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Science 18 February 1994:
Vol. 263. no. 5149, pp. 971 - 973
DOI: 10.1126/science.8310296
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Articles

Science, Vol 263, Issue 5149, 971-973
Copyright © 1994 by American Association for the Advancement of Science

articles

Kinetics of molecular chaperone action

D Schmid, A Baici, H Gehring, and P Christen

Biochemisches Institut, Universitat Zurich, Switzerland.

Molecular chaperones of the Hsp70 type transiently sequester unfolded segments of proteins and promote their correct folding. Target peptides were labeled with an environmentally sensitive fluorophore so that their binding to the molecular chaperone DnaK of Escherichia coli could be followed in real time. The two-step process was characterized by relaxation times of 27 seconds and 200 seconds with 2 microM DnaK and 0.1 microM ligand at 25 degrees C. In the presence of adenosine triphosphate, the formation of the complex was greatly accelerated and appeared to be a single-exponential process with a relaxation time of 0.4 second. The binding-release cycle of DnaK thus occurs in the time range of polypeptide chain elongation and folding and is too fast to be stoichiometrically coupled to the adenosine triphosphatase activity of the chaperone (turnover number, 0.13 per minute at 30 degrees C).


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W.-C. Suh, C. Z. Lu, and C. A. Gross (1999)
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J. E. Davis, C. Voisine, and E. A. Craig (1999)
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Cer1p Functions as a Molecular Chaperone in the Endoplasmic Reticulum of Saccharomyces cerevisiae.
T. G. Hamilton, T. B. Norris, P. R. Tsuruda, and G. C. Flynn (1999)
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Interaction of BiP with the J-domain of the Sec63p Component of the Endoplasmic Reticulum Protein Translocation Complex.
B. Misselwitz, O. Staeck, K. E. S. Matlack, and T. A. Rapoport (1999)
J. Biol. Chem. 274, 20110-20115
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E. T. Michelini and G. C. Flynn (1999)
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Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones.
T. Laufen, M. P. Mayer, C. Beisel, D. Klostermeier, A. Mogk, J. Reinstein, and B. Bukau (1999)
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Interaction between the Nucleotide Exchange Factor Mge1 and the Mitochondrial Hsp70 Ssc1.
S. Sakuragi, Q. Liu, and E. Craig (1999)
J. Biol. Chem. 274, 11275-11282
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Chaperone-Mediated Protein Folding.
A. L. Fink (1999)
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Construction and Analysis of Hybrid Escherichia coli-Bacillus subtilis dnaK Genes.
A. Mogk, B. Bukau, R. Lutz, and W. Schumann (1999)
J. Bacteriol. 181, 1971-1974
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M. M. Endrich, P. Gehrig, and H. Gehring (1999)
J. Biol. Chem. 274, 5326-5332
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Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
W.-C. Suh, W. F. Burkholder, C. Z. Lu, X. Zhao, M. E. Gottesman, and C. A. Gross (1998)
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Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.
C. S. Gassler, A. Buchberger, T. Laufen, M. P. Mayer, H. Schroder, A. Valencia, and B. Bukau (1998)
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P. Lopez-Buesa, C. Pfund, and E. A. Craig (1998)
PNAS 95, 15253-15258
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Divergent Hsc70 Binding Properties of Mitochondrial and Cytosolic Aspartate Aminotransferase. IMPLICATIONS FOR THEIR SEGREGATION TO DIFFERENT CELLULAR COMPARTMENTS.
A. Artigues, D. L. Crawford, A. Iriarte, and M. Martinez-Carrion (1998)
J. Biol. Chem. 273, 33130-33134
   Abstract »    Full Text »    PDF »
The Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins.
H. Kosano, B. Stensgard, M. C. Charlesworth, N. McMahon, and D. Toft (1998)
J. Biol. Chem. 273, 32973-32979
   Abstract »    Full Text »    PDF »
Substrate Binding Induces Depolymerization of the C-terminal Peptide Binding Domain of Murine GRP78/BiP.
M. Chevalier, L. King, C. Wang, M.-J. Gething, E. Elguindi, and S. Y. Blond (1998)
J. Biol. Chem. 273, 26827-26835
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Characterization of Interactions between the Anti-apoptotic Protein BAG-1 and Hsc70 Molecular Chaperones.
J. K. Stuart, D. G. Myszka, L. Joss, R. S. Mitchell, S. M. McDonald, Z. Xie, S. Takayama, J. C. Reed, and K. R. Ely (1998)
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Role of the J-domain in the cooperation of Hsp40 with Hsp70.
M. K. Greene, K. Maskos, and S. J. Landry (1998)
PNAS 95, 6108-6113
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Involvement of Molecular Chaperonins in Nucleotide Excision Repair. DnaK LEADS TO INCREASED THERMAL STABILITY OF UvrA, CATALYTIC UvrB LOADING, ENHANCED REPAIR, AND INCREASED UV RESISTANCE.
Y. Zou, D. J. Crowley, and B. Van Houten (1998)
J. Biol. Chem. 273, 12887-12892
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D-Peptide Ligands for the Co-chaperone DnaJ.
B. Feifel, H.-J. Schonfeld, and P. Christen (1998)
J. Biol. Chem. 273, 11999-12002
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Visualization of a Slow, ATP-induced Structural Transition in the Bacterial Molecular Chaperone DnaK.
