메뉴 건너뛰기




Volumn 53, Issue 5, 1999, Pages 477-485

Conformational changes of urea-denatured colicin E1 induced by phospholipid membranes

Author keywords

Colicins; Lipid protein interaction; Protein folding; Protein insertion

Indexed keywords

COLICIN E1; PHOSPHOLIPID;

EID: 0033066176     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00041.x     Document Type: Article
Times cited : (2)

References (25)
  • 1
    • 0028176343 scopus 로고
    • Interaction of phospholipids with proteins and peptides
    • Cserhati, T. & Szogyi, M. (1994) Interaction of phospholipids with proteins and peptides. Int. J. Biochem. 26, 1-18.
    • (1994) Int. J. Biochem. , vol.26 , pp. 1-18
    • Cserhati, T.1    Szogyi, M.2
  • 4
    • 0021759126 scopus 로고
    • Dependence of the activity of colicin E1 in artificial membrane vesicles on pH, membrane potential, and vesicles size
    • Davidson, V.L., Cramer, W.A., Bishop, L.J. & Brunden, K.R. (1984) Dependence of the activity of colicin E1 in artificial membrane vesicles on pH, membrane potential, and vesicles size. J. Biol. Chem. 259, 594-600.
    • (1984) J. Biol. Chem. , vol.259 , pp. 594-600
    • Davidson, V.L.1    Cramer, W.A.2    Bishop, L.J.3    Brunden, K.R.4
  • 6
    • 0027447891 scopus 로고
    • Colicin E1 binding to membranes: Time-resolved studies of spin-labeled mutants
    • Shin, Y.K., Levinthal, C., Levinthal, F. & Hubbell, W.L. (1993) Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants. Science 259, 960-963.
    • (1993) Science , vol.259 , pp. 960-963
    • Shin, Y.K.1    Levinthal, C.2    Levinthal, F.3    Hubbell, W.L.4
  • 7
    • 0022553762 scopus 로고
    • Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E Coli
    • Randall, L.L. & Hardy, S.J.S. (1986) Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell 46, 921-928.
    • (1986) Cell , vol.46 , pp. 921-928
    • Randall, L.L.1    Hardy, S.J.S.2
  • 8
    • 0024294402 scopus 로고
    • The antifolding activity of secB promotes the export of the E coli maltose-binding protein
    • Collier, D.N., Bankaitis, V.A., Weiss, J.B. & Bassford, P.J. (1988) The antifolding activity of secB promotes the export of the E. coli maltose-binding protein. Cell 53, 273-283.
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, V.A.2    Weiss, J.B.3    Bassford, P.J.4
  • 9
    • 0023761756 scopus 로고
    • Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
    • Bochkareva, E.S., Lissin, N.M. & Girshovich, A.S. (1988) Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336, 254-257.
    • (1988) Nature , vol.336 , pp. 254-257
    • Bochkareva, E.S.1    Lissin, N.M.2    Girshovich, A.S.3
  • 10
    • 0023989329 scopus 로고
    • Import of proteins into mitochondria
    • Eilers, M., Hwang, S. & Schatz, G. (1988) Import of proteins into mitochondria. EMBO J. 7, 1139-1145.
    • (1988) EMBO J. , vol.7 , pp. 1139-1145
    • Eilers, M.1    Hwang, S.2    Schatz, G.3
  • 11
    • 0024961641 scopus 로고
    • Structure of the membrane pore-forming fragment of colicin A
    • Parker, M.W., Pattus, F., Tucker, A.D. & Tsemoglou, D. (1989) Structure of the membrane pore-forming fragment of colicin A. Nature 337, 93-96.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsemoglou, D.4
  • 12
    • 0025369969 scopus 로고
    • Insights into membrane insertion based on studies of colicins
    • Parker, M.W., Tucker, A.D., Tsemoglou, D. & Pattus, F. (1990) Insights into membrane insertion based on studies of colicins. TIBS 15, 126-129.
    • (1990) TIBS , vol.15 , pp. 126-129
    • Parker, M.W.1    Tucker, A.D.2    Tsemoglou, D.3    Pattus, F.4
  • 13
    • 0025763316 scopus 로고
    • Fluorescence energy transfer distance measurements using site-directed single cysteine mutants
    • Lakey, J.H., Baty, D. & Pattus, F. (1991) Fluorescence energy transfer distance measurements using site-directed single cysteine mutants. J. Mol. Biol. 218, 639-653.
    • (1991) J. Mol. Biol. , vol.218 , pp. 639-653
    • Lakey, J.H.1    Baty, D.2    Pattus, F.3
  • 14
    • 0345188286 scopus 로고
    • Acidic pH requirement for insertion of colicin E1 into artificial membrane vesicles: Relevance to the mechanism of colicins and certain toxins
    • Davidson, V.L., Brunden, K.R. & Cramer, W.A. (1985) Acidic pH requirement for insertion of colicin E1 into artificial membrane vesicles: relevance to the mechanism of colicins and certain toxins. Proc. Natl Acad. Sci. USA 82, 1386-1390.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1386-1390
