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Volumn 293, Issue 1, 1999, Pages 125-137

Chaperonin-affected refolding of α-lactalbumin: Effects of nucleotides and the co-chaperonin GroES

Author keywords

Cooperativity; Molecular chaperone; Protein folding; Stopped flow; lactalbumin

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONE; CHAPERONIN; LACTALBUMIN; NUCLEOTIDE;

EID: 0033569635     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3142     Document Type: Article
Times cited : (29)

References (42)
  • 1
    • 0031436142 scopus 로고    scopus 로고
    • Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction
    • Aoki K., Taguchi H., Shindo Y., Yoshida M., Ogasahara K., Yutani K., Tanaka N. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J. Biol. Chem. 272:1997;32158-32162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32158-32162
    • Aoki, K.1    Taguchi, H.2    Shindo, Y.3    Yoshida, M.4    Ogasahara, K.5    Yutani, K.6    Tanaka, N.7
  • 2
    • 0030348041 scopus 로고    scopus 로고
    • Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
    • Arai M., Kuwajima K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Design. 1:1996;275-287.
    • (1996) Fold. Design , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 3
    • 0029881740 scopus 로고    scopus 로고
    • Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coliβ-galactosidase
    • Ayling A., Baneyx F. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coliβ-galactosidase. Protein Sci. 5:1996;478-487.
    • (1996) Protein Sci. , vol.5 , pp. 478-487
    • Ayling, A.1    Baneyx, F.2
  • 4
    • 0030995661 scopus 로고    scopus 로고
    • Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
    • Behlke J., Ristau O., Schoenfeld H.-J. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry. 36:1997;5149-5156.
    • (1997) Biochemistry , vol.36 , pp. 5149-5156
    • Behlke, J.1    Ristau, O.2    Schoenfeld, H.-J.3
  • 7
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K., Adams P. D., Brhnger A. T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2:1995;1083-1094.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brhnger, A.T.3
  • 8
    • 0024726838 scopus 로고
    • Determination of the dead time of a stopped-flow fluorometer
    • Brissette P., Ballou D. P., Massey V. Determination of the dead time of a stopped-flow fluorometer. Anal. Biochem. 181:1989;234-238.
    • (1989) Anal. Biochem. , vol.181 , pp. 234-238
    • Brissette, P.1    Ballou, D.P.2    Massey, V.3
  • 10
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A. L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 11
    • 0029882517 scopus 로고
    • Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL
    • Clark A. C., Hugo E., Frieden C. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry. 35:1995;5893-5901.
    • (1995) Biochemistry , vol.35 , pp. 5893-5901
    • Clark, A.C.1    Hugo, E.2    Frieden, C.3
  • 13
    • 0029019467 scopus 로고
    • The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding
    • Corrales F. J., Fersht A. R. The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding. Proc. Natl Acad. Sci. USA. 92:1995;5326-5330.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5326-5330
    • Corrales, F.J.1    Fersht, A.R.2
  • 14
    • 0029664316 scopus 로고    scopus 로고
    • Toward a mechanism for GroEL/GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
    • Corrales F. J., Fersht A. R. Toward a mechanism for GroEL/GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc. Natl Acad. Sci. USA. 93:1996;4509-4512.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4509-4512
    • Corrales, F.J.1    Fersht, A.R.2
  • 15
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton W. A., Horwich A. L. GroEL-mediated protein folding. Protein Sci. 6:1997;743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 16
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.-J., Sambrook J. Protein folding in the cell. Nature. 355:1992;33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 17
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt J. F., Weaver A. J., Landry S. J., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 18
    • 0025812217 scopus 로고
    • In vivo analysis of integration of membrane proteins in Escherichia coli
    • Ito K., Akiyama Y. In vivo analysis of integration of membrane proteins in Escherichia coli. Mol. Microbiol. 5:1991;2243-2253.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2243-2253
    • Ito, K.1    Akiyama, Y.2
  • 19
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on the re-folding kinetics of α-lactalbumin
    • Katsumata K., Okazaki A., Kuwajima K. Effect of GroEL on the re-folding kinetics of α-lactalbumin. J. Mol. Biol. 258:1996a;827-838.
    • (1996) J. Mol. Biol. , vol.258 , pp. 827-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 20
