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Volumn 8, Issue 2, 1999, Pages 381-393

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state

Author keywords

Apocytochrome c; Collapsed state; Folding intermediates; Folding kinetics; Membrane insertion; Protein folding in membranes

Indexed keywords

APOCYTOCHROME C; APOPROTEIN; CYTOCHROME C; UNCLASSIFIED DRUG;

EID: 0033005315     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.2.381     Document Type: Article
Times cited : (20)

References (55)
  • 1
    • 0031302710 scopus 로고    scopus 로고
    • Folding α-helical membrane proteins: Kinetic studies on bacteriorhodopsin
    • Booth PJ. 1997. Folding α-helical membrane proteins: Kinetic studies on bacteriorhodopsin. Fold Design 2:R85-R92.
    • (1997) Fold Design , vol.2
    • Booth, P.J.1
  • 2
    • 0018065969 scopus 로고
    • Mitochondrial cytochrome c: Preparation and activity of native and chemically modified cytochrome c
    • Brautigan DL, Ferguson-Miller S, Margoliash E. 1978. Mitochondrial cytochrome c: Preparation and activity of native and chemically modified cytochrome c. Methods Enzymol 53:128-191.
    • (1978) Methods Enzymol , vol.53 , pp. 128-191
    • Brautigan, D.L.1    Ferguson-Miller, S.2    Margoliash, E.3
  • 3
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colón W, Elöve GA, Wakem LP, Sherman F, Roder H. 1996. Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry 35:5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 4
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colón W, Roder H. 1996. Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct Biol 3:1019-1025.
    • (1996) Nature Struct Biol , vol.3 , pp. 1019-1025
    • Colón, W.1    Roder, H.2
  • 7
    • 0025092697 scopus 로고
    • The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents. A circular dichroism study
    • de Jongh HHJ, de Kruijff B. 1990. The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents. A circular dichroism study. Biochim Biophys Acta 1029:105-112.
    • (1990) Biochim Biophys Acta , vol.1029 , pp. 105-112
    • De Jongh, H.H.J.1    De Kruijff, B.2
  • 8
    • 0026603603 scopus 로고
    • A water lipid interface induces a highly dynamic folded state in apocytochrome c which may represent a common folding intermediate
    • de Jongh HHJ, Killian JA, de Kruijff B. 1992. A water lipid interface induces a highly dynamic folded state in apocytochrome c which may represent a common folding intermediate. Biochemistry 31:1636-1643.
    • (1992) Biochemistry , vol.31 , pp. 1636-1643
    • De Jongh, H.H.J.1    Killian, J.A.2    De Kruijff, B.3
  • 9
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. 1997. From Levinthal to pathways to funnels. Nature Struct Biol 4:10-19.
    • (1997) Nature Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 10
    • 0028466243 scopus 로고
    • Solid evidence for molten globules
    • Dobson CM. 1994. Solid evidence for molten globules. Curr Biol 4:636-640.
    • (1994) Curr Biol , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 11
    • 0025292246 scopus 로고
    • In vitro folding and oligomerisation of a membrane protein
    • Eisele J-L, Rosenbusch JP. 1990. In vitro folding and oligomerisation of a membrane protein. J Biol Chem 265:10127-10220.
    • (1990) J Biol Chem , vol.265 , pp. 10127-10220
    • Eisele, J.-L.1    Rosenbusch, J.P.2
  • 12
    • 0028127827 scopus 로고
    • Roles of molecular chaperones in protein folding
    • Ellis J. 1994. Roles of molecular chaperones in protein folding. Curr Biol 4:117-122.
    • (1994) Curr Biol , vol.4 , pp. 117-122
    • Ellis, J.1
  • 13
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve GA, Bhuyan AK, Roder H. 1994. Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry 33:6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 14
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elöve GA, Chaffotte AF, Roder H, Goldberg ME. 1992. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry 31:6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 15