    • Davidson, V.L.1    Brunden, K.R.2    Cramer, W.A.3
  • 15
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn, O.B. (1987) Protein folding: hypotheses and experiments. J. Protein Chem. 6, 273-293.
    • (1987) J. Protein Chem. , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 16
    • 0025314326 scopus 로고
    • On the nature of the structural change of the colicin E1 channel peptide necessary for its translocation-competent state
    • Merrill, A.R., Cohen, F.S. & Cramer, W.A. (1990) On the nature of the structural change of the colicin E1 channel peptide necessary for its translocation-competent state. Biochemistry 29, 5829-5836.
    • (1990) Biochemistry , vol.29 , pp. 5829-5836
    • Merrill, A.R.1    Cohen, F.S.2    Cramer, W.A.3
  • 17
    • 0028206797 scopus 로고
    • The colicin E1 interaction-competent state: Detection of sructural changes using fluorescence resonance energy transfer
    • Steer, B.A. & Merrill, A.R. (1994) The colicin E1 interaction-competent state: detection of sructural changes using fluorescence resonance energy transfer. Biochemistry 33, 1108-1115.
    • (1994) Biochemistry , vol.33 , pp. 1108-1115
    • Steer, B.A.1    Merrill, A.R.2
  • 18
    • 0026541379 scopus 로고
    • Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed
    • Benedetti, H., Lloubes, R., Lazdunski, L. & Letellier, L. (1992) Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed. EMBO J. 11, 441-447.
    • (1992) EMBO J. , vol.11 , pp. 441-447
    • Benedetti, H.1    Lloubes, R.2    Lazdunski, L.3    Letellier, L.4
  • 19
    • 0027938907 scopus 로고
    • Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • Duche, D., Baty, D., Chartier, M. & Letellier, L. (1994) Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering. J. Biol. Chem. 269, 24820-24825.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24820-24825
    • Duche, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 20
    • 0020478894 scopus 로고
    • On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization
    • Dankert, J.R., Uratani, Y., Grabau, C., Cramer, W.A. & Hermodson, M. (1982) On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization. J. Biol. Chem. 257, 3857-3863.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3857-3863
    • Dankert, J.R.1    Uratani, Y.2    Grabau, C.3    Cramer, W.A.4    Hermodson, M.5
  • 21
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence, quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S.S. (1971) Solute perturbation of protein fluorescence, quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10, 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 22
    • 0023052464 scopus 로고
    • Incorporation easily of a synthetic mitochondrial signal peptide into charged and uncharged phospholipid monolayers
    • Tamm, L.K. (1986) Incorporation easily of a synthetic mitochondrial signal peptide into charged and uncharged phospholipid monolayers. Biochemistry 25, 7470-7476.
    • (1986) Biochemistry , vol.25 , pp. 7470-7476
    • Tamm, L.K.1
  • 23
    • 0013632232 scopus 로고
    • Study on the penetration of apocytochrome C into soybean phospholipids monolayer
    • Han, X., Sui, S.-F. & Yang, F. (1993) Study on the penetration of apocytochrome C into soybean phospholipids monolayer. Acta Biophys. Sin. 3, 396-401.
    • (1993) Acta Biophys. Sin. , vol.3 , pp. 396-401
    • Han, X.1    Sui, S.-F.2    Yang, F.3
  • 24
    • 0021237572 scopus 로고
    • Dependence of the conformaion of a colicin E1 channel-forming peptide on acidic pH and solvent polarity
    • Brunden, K.R., Uratani, Y. & Cramer, W.A. (1984) Dependence of the conformaion of a colicin E1 channel-forming peptide on acidic pH and solvent polarity. J. Biol. Chem. 259, 7682-7687.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7682-7687
    • Brunden, K.R.1    Uratani, Y.2    Cramer, W.A.3
  • 25
    • 0028024523 scopus 로고
    • Conformational changes of melittin upon insertion into phospholipid monolayer and vesicle
    • Sui, S.-F., Wu, H., Guo, Y. & Chen, K.-S. (1994) Conformational changes of melittin upon insertion into phospholipid monolayer and vesicle. J. Biochem. 116, 482-487.
    • (1994) J. Biochem. , vol.116 , pp. 482-487
    • Sui, S.-F.1    Wu, H.2    Guo, Y.3    Chen, K.-S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.