protein translocation in Escherichia coli
    • Arkowitz, R. A. & Bassilana, M. (1994) Protein translocation in Escherichia coli, Biochim. Biophys. Acta 1197, 311-343.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 311-343
    • Arkowitz, R.A.1    Bassilana, M.2
  • 2
    • 0028128453 scopus 로고
    • Signal Peptides: Exquisitely designed transport promoters
    • Izard, J. W. & Kendall, D. A. (1994) Signal Peptides: exquisitely designed transport promoters, Mol. Micobiol. 13, 765-773.
    • (1994) Mol. Micobiol. , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 3
    • 0027891806 scopus 로고
    • SecB: A molecular chaperone of Escherichia coli protein secretion pathway
    • Collier, D. N. (1993) SecB: A molecular chaperone of Escherichia coli protein secretion pathway, Adv. Protein Chem. 44, 151-193.
    • (1993) Adv. Protein Chem. , vol.44 , pp. 151-193
    • Collier, D.N.1
  • 4
    • 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. (1990) The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane, Cell 63, 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
  • 6
    • 0023878031 scopus 로고
    • Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
    • de Vrije, T., de Swart, R. L., Dowhan, W., Tommassen, J. & de Kruijff, B. (1988) Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes, Nature 334, 173-175.
    • (1988) Nature , vol.334 , pp. 173-175
    • De Vrije, T.1    De Swart, R.L.2    Dowhan, W.3    Tommassen, J.4    De Kruijff, B.5
  • 7
    • 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. (1990) The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins, Cell 60, 271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 8
    • 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. (1992) SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: A monolayer study, Biochemistry 31, 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
  • 9
    • 0025299110 scopus 로고
    • Biophysical studies of signal peptides: Implications for signal sequence functions and the involvement of lipid in protein export
    • Jones, J. D., McKnight, C. J. & Gierasch, L. M. (1990) Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein export, J. Bioenerg. Biomembr. 22, 213-232.
    • (1990) J. Bioenerg. Biomembr. , vol.22 , pp. 213-232
    • Jones, J.D.1    McKnight, C.J.2    Gierasch, L.M.3
  • 10
    • 0022415759 scopus 로고
    • In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides
    • Briggs, M. S., Gierasch, L. M., Zlotnick, A., Lear, J. D. & DeGrado, W. F. (1985) In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides, Science 228, 1096-1098.
    • (1985) Science , vol.228 , pp. 1096-1098
    • Briggs, M.S.1    Gierasch, L.M.2    Zlotnick, A.3    Lear, J.D.4    DeGrado, W.F.5
  • 11
    • 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. (1988) 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, 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
  • 12
    • 0025180750 scopus 로고
    • Lipid and peptide specificities in signal peptide-lipid interactions in model membranes
    • Demel, R. A., Goormaghtigh, E. & de Kruijff, B. (1990) Lipid and peptide specificities in signal peptide-lipid interactions in model membranes, Biochim. Biophys. Acta 1027, 155-162.
    • (1990) Biochim. Biophys. Acta , vol.1027 , pp. 155-162
    • Demel, R.A.1    Goormaghtigh, E.2    De Kruijff, B.3
  • 13
  • 14
    • 0025196904 scopus 로고
    • Tryptophan fluorescence study on the interaction of the signal peptide of the Escherichia coliouter membrane protein PhoE with model membranes
    • Killian, J. A., Keller, R. C. A., Struyve, M., de Kroon, A. I. P. M., Tommassen, J. & de Kruijff, B. (1990) Tryptophan fluorescence study on the interaction of the signal peptide of the Escherichia coliouter membrane protein PhoE with model membranes, Biochemistry 29, 8131-8137.
    • (1990) Biochemistry , vol.29 , pp. 8131-8137
    • Killian, J.A.1    Keller, R.C.A.2    Struyve, M.3    De Kroon, A.I.P.M.4    Tommassen, J.5    De Kruijff, B.6
  • 15
  • 16
    • 0026573926 scopus 로고
    • Anionic phospholipids are essential for α-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles
    • Keller, R. C. A., Killian, J. A. & de Kruijff, B. (1992) Anionic phospholipids are essential for α-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles, Biochemistry 31, 1672-1677.