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • Fisher WR, Taniuchi H, Anfinsen CB. 1973. On the role of heme in the formation of the structure of cytochrome c. J Biol Chem 248:3188-3195.
    • (1973) J Biol Chem , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 16
    • 0026323440 scopus 로고
    • Import of proteins into mitochondria
    • Glick B, Schatz G. 1991. Import of proteins into mitochondria. Annu Rev Genet 25:21-44.
    • (1991) Annu Rev Genet , vol.25 , pp. 21-44
    • Glick, B.1    Schatz, G.2
  • 18
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F-U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 19
    • 0025091956 scopus 로고
    • Protein sorting to mitochondria - Evolutionary conservations of folding and assembly
    • Hartl F-U, Neupert W. 1990. Protein sorting to mitochondria - Evolutionary conservations of folding and assembly. Science 247:930-938.
    • (1990) Science , vol.247 , pp. 930-938
    • Hartl, F.-U.1    Neupert, W.2
  • 20
    • 0026012387 scopus 로고
    • 31P NMR spectroscopy. Correlation between the conformational changes of the protein and lipid bilayer
    • 31P NMR spectroscopy. Correlation between the conformational changes of the protein and lipid bilayer. Biochemistry 30:9084-9089.
    • (1991) Biochemistry , vol.30 , pp. 9084-9089
    • Heimburg, T.1    Hildebrandt, P.2    Marsh, D.3
  • 21
    • 0019756052 scopus 로고
    • Assembly of cytochrome c. Apocytochrome c is bound to specific sites in mitochondria before its conversion to holocytochrome c
    • Hennig B, Neupert W. 1981. Assembly of cytochrome c. Apocytochrome c is bound to specific sites in mitochondria before its conversion to holocytochrome c. Eur J Biochem 121:203-212.
    • (1981) Eur J Biochem , vol.121 , pp. 203-212
    • Hennig, B.1    Neupert, W.2
  • 22
    • 0021010724 scopus 로고
    • Biogenesis of cytochrome c in Neurospora crassa
    • Hennig B, Neupert W. 1983. Biogenesis of cytochrome c in Neurospora crassa. Methods Enzymol 97:261-274.
    • (1983) Methods Enzymol , vol.97 , pp. 261-274
    • Hennig, B.1    Neupert, W.2
  • 23
    • 0015820465 scopus 로고
    • Synthesis and characterization of two fluorescent sulfydryl reagents
    • Hudson EN, Weber G. 1973. Synthesis and characterization of two fluorescent sulfydryl reagents. Biochemistry 12:4154-4161.
    • (1973) Biochemistry , vol.12 , pp. 4154-4161
    • Hudson, E.N.1    Weber, G.2
  • 24
    • 0028227296 scopus 로고
    • Tertiary interactions in the pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki LS, Evans PA, Dobson CM, Radford SE. 1994. Tertiary interactions in the pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 33:5212-5220.
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 25
    • 0028561835 scopus 로고
    • Development of non-polar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
    • Jones BE, Jennings PA, Pierre RA, Matthews CR. 1994. Development of non-polar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry 33:15250-15258.
    • (1994) Biochemistry , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre, R.A.3    Matthews, C.R.4
  • 26
    • 0024600228 scopus 로고
    • The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes
    • Jordi W, Li-Xin Z, Pilon M, Demel RA, de Kruijff B. 1989. The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes. J Biol Chem 264:2292-2301.
    • (1989) J Biol Chem , vol.264 , pp. 2292-2301
    • Jordi, W.1    Li-Xin, Z.2    Pilon, M.3    Demel, R.A.4    De Kruijff, B.5
  • 27
    • 0027523179 scopus 로고
    • Residual helical structure in the C-terminal fragment of cytochrome c
    • Kuroda Y. 1993. Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry 32:1219-1224.
    • (1993) Biochemistry , vol.32 , pp. 1219-1224
    • Kuroda, Y.1
  • 30
    • 0030956720 scopus 로고    scopus 로고
    • Anionic phospholipids modulate peptide insertion into membranes
