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Volumn 15, Issue 3, 2006, Pages 620-627

Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes

Author keywords

Calorimetry; Circular dichroism; Conformational changes; Enzymes; Fluorescence; Hydrodynamics; Membrane associated proteins; Thermodynamics

Indexed keywords

1,2 DIOLEOYLGLYCERO 3 PHOSPHATE(MONOSODIUM); COLICIN E3; DIOLEOYLPHOSPHATIDYLCHOLINE; GLYCEROPHOSPHATE; PHOSPHOLIPID; RIBONUCLEASE; SODIUM CHLORIDE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 33644512106     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051890306     Document Type: Article
Times cited : (23)

References (33)
  • 2
    • 0034702860 scopus 로고    scopus 로고
    • Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry
    • Breukink, E., Ganz, P., de Kruijff, B., and Seelig, J. 2000. Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry. Biochemistry 39: 10247-10254.
    • (2000) Biochemistry , vol.39 , pp. 10247-10254
    • Breukink, E.1    Ganz, P.2    De Kruijff, B.3    Seelig, J.4
  • 3
    • 0030725122 scopus 로고    scopus 로고
    • Interaction of the δ-endotoxin CytA from Bacillus thuringiensis var. israelensis with lipid membranes
    • Butko, P., Huang, F., Pusztai-Carey, M., and Surewicz, W.K. 1997. Interaction of the δ-endotoxin CytA from Bacillus thuringiensis var. israelensis with lipid membranes. Biochemistry 36: 12862-12868.
    • (1997) Biochemistry , vol.36 , pp. 12862-12868
    • Butko, P.1    Huang, F.2    Pusztai-Carey, M.3    Surewicz, W.K.4
  • 4
    • 0034665456 scopus 로고    scopus 로고
    • Inhibition of a ribosome-inactivating ribonuclease: The crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity protein
    • Carr, S., Walker, D., James, R., Kleanthous, C., and Hemmings, A.M. 2000. Inhibition of a ribosome-inactivating ribonuclease: The crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity protein. Struct. Fold. Des. 8: 949-960.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 949-960
    • Carr, S.1    Walker, D.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 6
    • 0037176821 scopus 로고    scopus 로고
    • Binding of ricin A-chain to negatively charged phospholipid vesicles leads to protein structural changes and destabilizes the lipid bilayer
    • Day, P.J., Pinheiro, T.J.T., Roberts, L.M., and Lord, J.M. 2002. Binding of ricin A-chain to negatively charged phospholipid vesicles leads to protein structural changes and destabilizes the lipid bilayer. Biochemistry 41: 2836-2843.
    • (2002) Biochemistry , vol.41 , pp. 2836-2843
    • Day, P.J.1    Pinheiro, T.J.T.2    Roberts, L.M.3    Lord, J.M.4
  • 7
    • 0037066109 scopus 로고    scopus 로고
    • The low lysine content of ricin a chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol
    • Deeks, E.D., Cook, J.P., Day, P.J., Smith, D.C., Roberts, L.M., and Lord, J.M. 2002. The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol. Biochemistry 41: 3405-3413.
    • (2002) Biochemistry , vol.41 , pp. 3405-3413
    • Deeks, E.D.1    Cook, J.P.2    Day, P.J.3    Smith, D.C.4    Roberts, L.M.5    Lord, J.M.6
  • 8
    • 0034643906 scopus 로고    scopus 로고
    • Interaction of albumins from different species with phospholipid liposomes. Multiple binding sites system
    • Dimitrova, M.N., Matsumura, H., Dimitrova, A., and Neitchev, V.Z. 2000. Interaction of albumins from different species with phospholipid liposomes. Multiple binding sites system. Int. J. Biol. Macromol. 27: 187-194.
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 187-194
    • Dimitrova, M.N.1    Matsumura, H.2    Dimitrova, A.3    Neitchev, V.Z.4
  • 10
    • 2342447390 scopus 로고    scopus 로고
    • Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein
    • Graille, M., Mora, L., Buckingham, R.H., Van Tilbeurgh, H., and De Zamaroczy, M. 2004. Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein. EMBO J. 23: 1474-1482.
    • (2004) EMBO J. , vol.23 , pp. 1474-1482
    • Graille, M.1    Mora, L.2    Buckingham, R.H.3    Van Tilbeurgh, H.4    De Zamaroczy, M.5
  • 11
    • 0034700142 scopus 로고    scopus 로고
    • Effect of the protein import machinery at the mitochondrial surface on precursor stability
    • Huang, S., Murphy, S., and Matouschek, A. 2000. Effect of the protein import machinery at the mitochondrial surface on precursor stability. Proc. Natl. Acad. Sci. 97: 12991-12996.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 12991-12996
    • Huang, S.1    Murphy, S.2    Matouschek, A.3
  • 12
    • 0036221085 scopus 로고    scopus 로고
    • Protein unfolding by the mitochondrial membrane potential
    • Huang, S., Ratliff, K.S., and Matouschek, A. 2002. Protein unfolding by the mitochondrial membrane potential. Nat. Struct. Biol. 9: 301-307.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 301-307
    • Huang, S.1    Ratliff, K.S.2    Matouschek, A.3
  • 13
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by E group nuclease colicins
    • James, R., Penfold, C.N., Moore, G.R., and Kleanthous, C. 2002. Killing of E. coli cells by E group nuclease colicins. Biochimie 84: 381-389.
    • (2002) Biochimie , vol.84 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 14
    • 0002650761 scopus 로고    scopus 로고
    • Cytoplasmic membrane
    • eds. R. Curtis III et al., American Society for Microbiology Press, Washington, DC
    • Kadner, R.J. 1996. Cytoplasmic membrane. In Escherichia coli and Salmonella: Cellular and molecular biology (eds. R. Curtis III et al.), pp. 58-87. American Society for Microbiology Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 58-87
    • Kadner, R.J.1
  • 18