C. D. Farr, S. V. Slepenkov, and S. N. Witt (1998)
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The Carboxy-Terminal Domain of Hsc70 Provides Binding Sites for a Distinct Set of Chaperone Cofactors.
J. Demand, J. Lüders, and J. Höhfeld (1998)
Mol. Cell. Biol. 18, 2023-2028
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Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE.
E. V. Pierpaoli, E. Sandmeier, H.-J. Schonfeld, and P. Christen (1998)
J. Biol. Chem. 273, 6643-6649
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Intrinsic ADP-ATP Exchange Activity Is a Novel Function of the Molecular Chaperone, Hsp70.
M. Hiromura, M. Yano, H. Mori, M. Inoue, and H. Kido (1998)
J. Biol. Chem. 273, 5435-5438
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The Molecular Chaperone Hsc70 Assists the in Vitro Folding of the N-terminal Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator.
E. Strickland, B.-H. Qu, L. Millen, and P. J. Thomas (1997)
J. Biol. Chem. 272, 25421-25424
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The Mitochondrial hsp70 Chaperone System. EFFECT OF ADENINE NUCLEOTIDES, PEPTIDE SUBSTRATE, AND mGrpE ON THE OLIGOMERIC STATE OF mhsp70.
A. Azem, W. Oppliger, A. Lustig, P. Jeno, B. Feifel, G. Schatz, and M. Horst (1997)
J. Biol. Chem. 272, 20901-20906
   Abstract »    Full Text »    PDF »
Refolding Intermediates of Acid-unfolded Mitochondrial Aspartate Aminotransferase Bind to hsp70.
A. Artigues, A. Iriarte, and M. Martinez-Carrion (1997)
J. Biol. Chem. 272, 16852-16861
   Abstract »    Full Text »    PDF »
Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent.
P. A. Wearsch and C. V. Nicchitta (1997)
J. Biol. Chem. 272, 5152-5156
   Abstract »    Full Text »    PDF »
Enzymatic Characterization of FliI. AN ATPase INVOLVED IN FLAGELLAR ASSEMBLY IN SALMONELLA TYPHIMURIUM.
F. Fan and R. M. Macnab (1996)
J. Biol. Chem. 271, 31981-31988
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Purification and Biochemical Properties of Saccharomyces cerevisiae's Mge1p, the Mitochondrial Cochaperone of Ssc1p.
O. Deloche and C. Georgopoulos (1996)
J. Biol. Chem. 271, 23960-23966
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Conformations of the Nucleotide and Polypeptide Binding Domains of a Cytosolic Hsp70 Molecular Chaperone Are Coupled.
K. L. Fung, L. Hilgenberg, N. M. Wang, and W. J. Chirico (1996)
J. Biol. Chem. 271, 21559-21565
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Regulation of the Heat-shock Protein 70Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40.
Y. Minami, J. Hohfeld, K. Ohtsuka, and F.-U. Hartl (1996)
J. Biol. Chem. 271, 19617-19624
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Effect of Nucleotides, Peptides, and Unfolded Proteins on the Self-association of the Molecular Chaperone HSC70.
N. Benaroudj, F. Triniolles, and M. M. Ladjimi (1996)
J. Biol. Chem. 271, 18471-18476
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Real Time Kinetics of the DnaK/DnaJ/GrpE Molecular Chaperone Machine Action.
B. Banecki and M. Zylicz (1996)
J. Biol. Chem. 271, 6137-6143
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The speed of partial reactions of the uncoating ATPase Hsc70 depends on the source of coated vesicles.
E. Buxbaum and P. G. Woodman (1996)
J. Cell Sci. 109, 705-711
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Binding of Mitochondrial Presequences to Yeast Cytosolic Heat Shock Protein 70 Depends on the Amphiphilicity of the Presequence.
T. Endo, S. Mitsui, M. Nakai, and D. Roise (1996)
J. Biol. Chem. 271, 4161-4167
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ATP Binding and Hydrolysis by the Multifunctional Protein Disulfide Isomerase.
Rég. Guthapfel, P. Guéguen, and E. Quéméneur (1996)
J. Biol. Chem. 271, 2663-2666
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Analysis of Three DnaK Mutant Proteins Suggests That Progression through the ATPase Cycle Requires Conformational Changes.
A. S. Kamath-Loeb, C. Z. Lu, W.-C. Suh, M. A. Lonetto, and C. A. Gross (1995)
J. Biol. Chem. 270, 30051-30059
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Divergent Effects of ATP on the Binding of the DnaK and DnaJ Chaperones to Each Other, or to Their Various Native and Denatured Protein Substrates.
A. Wawrzynów and M. Zylicz (1995)
J. Biol. Chem. 270, 19300-19306
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Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication.
A. Buchberger, H. Theyssen, H. Schröder, J. S. McCarty, G. Virgallita, P. Milkereit, J. Reinstein, and B. Bukau (1995)
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The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates.
T. Ziegelhoffer, P. Lopez-Buesa, and E. A. Craig (1995)
J. Biol. Chem. 270, 10412-10419
   Abstract »    Full Text »    PDF »
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Interaction of Murine BiP/GRP78 with the DnaJ Homologue MTJ1.
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Reversible Thermal Transition in GrpE, the Nucleotide Exchange Factor of the DnaK Heat-Shock System.
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Characterization of a Lidless Form of the Molecular Chaperone DnaK. DELETION OF THE LID INCREASES PEPTIDE ON- AND OFF-RATE CONSTANTS.
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Bag-1M Accelerates Nucleotide Release for Human Hsc70 and Hsp70 and Can Act Concentration-dependent as Positive and Negative Cofactor.
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