메뉴 건너뛰기




Volumn 285, Issue 4, 1999, Pages 1777-1788

The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases

Author keywords

Binding free energy; Chaperonin; DHFR; Kinetics; Protein folding

Indexed keywords

CHAPERONIN; DIHYDROFOLATE REDUCTASE;

EID: 0033613819     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2403     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 0031058827 scopus 로고    scopus 로고
    • Detection of changes in pairwise interaction during allosteric transitions - coupling between local and global conformational changes in GroEL
    • Aharoni A., Horovitz A. Detection of changes in pairwise interaction during allosteric transitions - coupling between local and global conformational changes in GroEL. Proc. Natl Acad. Sci. USA. 94:1997;1698-1702.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1698-1702
    • Aharoni, A.1    Horovitz, A.2
  • 2
    • 0025989451 scopus 로고
    • Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase
    • Ahrweiler P. M., Frieden C. Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase. Biochemistry. 30:1991;7801-7809.
    • (1991) Biochemistry , vol.30 , pp. 7801-7809
    • Ahrweiler, P.M.1    Frieden, C.2
  • 3
    • 0016709592 scopus 로고
    • Purification and properties of Escherichia coli dihydrofolate reductase
    • Baccanari D., Phillips A., Smith S., Sinski D., Burchall J. Purification and properties of Escherichia coli dihydrofolate reductase. Biochemistry. 14:1975;5267-5273.
    • (1975) Biochemistry , vol.14 , pp. 5267-5273
    • Baccanari, D.1    Phillips, A.2    Smith, S.3    Sinski, D.4    Burchall, J.5
  • 4
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - A flexible, portable system
    • Barshop B. A., Wrenn R. F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM - a flexible, portable system. Anal. Biochem. 130:1983;134-145.
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 5
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
    • Boisvert D. C., Wang J., Otwinowski Z., Horwich A. L., Sigler P. B. The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nature Struct. Biol. 3:1996;170-177.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 7
    • 0024977331 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies
    • Chen B.-I., Schellmann J. A. Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. Biochemistry. 28:1989;685-691.
    • (1989) Biochemistry , vol.28 , pp. 685-691
    • Chen, B.-I.1    Schellmann, J.A.2
  • 8
    • 0031547963 scopus 로고    scopus 로고
    • GroEL-mediated folding of structurally homologous dihydrofolate reductases
    • Clark A. C., Frieden C. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J. Mol. Biol. 268:1997;512-525.
    • (1997) J. Mol. Biol. , vol.268 , pp. 512-525
    • Clark, A.C.1    Frieden, C.2
  • 9
    • 0033613814 scopus 로고    scopus 로고
    • Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures
    • Clark A. C., Frieden C. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J. Mol. Biol. 285:1999;1763-1774.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1763-1774
    • Clark, A.C.1    Frieden, C.2
  • 10
    • 0029882517 scopus 로고    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. 35:1996;5893-5901.
    • (1996) Biochemistry , vol.35 , pp. 5893-5901
    • Clark, A.C.1    Hugo, E.2    Frieden, C.3
  • 11
    • 0031918147 scopus 로고    scopus 로고
    • Purification of GroEL with low fluorescence background
    • Clark A. C., Ramanathan R., Frieden C. Purification of GroEL with low fluorescence background. Methods Enzymol. 290:1998;100-118.
    • (1998) Methods Enzymol. , vol.290 , pp. 100-118
    • Clark, A.C.1    Ramanathan, R.2    Frieden, C.3
  • 12
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the anfinsen cage
    • Ellis R. J. Revisiting the anfinsen cage. Fold. Design. 1:1996;R9-R15.
    • (1996) Fold. Design , vol.1
    • Ellis, R.J.1
  • 13
    • 0031574908 scopus 로고    scopus 로고
    • GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
    • Fedorov A. N., Baldwin T. O. GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J. Mol. Biol. 268:1997;712-723.
    • (1997) J. Mol. Biol. , vol.268 , pp. 712-723
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 14
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W. A., Kashi Y., Furtak K., Horwich A. L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 15
    • 0026741821 scopus 로고
    • Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP