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
    • Katsumata K., Okazaki A., Tsurupa G. P., Kuwajima K. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J. Mol. Biol. 364:1996b;643-649.
    • (1996) J. Mol. Biol. , vol.364 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 21
    • 0028307452 scopus 로고
    • Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation
    • Kawata Y., Nosaka K., Hongo K., Mizobata T., Nagai J. Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation. FEBS Letters. 345:1994;229-232.
    • (1994) FEBS Letters , vol.345 , pp. 229-232
    • Kawata, Y.1    Nosaka, K.2    Hongo, K.3    Mizobata, T.4    Nagai, J.5
  • 22
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 23
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 24
    • 0028228564 scopus 로고
    • Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding
    • Landry S. J., Gierasch L. M. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu. Rev. Biophys. Biomol. Struct. 23:1994;645-669.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 645-669
    • Landry, S.J.1    Gierasch, L.M.2
  • 25
    • 0028838951 scopus 로고
    • The hydrophobic nature of GroEL-substrate binding
    • Lin Z., Schwarz F. P., Eisenstein E. The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 270:1994;1011-1014.
    • (1994) J. Biol. Chem. , vol.270 , pp. 1011-1014
    • Lin, Z.1    Schwarz, F.P.2    Eisenstein, E.3
  • 26
    • 0028799620 scopus 로고
    • Homologous proteins with different affinities for groEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures
    • Mattingly J. R. Jr, Iriarte A., Martinez-Carrion M. Homologous proteins with different affinities for groEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures. J. Biol. Chem. 270:1995;1138-1148.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1138-1148
    • Mattingly J.R., Jr.1    Iriarte, A.2    Martinez-Carrion, M.3
  • 28
    • 0028466392 scopus 로고
    • The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
    • Okazaki A., Ikura T., Nikaido K., Kuwajima K. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nature Struct. Biol. 1:1994;439-446.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 439-446
    • Okazaki, A.1    Ikura, T.2    Nikaido, K.3    Kuwajima, K.4
  • 30
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A. M., Chen S., White G., Braig K., Saibil G. R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, G.3    Braig, K.4    Saibil, G.R.5
  • 31
  • 32
    • 0030994081 scopus 로고    scopus 로고
    • How GroES regulates binding of nonnative protein to GroEL
    • Sparrer H., Buchner J. How GroES regulates binding of nonnative protein to GroEL. J. Biol. Chem. 272:1997;14080-14086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14080-14086
    • Sparrer, H.1    Buchner, J.2
  • 33
    • 0029975103 scopus 로고    scopus 로고
    • Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
    • Sparrer H., Lille H., Buchner J. Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants. J. Mol. Biol. 258:1996;74-87.
    • (1996) J. Mol. Biol. , vol.258 , pp. 74-87
    • Sparrer, H.1    Lille, H.2    Buchner, J.3
  • 34
    • 0028231826 scopus 로고
    • Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
    • Staniforth R. A., Burston S. G., Atkinson T., Clarke A. R. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem. J. 300:1994;651-658.
    • (1994) Biochem. J. , vol.300 , pp. 651-658
    • Staniforth, R.A.1    Burston, S.G.2    Atkinson, T.3    Clarke, A.R.4
  • 35
    • 0032932922 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding
    • Terada T. P., Kuwajima K. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding. Biophys. Biochim. Acta. 1431:1999;269-281.
    • (1999) Biophys. Biochim. Acta , vol.1431 , pp. 269-281
    • Terada, T.P.1    Kuwajima, K.2
  • 36
    • 0032478538 scopus 로고    scopus 로고
    • Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
    • Tsurupa G. P., Ikura T., Makio T., Kuwajima K. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL. J. Mol. Biol. 277:1998;733-745.
    • (1998) J. Mol. Biol. , vol.277 , pp. 733-745
    • Tsurupa, G.P.1    Ikura, T.2    Makio, T.3    Kuwajima, K.4
  • 38
    • 0025940841 scopus 로고
    • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
    • Viitanen P. V., Donaldson G. K., Lorimer G. H., Lubben T. H., Gatenby A. A. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry. 30:1991;9716-9723.
    • (1991) Biochemistry , vol.30 , pp. 9716-9723
    • Viitanen, P.V.1    Donaldson, G.K.2    Lorimer, G.H.3    Lubben, T.H.4    Gatenby, A.A.5
  • 40
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman J. S., Rye H. S., Fenton W. A., Beechem J. M., Horwich A. L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 84:1996;481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 42
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.