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Science 18 May 1990:
Vol. 248. no. 4957, pp. 850 - 854
DOI: 10.1126/science.2188360

Articles

Science, Vol 248, Issue 4957, 850-854
Copyright © 1990 by American Association for the Advancement of Science


articles

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly

RP Beckmann, LE Mizzen, and WJ Welch

Department of Medicine, University of California, San Francisco 94143.

The 70-kilodalton family of heat shock proteins (Hsp 70) has been implicated in posttranslational protein assembly and translocation. Binding of cytosolic forms of Hsp 70 (Hsp 72,73) with nascent proteins in the normal cell was investigated and found to be transient and adenosine triphosphate (ATP)-dependent. Interaction of Hsp 72,73 with newly synthesized proteins appeared to occur cotranslationally, because nascent polypeptides released prematurely from polysomes in vivo can be isolated in a complex with Hsp 72,73. Moreover, isolation of polysomes from short-term [35S]Met-labeled cells (pulsed) revealed that Hsp 72,73 associated with nascent polypeptide chains. In cells experiencing stress, newly synthesized proteins coimmunoprecipitated with Hsp 72,73; however, in contrast to normal cells, interaction with Hsp 72,73 was not transient. A model consistent with these data suggests that under normal growth conditions, cytosolic Hsp 72,73 interact transiently with nascent polypeptides to facilitate proper folding, and that metabolic stress interferes with these events.


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The Cysteine String Secretory Vesicle Protein Activates Hsc70 ATPase.
J. E.A. Braun, S. M. Wilbanks, and R. H. Scheller (1996)
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Evidence That a Rapidly Turning Over Protein, Normally Degraded by Proteasomes, Regulates hsp72 Gene Transcription in HepG2 Cells.
M. Zhou, X. Wu, and H. N. Ginsberg (1996)
J. Biol. Chem. 271, 24769-24775
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Overexpression of Heat Shock Protein 72 in Transgenic Mice Decreases Infarct Size In Vivo.
J. J. Hutter, R. Mestril, E. K.W. Tam, R. E. Sievers, W. H. Dillmann, and C. L. Wolfe (1996)
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Regulation of the Heat-shock Protein 70Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40.
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Purification and Characterization of a 66-kDa Protein from Rabbit Reticulocyte Lysate Which Promotes the Recycling of Hsp 70.
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Effect of Scrapie Infection on the Activity of Neuronal Nitric-oxide Synthase in Brain and Neuroblastoma Cells.
H. Ovadia, H. Rosenmann, E. Shezen, M. Halimi, I. Ofran, and R. Gabizon (1996)
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J. Biol. Chem. 270, 25220-25224
   Abstract »    Full Text »    PDF »
Polymerization of 70-kDa Heat Shock Protein by Yeast DnaJ in ATP.
C. King, E. Eisenberg, and L. Greene (1995)
J. Biol. Chem. 270, 22535-22540
   Abstract »    Full Text »    PDF »
70-kDa Heat Shock Cognate Protein Interacts Directly with the N-terminal Region of the Retinoblastoma Gene Product pRb.
A. Inoue, T. Torigoe, K. Sogahata, K. Kamiguchi, S. Takahashi, Y. Sawada, M. Saijo, Y. Taya, S.-i. Ishii, N. Sato, et al. (1995)
J. Biol. Chem. 270, 22571-22576
   Abstract »    Full Text »    PDF »
Components of the Protein Synthesis and Folding Machinery Are Induced in Vascular Smooth Muscle Cells by Hypertrophic and Hyperplastic Agents.
W. F. Patton, H. Erdjument-Bromage, A. R. Marks, P. Tempst, and M. B. Taubman (1995)
J. Biol. Chem. 270, 21404-21410
   Abstract »    Full Text »    PDF »
Heat Shock Enhances the Susceptibility of Tumor Cells to Lysis by Lymphokine-Activated Killer Cells.
S. Fujieda, I. Noda, H. Saito, T. Hoshino, and M. Yagita (1995)
Arch Otolaryngol Head Neck Surg 121, 1009-1014
   Abstract »    PDF »
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
   Abstract »    Full Text »    PDF »
Calf Thymus Hsc70 Protein Protects and Reactivates Prokaryotic and Eukaryotic Enzymes.
A. Ziemienowicz, M. Zylicz, C. Floth, and U. Hübscher (1995)
J. Biol. Chem. 270, 15479-15484
   Abstract »    Full Text »    PDF »
Accelerated recovery of postischemic stunned myocardium after induced expression of myocardial heat-shock protein (HSP70).
B. L. Robinson, T. Morita, D. O. Toft, and J. J. Morris (1995)
J. Thorac. Cardiovasc. Surg. 109, 753-764
   Abstract »    Full Text »
Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock Protein.
L. E. Greene, R. Zinner, S. Naficy, and E. Eisenberg (1995)
J. Biol. Chem. 270, 2967-2973
   Abstract »    Full Text »    PDF »
Enzyme Assembly after de Novo Synthesis in Rabbit Reticulocyte Lysate Involves Molecular Chaperones and Immunophilins.
M. Kruse, M. Brunke, A. Escher, A. A. Szalay, M. Tropschug, and R. Zimmermann (1995)
J. Biol. Chem. 270, 2588-2594
   Abstract »    Full Text »    PDF »
Heat shock protein (HSP 72) expression in patients undergoing cardiac operations.
L. B. McGrath, M. Locke, M. Cane, C. Chen, and C. D. Ianuzzo (1995)
J. Thorac. Cardiovasc. Surg. 109, 370-376
   Abstract »    Full Text »
Isoalloxazine Ring of FAD Is Required for the Formation of the Core in the Hsp60-assisted Folding of Medium Chain Acyl-CoA Dehydrogenase Subunit into the Assembly Competent Conformation in Mitochondria.
T. Saijo and K. Tanaka (1995)
J. Biol. Chem. 270, 1899-1907
   Abstract »    Full Text »    PDF »



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