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W.K. 1999. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274: 36859-36865.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 20
    • 2542441795 scopus 로고    scopus 로고
    • Destabilization of the colicin E9 endonuclease domain by interaction with negatively charged phospholipids: Implications for colicin translocation into bacteria
    • Mosbahi, K.,Walker, D., Lea, E., Moore, G.R., James, R., and Kleanthous, C. 2004. Destabilization of the colicin E9 endonuclease domain by interaction with negatively charged phospholipids: Implications for colicin translocation into bacteria. J. Biol. Chem. 279: 22145-22151.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22145-22151
    • Mosbahi, K.1    Walker, D.2    Lea, E.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 21
    • 0027464626 scopus 로고
    • pH-dependent stability and membrane interaction of the pore-forming domain of colicin A
    • Muga, A., Gonzalez-Manas, J.M., Lakey, J.H., Pattus, F., and Surewicz, W.K. 1993. pH-dependent stability and membrane interaction of the pore-forming domain of colicin A. J. Biol. Chem. 268: 1553-1557.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1553-1557
    • Muga, A.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4    Surewicz, W.K.5
  • 22
    • 0033605708 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease targeting specific transfer RNA anticodons
    • Ogawa, T., Tomita, K., Ueda, T., Watanabe, K., Uozumi, T., and Masaki, H. 1999. A cytotoxic ribonuclease targeting specific transfer RNA anticodons. Science 283: 2097-2100.
    • (1999) Science , vol.283 , pp. 2097-2100
    • Ogawa, T.1    Tomita, K.2    Ueda, T.3    Watanabe, K.4    Uozumi, T.5    Masaki, H.6
  • 23
    • 0018719041 scopus 로고
    • Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes
    • Olson, F., Hunt, C.A., Szoka, F.C., Vail, W.J., and Papahadjopoulos, D. 1979. Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes. Biochim. Biophys. Acta. 557: 9-23.
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 9-23
    • Olson, F.1    Hunt, C.A.2    Szoka, F.C.3    Vail, W.J.4    Papahadjopoulos, D.5
  • 25
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera, N. and Pinheiro, T.J. 2002. Binding of prion protein to lipid membranes and implications for prion conversion. J. Mol. Biol. 315: 1241-1256.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 26
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze, S.R., Ho, A., Vocero-Akbani, A., and Dowdy, S.F. 1999. In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science 285: 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 27
    • 0032879634 scopus 로고    scopus 로고
    • Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
    • Simpson, J.C., Roberts, L.M., Romisch, K., Davey, J., Wolf, D.H., and Lord, J.M. 1999. Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast. FEBS Lett. 459: 80-84.
    • (1999) FEBS Lett. , vol.459 , pp. 80-84
    • Simpson, J.C.1    Roberts, L.M.2    Romisch, K.3    Davey, J.4    Wolf, D.H.5    Lord, J.M.6
  • 28
    • 0037022295 scopus 로고    scopus 로고
    • Translocation of a functional protein by a voltage-dependent ion channel
    • Slatin, S.L., Nardi, A., Jakes, K.S., Baty, D., and Duché, D. 2002. Translocation of a functional protein by a voltage-dependent ion channel. Proc. Natl. Acad. Sci. 99: 1286-1291.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 1286-1291
    • Slatin, S.L.1    Nardi, A.2    Jakes, K.S.3    Baty, D.4    Duché, D.5
  • 29
    • 0034682503 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease which specifically cleaves four isoaccepting arginine tRNAs at their anticodon loops
    • Tomita, K., Ogawa, T., Uozumi, T., Watanabe, K., and Masaki, H. 2000. A cytotoxic ribonuclease which specifically cleaves four isoaccepting arginine tRNAs at their anticodon loops. Proc. Natl. Acad. Sci. 97: 8278-8283.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8278-8283
    • Tomita, K.1    Ogawa, T.2    Uozumi, T.3    Watanabe, K.4    Masaki, H.5
  • 30
    • 0345701261 scopus 로고    scopus 로고
    • Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3
    • Walker, D., Moore, G.R., James, R., and Kleanthous, C. 2003. Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3. Biochemistry 42: 4161-4171.
    • (2003) Biochemistry , vol.42 , pp. 4161-4171
    • Walker, D.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 31
    • 2442713814 scopus 로고    scopus 로고
    • Identification of the catalytic motif of the ribosome inactivating cytotoxin colicin E3
    • Walker, D., Lancaster, L., James, R., and Kleanthous, C. 2004. Identification of the catalytic motif of the ribosome inactivating cytotoxin colicin E3. Protein Sci. 13: 1603-1611.
    • (2004) Protein Sci. , vol.13 , pp. 1603-1611
    • Walker, D.1    Lancaster, L.2    James, R.3    Kleanthous, C.4
  • 32
    • 0037064252 scopus 로고    scopus 로고
    • Colicin crystal structures: Pathways and mechanisms for colicin insertion into membranes
    • Zakharov, S.D. and Cramer, W.A. 2002. Colicin crystal structures: Pathways and mechanisms for colicin insertion into membranes. Biochim. Biophys. Acta 1565: 333-346.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 333-346
    • Zakharov, S.D.1    Cramer, W.A.2
  • 33
    • 0043166977 scopus 로고    scopus 로고
    • Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis
    • Ziegler, A., Blatter, X.L., Seelig, A., and Seelig, J. 2003. Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis. Biochemistry 42: 9185-9194.
    • (2003) Biochemistry , vol.42 , pp. 9185-9194
    • Ziegler, A.1    Blatter, X.L.2    Seelig, A.3    Seelig, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.