    • Fisher M. T. Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP. Biochemistry. 31:1992;3955-3963.
    • (1992) Biochemistry , vol.31 , pp. 3955-3963
    • Fisher, M.T.1
  • 16
    • 0031004530 scopus 로고    scopus 로고
    • Protein folding: How the mechanism of GroEL action is defined by kinetics
    • Frieden C., Clark A. C. Protein folding: how the mechanism of GroEL action is defined by kinetics. Proc. Natl Acad. Sci. USA. 94:1997;5535-5538.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5535-5538
    • Frieden, C.1    Clark, A.C.2
  • 17
    • 0027179284 scopus 로고
    • Refolding of barnase in the presence of GroE
    • Gray T. E., Fersht A. R. Refolding of barnase in the presence of GroE. J. Mol. Biol. 232:1993;1197-1207.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1197-1207
    • Gray, T.E.1    Fersht, A.R.2
  • 18
    • 0012269326 scopus 로고    scopus 로고
    • Evolutionary relationships of chaperonins
    • R. J. Ellis. New York: Academic Press
    • Gupta R. S. Evolutionary relationships of chaperonins. Ellis R. J. The Chaperonins. 1996;27-64 Academic Press, New York.
    • (1996) The Chaperonins , pp. 27-64
    • Gupta, R.S.1
  • 19
    • 0027507970 scopus 로고
    • Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP
    • Hansen J. E., Gafni A. Thermal switching between enhanced and arrested reactivation of bacterial glucose-6-phosphate dehydrogenase assisted by GroEL in the absence of ATP. J. Biol. Chem. 268:1993;21632-21636.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21632-21636
    • Hansen, J.E.1    Gafni, A.2
  • 20
    • 0028175779 scopus 로고
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies. Biochemistry. 33:1994;5502-5509.
    • (1994) Biochemistry , vol.33 , pp. 5502-5509
    • Hoeltzli, S.D.1    Frieden, C.2
  • 21
    • 0030475699 scopus 로고    scopus 로고
    • 19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy
    • 19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy. Biochemistry. 35:1996;16843-16851.
    • (1996) Biochemistry , vol.35 , pp. 16843-16851
    • Hoeltzli, S.D.1    Frieden, C.2
  • 22
    • 0032488452 scopus 로고    scopus 로고
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: A stopped-flow NMR spectroscopy study
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study. Biochemistry. 37:1998;387-398.
    • (1998) Biochemistry , vol.37 , pp. 387-398
    • Hoeltzli, S.D.1    Frieden, C.2
  • 23
    • 0030569019 scopus 로고    scopus 로고
    • Interaction of GroEL with conformational states of horse cytochrome c
    • Hoshino M., Kawata Y., Goto Y. Interaction of GroEL with conformational states of horse cytochrome c. J. Mol. Biol. 262:1996;575-587.
    • (1996) J. Mol. Biol. , vol.262 , pp. 575-587
    • Hoshino, M.1    Kawata, Y.2    Goto, Y.3
  • 24
    • 0030827121 scopus 로고    scopus 로고
    • GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex
    • Inbar E., Horovitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex. Biochemistry. 36:1997;12276-12281.
    • (1997) Biochemistry , vol.36 , pp. 12276-12281
    • Inbar, E.1    Horovitz, A.2
  • 25
    • 0028947956 scopus 로고
    • Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones B. E., Matthews C. R. Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 4:1995;167-177.
    • (1995) Protein Sci. , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 26
    • 0028925815 scopus 로고
    • Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy
    • Jones B. E., Beechem J. A., Matthews C. R. Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry. 34:1995;1867-1877.
    • (1995) Biochemistry , vol.34 , pp. 1867-1877
    • Jones, B.E.1    Beechem, J.A.2    Matthews, C.R.3
  • 27
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on the refolding kinetics of alpha-lactalbumin
    • Katsumata K., Okazaki A., Kuwajima K. Effect of GroEL on the refolding kinetics of alpha-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
  • 28
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL
    • Katsumata K., Okazaki A., Tsurupa G. P., Kuwajima K. Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL. J. Mol. Biol. 264:1996b;643-649.
    • (1996) J. Mol. Biol. , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 29
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K., Garvey E. P., Finn B. E., Matthews C. R., Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry. 30:1991;7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 30
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor
