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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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Interaction between the Nucleotide Exchange Factor Mge1 and the Mitochondrial Hsp70 Ssc1.
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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)
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Refolding Intermediates of Acid-unfolded Mitochondrial Aspartate Aminotransferase Bind to hsp70.
A. Artigues, A. Iriarte, and M. Martinez-Carrion (1997)
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P. A. Wearsch and C. V. Nicchitta (1997)
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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)
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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)
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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)
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   Abstract »    Full Text »    PDF »
Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication.
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The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates.
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The Conserved G/F Motif of the DnaJ Chaperone Is Necessary for the Activation of the Substrate Binding Properties of the DnaK Chaperone.
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Complex Multigene Family of Functionally Distinct Hsp70s of Yeast.
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Cold Spring Harb Symp Quant Biol 60, 441-449
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Interaction of Murine BiP/GRP78 with the DnaJ Homologue MTJ1.
M. Chevalier, H. Rhee, E. C. Elguindi, and S. Y. Blond (2000)
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Identification of an Inhibitor of hsc70-mediated Protein Translocation and ATP Hydrolysis.
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