    • (1992) Biochemistry , vol.31 , pp. 1672-1677
    • Keller, R.C.A.1    Killian, J.A.2    De Kruijff, B.3
  • 17
    • 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. (1989) Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties, J. Biol. Chem. 264, 17293-17297.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17293-17297
    • McKnight, C.J.1    Briggs, M.S.2    Gierasch, L.M.3
  • 18
    • 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. (1994) A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane, J. Biol. Chem. 269, 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
  • 19
    • 0027248503 scopus 로고
    • OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidyl-glycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane
    • Phoenix, D. A., Kusters, R., Hikita, C. Mizushima, S. & de Kruijff, B. (1993) OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidyl-glycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane, J. Biol. Chem. 268, 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
  • 20
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M. W., Brunner, J. & Dobberstein, B. (1995) The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer, Cell 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 21
    • 0028247158 scopus 로고
    • Requirement for conformational flexibility in the signal sequence of precursor protein
    • Nouwen, N., Tommassen, J. & de Kruijff, B. (1994) Requirement for conformational flexibility in the signal sequence of precursor protein, J. Biol. Chem. 269, 16029-16033.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16029-16033
    • Nouwen, N.1    Tommassen, J.2    De Kruijff, B.3
  • 22
    • 0019413905 scopus 로고
    • E. coli mutant pleiotropically defective in the export of secreted proteins
    • Oliver, D. B. & Beckwith, J. (1981) E. coli mutant pleiotropically defective in the export of secreted proteins, Cell 25, 765-772.
    • (1981) Cell , vol.25 , pp. 765-772
    • Oliver, D.B.1    Beckwith, J.2
  • 23
    • 0024790857 scopus 로고
    • SecB protein stabilizes a translocation-competent state of purified prePhoE protein
    • Kusters, R., de Vrije, T., Breukink, E. & de Kruijff, B. (1989) SecB protein stabilizes a translocation-competent state of purified prePhoE protein, J. Biol. Chem. 264, 20827-20830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20827-20830
    • Kusters, R.1    De Vrije, T.2    Breukink, E.3    De Kruijff, B.4
  • 24
    • 2642634461 scopus 로고
    • Purified SecB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
    • Weiss, J. B., Ray, P. H. & Bassford, P. J. (1988) Purified SecB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro, Proc. Natl Acad. Sci. USA 85, 8978-8982.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8978-8982
    • Weiss, J.B.1    Ray, P.H.2    Bassford, P.J.3
  • 25
    • 0021992333 scopus 로고
    • Alteration of phospholipid composition by combined defeccts in phosphatidylserine and cardiolipin synthase and physiological consequences in Escherichia coli
    • Shibuya, I., Miyasaki, C. & Ohta, A. (1985) Alteration of phospholipid composition by combined defeccts in phosphatidylserine and cardiolipin synthase and physiological consequences in Escherichia coli, J. Bacteriol 161, 1086-1092.
    • (1985) J. Bacteriol , vol.161 , pp. 1086-1092
    • Shibuya, I.1    Miyasaki, C.2    Ohta, A.3
  • 26
    • 0026577035 scopus 로고
    • Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein
    • de Cock, H., Overeem, W. & Tommassen, J. (1992) Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein, J. Mol. Biol. 224, 369-379.
    • (1992) J. Mol. Biol. , vol.224 , pp. 369-379
    • De Cock, H.1    Overeem, W.2    Tommassen, J.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014784107 scopus 로고
    • Structural investigations on the 2-keto-3-deoxyoctonate region of lipopolisaccharides
    • Droge, W., Lehmann, V., Luderitz, O. & Westphal, O. (1967) Structural investigations on the 2-keto-3-deoxyoctonate region of lipopolisaccharides, Eur. J. Biochem. 14, 175-184.
    • (1967) Eur. J. Biochem. , vol.14 , pp. 175-184
    • Droge, W.1    Lehmann, V.2    Luderitz, O.3    Westphal, O.4
  • 29
    • 0022032619 scopus 로고
    • Monoclonal antibodies directed against the cell-surface-exposed part of PhoE pore protein of the Escherichia coli K-12 outer membrane
    • Van der Leij, P., Amesz, H., Thomassen, J. & Lugtenberg, P. (1985) Monoclonal antibodies directed against the cell-surface-exposed part of PhoE pore protein of the Escherichia coli K-12 outer membrane, Eur. J. Biochem. 147, 401-407.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 401-407
    • Van Der Leij, P.1    Amesz, H.2    Thomassen, J.3    Lugtenberg, P.4
  • 30
    • 0022446218 scopus 로고
    • Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12
    • Bosch, D., Leunissen, J., Verbakel, J., de Jong, M., van Erp, H. & Tommassen, J. (1986) Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12, J. Mol. Biol. 189, 449-455.