    • Liu LP, Deber CM. 1997. Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36:5476-5482.
    • (1997) Biochemistry , vol.36 , pp. 5476-5482
    • Liu, L.P.1    Deber, C.M.2
  • 31
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. 1996. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 32
    • 0000597110 scopus 로고
    • Cytochrome c from vertebrate and invertebrate sources
    • Margoliash E, Walasek OF. 1967. Cytochrome c from vertebrate and invertebrate sources. Methods Enzymol 10:339-348.
    • (1967) Methods Enzymol , vol.10 , pp. 339-348
    • Margoliash, E.1    Walasek, O.F.2
  • 33
    • 0028360934 scopus 로고
    • Interaction of synthetic peptide analogs of the class A amphipathic helix with lipids
    • Mishra VK, Palgunachari MN, Segrest JP, Anantharamaiah GM. 1994. Interaction of synthetic peptide analogs of the class A amphipathic helix with lipids. J Biol Chem 269:7185-7191.
    • (1994) J Biol Chem , vol.269 , pp. 7185-7191
    • Mishra, V.K.1    Palgunachari, M.N.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 34
    • 0024059673 scopus 로고
    • Import of proteins into mitochondria: A multistep process
    • Pfanner N, Hartl F-U, Neupert W. 1987. Import of proteins into mitochondria: A multistep process. Eur J Biochem 175:205-212.
    • (1987) Eur J Biochem , vol.175 , pp. 205-212
    • Pfanner, N.1    Hartl, F.-U.2    Neupert, W.3
  • 35
    • 0028080126 scopus 로고
    • The interaction of horse heart cytochrome c with phospholipid hilayers. Structural and dynamic effects
    • Pinheiro TJT. 1994. The interaction of horse heart cytochrome c with phospholipid hilayers. Structural and dynamic effects. Biochimie 76:489-500.
    • (1994) Biochimie , vol.76 , pp. 489-500
    • Pinheiro, T.J.T.1
  • 37
    • 17044441821 scopus 로고    scopus 로고
    • Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles
    • Pinheiro TJT, Elöve GA, Watts A, Roder H. 1997. Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry 36:13122-13132.
    • (1997) Biochemistry , vol.36 , pp. 13122-13132
    • Pinheiro, T.J.T.1    Elöve, G.A.2    Watts, A.3    Roder, H.4
  • 38
    • 0028260185 scopus 로고
    • Lipid specificity in the interaction of cytochrome c with anionic phospholipid membranes
    • Pinheiro TJT, Watts A. 1994. Lipid specificity in the interaction of cytochrome c with anionic phospholipid membranes. Biochemistry 33:2451-2458.
    • (1994) Biochemistry , vol.33 , pp. 2451-2458
    • Pinheiro, T.J.T.1    Watts, A.2
  • 39
    • 0000683917 scopus 로고
    • Reconstitution of chlorophyll a/b light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer
    • Plumley FG, Schmidt GW. 1987. Reconstitution of chlorophyll a/b light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer. Proc Natl Acad Sci USA 84:146-150.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 146-150
    • Plumley, F.G.1    Schmidt, G.W.2
  • 40
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
    • Popot J-L, Gerchman S-E, Engelman DM. 1987. Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J Mol Biol 198:655-676.
    • (1987) J Mol Biol , vol.198 , pp. 655-676
    • Popot, J.-L.1    Gerchman, S.-E.2    Engelman, D.M.3
  • 41
    • 0022537005 scopus 로고
    • Lateral proton conduction at lipid-water interfaces and its implications for the chemiosmotic-coupling hypothesis
    • Prats M, Teissié J, Toccane JF. 1986. Lateral proton conduction at lipid-water interfaces and its implications for the chemiosmotic-coupling hypothesis. Nature 322:756-758.
    • (1986) Nature , vol.322 , pp. 756-758
    • Prats, M.1    Teissié, J.2    Toccane, J.F.3
  • 42
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 43
    • 0032497370 scopus 로고    scopus 로고
    • Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid
    • Rankin SE, Watts A, Pinheiro TJT. 1998. Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid. Biochemistry 37:12588-12595.
    • (1998) Biochemistry , vol.37 , pp. 12588-12595
    • Rankin, S.E.1    Watts, A.2    Pinheiro, T.J.T.3
