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Volumn 402, Issue 6758, 1999, Pages 147-154

Identification of in vivo substrates of the chaperonin GroEL

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN;

EID: 0033547324     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/45977     Document Type: Article
Times cited : (446)

References (49)
  • 1
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C. & Welch, W. J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634 (1993).
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 2
    • 0028127827 scopus 로고
    • Roles of molecular chaperones in protein folding
    • Ellis, R. J. Roles of molecular chaperones in protein folding. Curr. Opin. Struct. Biol. 4,.117-122 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 117-122
    • Ellis, R.J.1
  • 3
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. Molecular chaperones in cellular protein folding. Nature 381, 571-580 (1996).
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 4
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet, O., Ziegelhoffer, T. & Georgopoulos, C. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 5
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A. L., Low, K. B., Fenton, W. A., Hirshfield, I. N. 8: Furtak, K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74, 909-917 ( 1993).
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 6
    • 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, 614-619 (1994).
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 7
    • 0031297406 scopus 로고    scopus 로고
    • Structural and mechanistic consequences of polypeptide binding by GroEL
    • Coyle, J. E., Jaeger, J., Gross, M., Robinson, C. V. & Radford, S. E. Structural and mechanistic consequences of polypeptide binding by GroEL. Fold. Design 2, R93-R104 (1997).
    • (1997) Fold. Design , vol.2
    • Coyle, J.E.1    Jaeger, J.2    Gross, M.3    Robinson, C.V.4    Radford, S.E.5
  • 8
    • 0031684079 scopus 로고    scopus 로고
    • Structure and function in GroEL-mediated protein folding
    • Sigler, P. B. et al. Structure and function in GroEL-mediated protein folding. Annu., Rev. Biochem. 67, 581-608 (1998).
    • (1998) Annu., Rev. Biochem. , vol.67 , pp. 581-608
    • Sigler, P.B.1
  • 10
    • 0030750584 scopus 로고    scopus 로고
    • In vim observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt, K. L., Hendrick, J. P., Houry, W. A. & Hartl, F. U. In vim observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 491-500 (1997).
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 11
    • 0021731777 scopus 로고
    • Escherichia coli ribosomes translate in vivo with variable rate
    • Pedersen, S. Escherichia coli ribosomes translate in vivo with variable rate. EMBO J. 3, 2895-2898 (1984).
    • (1984) EMBO J. , vol.3 , pp. 2895-2898
    • Pedersen, S.1
  • 12
    • 0031932170 scopus 로고    scopus 로고
    • Favorable domain size in proteins
    • Xu, D. & Nussinov, R. Favorable domain size in proteins. Fold. Design 3, 11-17 (1998).
    • (1998) Fold. Design , vol.3 , pp. 11-17
    • Xu, D.1    Nussinov, R.2
  • 14
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis, R. J. & Hartl, F. U. Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10, 20-26 (1996).
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 15
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye, H. S. et al. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97, 325-338 (1999).
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1
  • 16
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • Ellis, R. J. Molecular chaperones: avoiding the crowd. Curr. Biol. 7, R531-R533 (1997).
    • (1997) Curr. Biol. , vol.7
    • Ellis, R.J.1
  • 17
    • 0022913522 scopus 로고
    • The cloning and sequence of the gene encoding the omega subunit of Escherichia coli RNA polymerase
    • Gentry, D. R. & Burgess, R. R. The cloning and sequence of the gene encoding the omega subunit of Escherichia coli RNA polymerase. Gene 48, 33-40 (1986).
    • (1986) Gene , vol.48 , pp. 33-40
    • Gentry, D.R.1    Burgess, R.R.2
  • 18
    • 0023108779 scopus 로고
    • Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNa polymerase of Escherichia coli K-12
    • Wada, M., Fujita, H. & Itikawa, H. Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNA polymerase of Escherichia coli K-12. J. Bacteriol. 169, 1102-1106 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 1102-1106
    • Wada, M.1    Fujita, H.2    Itikawa, H.3
  • 19
    • 0027331573 scopus 로고
    • Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/ GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity
    • Ziemienowicz, A. et al. Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/ GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. J. Biol. Chem. 268, 25425-25431 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25425-25431
    • Ziemienowicz, A.1
  • 22
    • 0032926060 scopus 로고    scopus 로고
    • The CATH database provides insights into protein structure/function relationships
    • Orengo, C. A. et al. The CATH database provides insights into protein structure/function relationships. Nucleic Acids Res. 27, 275-279 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 275-279
    • Orengo, C.A.1
  • 23
    • 0022539429 scopus 로고
    • Hydrophobicity and amphiphilicity in protein structure
    • Eisenberg, D., Wilcox, W. & McLachlan, A. D. Hydrophobicity and amphiphilicity in protein structure. J. Cell. Biochem. 31, 11-17 (1986).
    • (1986) J. Cell. Biochem. , vol.31 , pp. 11-17
    • Eisenberg, D.1    Wilcox, W.2    McLachlan, A.D.3
  • 24
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protien hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng, M. Y. et al. Mitochondrial heat-shock protien hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620-625 (1989).
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1
  • 25
    • 0030804446 scopus 로고    scopus 로고
    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • Rye, H. S. et al. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388, 792-798 (1997).