    • (1986) J. Mol. Biol. , vol.189 , pp. 449-455
    • Bosch, D.1    Leunissen, J.2    Verbakel, J.3    De Jong, M.4    Van Erp, H.5    Tommassen, J.6
  • 31
    • 0025214278 scopus 로고
    • Assembly of an in vitro synthesized outer membrane porin into its stable trimeric configuration
    • de Cock, H., Hendriks, R., de Vrije, T. & Tommassen, J. (1990) Assembly of an in vitro synthesized outer membrane porin into its stable trimeric configuration, J. Biol. Chem. 265, 4646-4651.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4646-4651
    • De Cock, H.1    Hendriks, R.2    De Vrije, T.3    Tommassen, J.4
  • 32
    • 0026687341 scopus 로고
    • In-vitro studies on the folding characteristics of the Escherichia coli precursor protein prePhoE
    • Breukink, E., Kusters, R. & de Kruijff, B. (1992) In-vitro studies on the folding characteristics of the Escherichia coli precursor protein prePhoE, Eur. J. Biochem. 208, 419-425.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 419-425
    • Breukink, E.1    Kusters, R.2    De Kruijff, B.3
  • 33
    • 0016369116 scopus 로고
    • Monolayers-description of use and interaction
    • Demel, R. A. (1974) Monolayers-description of use and interaction, Methods Enzymol 32, 539-545.
    • (1974) Methods Enzymol , vol.32 , pp. 539-545
    • Demel, R.A.1
  • 34
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope, M. J., Bally, M. B., Webb, G. & Cullis, P. R. (1985) Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential, Biochim. Biophys. Acta 812, 55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 36
    • 0023093597 scopus 로고
    • Consequences of the interaction of calcium with dioleoylphosphatidate containing model membranes: Calcium-membrane and membrane-membrane interactions
    • Smaal, E. B., Mandersloot, J. G., Demel, R. A., de Kruijff, B. & de Gier, J. (1987) Consequences of the interaction of calcium with dioleoylphosphatidate containing model membranes: calcium-membrane and membrane-membrane interactions, Biochim. Biophys. Acta 897, 180-190.
    • (1987) Biochim. Biophys. Acta , vol.897 , pp. 180-190
    • Smaal, E.B.1    Mandersloot, J.G.2    Demel, R.A.3    De Kruijff, B.4    De Gier, J.5
  • 37
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the intertacial phospholipid pressure in monolayers
    • Demel, R. A., Geurts van Kessel, W. S. M., Zwaal, R. F. A., Roelofsen, B. & van Deenen, L. L. M. (1975) Relation between various phospholipase actions on human red cell membranes and the intertacial phospholipid pressure in monolayers, Biochim. Biophys. Acta 406, 91-107.
    • (1975) Biochim. Biophys. Acta , vol.406 , pp. 91-107
    • Demel, R.A.1    Geurts Van Kessel, W.S.M.2    Zwaal, R.F.A.3    Roelofsen, B.4    Van Deenen, L.L.M.5
  • 39
    • 0029670438 scopus 로고    scopus 로고
    • + dependency of in vitro protein translocation into E. coli inner membrane vesicles varies with the signal sequence core region composition
    • in the press
    • + dependency of in vitro protein translocation into E. coli inner membrane vesicles varies with the signal sequence core region composition, Mol. Microbiol., in the press.
    • (1996) Mol. Microbiol.
    • Nouwen, N.1    De Kruijff, B.2    Tommussen, J.3
  • 40
    • 0017174518 scopus 로고
    • Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12
    • Lugtenberg, E. J. B. & Peters, R. (1976) Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12, Biochim. Biophys. Acta 441, 38-47.
    • (1976) Biochim. Biophys. Acta , vol.441 , pp. 38-47
    • Lugtenberg, E.J.B.1    Peters, R.2
  • 41
    • 0025239037 scopus 로고
    • In vitro trimerization of outer membrane protein PhoE
    • de Cock, H., Hekstra, D. & Tonimassen, J. (1990) In vitro trimerization of outer membrane protein PhoE, Biochimie (Paris) 72, 177-182.
    • (1990) Biochimie (Paris) , vol.72 , pp. 177-182
    • De Cock, H.1    Hekstra, D.2    Tonimassen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.