  • 44
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H, Colón W. 1997. Kinetic role of early intermediates in protein folding. Curr Opin Struct Biol 7:15-28.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 45
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder H, Elöve GA, Englander SW. 1988. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335:700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 46
    • 0031866483 scopus 로고    scopus 로고
    • Amide protection in an early folding intermediate of cytochrome c
    • Sauder JM, Roder H. 1998. Amide protection in an early folding intermediate of cytochrome c. Folding & Design 3:293-301.
    • (1998) Folding & Design , vol.3 , pp. 293-301
    • Sauder, J.M.1    Roder, H.2
  • 47
    • 0040286233 scopus 로고
    • Lipids in solution: Monomers and micelles
    • Hanahan DJ. ed. New York, London: Plenum Press
    • Small DM. 1986. Lipids in solution: Monomers and micelles. In: Hanahan DJ. ed. Physical chemistry of lipids. From alkanes to phospholipids. New York, London: Plenum Press. pp 58-72.
    • (1986) Physical Chemistry of Lipids. From Alkanes to Phospholipids , pp. 58-72
    • Small, D.M.1
  • 48
    • 0025910862 scopus 로고
    • Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements
    • Spooner PJR, Watts A. 1991. Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements. Biochemistry 30:3871-3879.
    • (1991) Biochemistry , vol.30 , pp. 3871-3879
    • Spooner, P.J.R.1    Watts, A.2
  • 49
    • 0024412334 scopus 로고
    • Interfacial properties and critical micelle concentration of lysophospholipids
    • Stafford RE, Fanni T, Dennis EA. 1989. Interfacial properties and critical micelle concentration of lysophospholipids. Biochemistry 28:5113-5120.
    • (1989) Biochemistry , vol.28 , pp. 5113-5120
    • Stafford, R.E.1    Fanni, T.2    Dennis, E.A.3
  • 50
    • 0015524145 scopus 로고
    • The conformation of horse heart apocytochrome c
    • Stellwagen E, Rysavy R, Babul G. 1972. The conformation of horse heart apocytochrome c. J Biol Chem 247:8074-8077.
    • (1972) J Biol Chem , vol.247 , pp. 8074-8077
    • Stellwagen, E.1    Rysavy, R.2    Babul, G.3
  • 51
    • 0025259678 scopus 로고
    • Apocytochrome c: An exceptional precursor protein using an exceptional import pathway
    • Stuart RA, Neupert W. 1990. Apocytochrome c: An exceptional precursor protein using an exceptional import pathway. Biochimie 72:115-121.
    • (1990) Biochimie , vol.72 , pp. 115-121
    • Stuart, R.A.1    Neupert, W.2
  • 52
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of a membrane protein into a lipid bilayer
    • Surrey T, Jähnig F. 1992. Refolding and oriented insertion of a membrane protein into a lipid bilayer. Proc Natl Acad Sci USA 89:7457-7461.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 53
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a β-barrel membrane protein
    • Surrey T, Jähnig F. 1995. Kinetics of folding and membrane insertion of a β-barrel membrane protein. J Biol Chem 270:28199-28203.
    • (1995) J Biol Chem , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jähnig, F.2
  • 54
    • 0030045746 scopus 로고    scopus 로고
    • Folding and membrane insertion of the trimeric β-barrel protein OmpF
    • Surrey T, Schmid A, Jähnig F. 1996. Folding and membrane insertion of the trimeric β-barrel protein OmpF. Biochemistry 35:2283-2288.
    • (1996) Biochemistry , vol.35 , pp. 2283-2288
    • Surrey, T.1    Schmid, A.2    Jähnig, F.3
  • 55
    • 0029283976 scopus 로고
    • The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide membrane interactions
    • Wall J, Golding CA, Van Veen M, O'Shea P. 1995. The use of fluoresceinphosphatidylethanolamine (FPE) as a real-time probe for peptide membrane interactions. Mol Membr Biol 12:183-192.
    • (1995) Mol Membr Biol , vol.12 , pp. 183-192
    • Wall, J.1    Golding, C.A.2    Van Veen, M.3    O'Shea, P.4


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