    • (1997) Nature , vol.388 , pp. 792-798
    • Rye, H.S.1
  • 27
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T. & Baker, D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 28
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M. P., Bennett, M. J. & Eisenberg, D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50, 61-122 (1997).
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 29
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry, S. I., Jordan, R., McMacken, R. & Gierasch, L. M. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature 355, 455-457 (1992).
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.I.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 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, 2315-2319 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Pluckthun, A.4
  • 31
    • 0025940841 scopus 로고
    • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
    • Vitanen, 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, 9716-9723 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9716-9723
    • Vitanen, P.V.1    Donaldson, G.K.2    Lorimer, G.H.3    Lubben, T.H.4    Gatenby, A.A.5
  • 32
    • 0032582806 scopus 로고    scopus 로고
    • Partitioning of rhodanese onto GroEL-chaperonin binds a reversibly oxidized form derived from the native protein
    • Smith, K. E., Voziyan, P. A. & Fisher, M. T. Partitioning of rhodanese onto GroEL-chaperonin binds a reversibly oxidized form derived from the native protein. J. Biol. Chem. 273, 28677-28681 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28677-28681
    • Smith, K.E.1    Voziyan, P.A.2    Fisher, M.T.3
  • 33
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl, M, K., Weber, F. & Hartl, F. U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15, 6111-6121 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 34
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale
    • Bjellqvist, B., Pasquali, C., Ravier, F., Sanchez, J. C. & Hochstrasser, D. A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis 14, 1357-1365 (1993).
    • (1993) Electrophoresis , vol.14 , pp. 1357-1365
    • Bjellqvist, B.1    Pasquali, C.2    Ravier, F.3    Sanchez, J.C.4    Hochstrasser, D.5
  • 35
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg, A., Postel, W. & Gunther, S. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9, 531-546 (1988).
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 36
    • 0031214574 scopus 로고    scopus 로고
    • Identification of proteins by matrix-assisted laser desorption ionization-mass spectrometry following in-gel digestion in low-salt, nonvolatile buffer and simplified peptide recovery
    • Fountoulakis, M. & Langen, H. Identification of proteins by matrix-assisted laser desorption ionization-mass spectrometry following in-gel digestion in low-salt, nonvolatile buffer and simplified peptide recovery. Anal. Biochem. 250, 153-156 (1997).
    • (1997) Anal. Biochem. , vol.250 , pp. 153-156
    • Fountoulakis, M.1    Langen, H.2
  • 37
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S. F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 38
    • 0001514262 scopus 로고
    • Statistics of local complexity in amino acid sequences and sequence databases
    • Wootton, J. & Federhen, S. Statistics of local complexity in amino acid sequences and sequence databases. Comput. Chem. 17, 149-163 (1993).
    • (1993) Comput. Chem. , vol.17 , pp. 149-163
    • Wootton, J.1    Federhen, S.2
  • 39
    • 0028802662 scopus 로고
    • Gene products of Escherichia coli: Sequence comparisons and common ancestries
    • Labedan, B. & Riley, W. Gene products of Escherichia coli: sequence comparisons and common ancestries. Mol. Biol. Evol. 12, 980-987 (1995).
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 980-987
    • Labedan, B.1    Riley, W.2
  • 40
    • 0021847027 scopus 로고
    • The detection and classification of membrane-spanning proteins
    • Klein, P., Kanehisa, M. & DeLisi, C. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta 815, 468-476 (1985).
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    DeLisi, C.3
  • 41
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary structure prediction
    • Frishman, D. & Argos, P. Seventy-five percent accuracy in protein secondary structure prediction. Proteins 27, 329-335 (1997).
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 42
    • 0022631926 scopus 로고
    • The folding type of a protein is relevant to the amino acid composition
    • Nakashima, H., Nishikawa, K. & Ooi, T. The folding type of a protein is relevant to the amino acid composition. J. Biochem. 99, 153-162 (1986).
    • (1986) J. Biochem. , vol.99 , pp. 153-162
    • Nakashima, H.1    Nishikawa, K.2    Ooi, T.3
  • 43
    • 0032540845 scopus 로고    scopus 로고
    • Homology-based fold predictions for Mycoplasma genitalium proteins
    • Huynen, M. et al. Homology-based fold predictions for Mycoplasma genitalium proteins. J. Mol. Biol. 280, 323-326 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 323-326
    • Huynen, M.1
  • 44
    • 0030879154 scopus 로고    scopus 로고
    • Pedantic genome analysis
    • Frishman, D. & Mewes, H. W. Pedantic genome analysis. Trends Genet. 13, 415-416 (1997).
    • (1997) Trends Genet. , vol.13 , pp. 415-416
    • Frishman, D.1    Mewes, H.W.2
  • 45
    • 0031864543 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
    • Bairoch, A. & Apweiler, R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998. Nucleic Acids Res. 26, 38-42 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 38-42
    • Bairoch, A.1    Apweiler, R.2
  • 48
    • 0032504132 scopus 로고    scopus 로고
    • Structure of the Escherichia coli RNA polymerase alpha subunit amino terminal domain
    • Zhang, G. & Darst, S. A. Structure of the Escherichia coli RNA polymerase alpha subunit amino terminal domain. Science 281, 262-266 (1998).
    • (1998) Science , vol.281 , pp. 262-266
    • Zhang, G.1    Darst, S.A.2
  • 49
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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