    • Laminet A. A., Ziegelhoffer T., Georgopoulos C., Pluckthun A. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9:1990;2315-2319.
    • (1990) EMBO J. , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Pluckthun, A.4
  • 31
    • 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. 270:1995;1011-1014.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1011-1014
    • Lin, Z.1    Schwarz, F.P.2    Eisenstein, E.3
  • 32
    • 0032571386 scopus 로고    scopus 로고
    • Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release
    • Martin J. Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release. J. Biol. Chem. 273:1998;7351-7357.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7351-7357
    • Martin, J.1
  • 34
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
    • Mendoza J. A., Rogers E., Lorimer G. H., Horowitz P. M. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem. 266:1991;13044-13049.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13044-13049
    • Mendoza, J.A.1    Rogers, E.2    Lorimer, G.H.3    Horowitz, P.M.4
  • 35
    • 0029090130 scopus 로고
    • Kinetic analysis of interactions between GroEL and reduced alpha lactalbumin - effect of GroES and nucleotides
    • Murai N., Taguchi H., Yoshida M. Kinetic analysis of interactions between GroEL and reduced alpha lactalbumin - effect of GroES and nucleotides. J. Biol. Chem. 270:1995;19957-19963.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19957-19963
    • Murai, N.1    Taguchi, H.2    Yoshida, M.3
  • 37
    • 0031588017 scopus 로고    scopus 로고
    • Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
    • Perrett S., Zahn R., Stenberg G., Fersht A. R. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J. Mol. Biol. 269:1997;892-901.
    • (1997) J. Mol. Biol. , vol.269 , pp. 892-901
    • Perrett, S.1    Zahn, R.2    Stenberg, G.3    Fersht, A.R.4
  • 38
    • 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. X., White H., Braig K., Saibil H. 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.X.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 39
    • 0029975103 scopus 로고    scopus 로고
    • Dynamics of the GroEL protein complex: Effects of nucleotides and folding mutants
    • Sparrer H., Lilie 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    Lilie, H.2    Buchner, J.3
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0029837424 scopus 로고    scopus 로고
    • A thermodynamic coupling mechanism for GroEL-mediated unfolding
    • Walter S., Lorimer G. H., Schmid F. X. A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc. Natl Acad. Sci. USA. 93:1996;9425-9430.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9425-9430
    • Walter, S.1    Lorimer, G.H.2    Schmid, F.X.3
  • 44
    • 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
  • 45
    • 0029995319 scopus 로고    scopus 로고
    • Allosteric control by ATP of non-folded protein binding to GroEL
    • Yifrach O., Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL. J. Mol. Biol. 255:1996;356-361.
    • (1996) J. Mol. Biol. , vol.255 , pp. 356-361
    • Yifrach, O.1    Horovitz, A.2
  • 46
    • 0028075011 scopus 로고
    • Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor
    • Zahn R., Axmann S. E., Rucknagel K.-P., Jaeger E., Laminet A. A., Pluckthun A. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor. J. Mol. Biol. 242:1994a;150-164.
    • (1994) J. Mol. Biol. , vol.242 , pp. 150-164
    • Zahn, R.1    Axmann, S.E.2    Rucknagel, K.-P.3    Jaeger, E.4    Laminet, A.A.5    Pluckthun, A.6
  • 47
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn R., Spitzfaden C., Ottiger M., Wuthrich K., Pluckthun A. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature. 368:1994b;261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, M.3    Wuthrich, K.4    Pluckthun, A.5
  • 48
    • 0030576536 scopus 로고    scopus 로고
    • Conformational states bound by the molecular chaperones GroEL and SecB - A hidden unfolding (annealing) activity
    • Zahn R., Perrett S., Fersht A. R. Conformational states bound by the molecular chaperones GroEL and SecB - a hidden unfolding (annealing) activity. J. Mol. Biol. 261:1996a;43-61.
    • (1996) J. Mol. Biol. , vol.261 , pp. 43-61
    • Zahn, R.1    Perrett, S.2    Fersht, A.R.3
  • 49
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn R., Perrett S., Stenberg G., Fersht A. R. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996b;642-645.
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.