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Science 28 July 1989:
Vol. 245. no. 4916, pp. 385 - 390
DOI: 10.1126/science.2756425

Articles

Science, Vol 245, Issue 4916, 385-390
Copyright © 1989 by American Association for the Advancement of Science


articles

Peptide binding and release by proteins implicated as catalysts of protein assembly

GC Flynn, TG Chappell, and JE Rothman

Department of Biology, Lewis Thomas Laboratory, Princeton University, NJ 08544.

Two members of the hsp70 family, termed hsc70 and BiP, have been implicated in promoting protein folding and assembly processes in the cytoplasm and the lumen of the endoplasmic reticulum, respectively. Short hydrophilic (8 to 25 residues) synthetic peptides have now been tested as possible mimics of polypeptide chain substrates to help define an enzymatic basis for these activities. Both BiP and hsc70 have specific peptide binding sites. Peptide binding elicits hydrolysis of adenosine triphosphate, with the subsequent release of bound peptide.


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J. Biol. Chem. 270, 19839-19844
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Folding of Human Intestinal Lactase-phlorizin Hydrolase.
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J. Biol. Chem. 270, 18678-18684
   Abstract »    Full Text »    PDF »
Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca[IMAGE].
W.-J. Ou, J. J. M. Bergeron, Y. Li, C. Y. Kang, and D. Y. Thomas (1995)
J. Biol. Chem. 270, 18051-18059
   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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Calf Thymus Hsc70 Protein Protects and Reactivates Prokaryotic and Eukaryotic Enzymes.
A. Ziemienowicz, M. Zylicz, C. Floth, and U. Hübscher (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
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A 110-amino Acid Region within the A1-domain of Coagulation Factor VIII Inhibits Secretion from Mammalian Cells.
K. A. Marquette, D. D. Pittman, and R. J. Kaufman (1995)
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To fold or not to fold....
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J. Bangs, L Uyetake, M. Brickman, A. Balber, and J. Boothroyd (1993)
J. Cell Sci. 105, 1101-1113
   Abstract »    PDF »
The nuclear membrane.
C Dingwall and R Laskey (1992)
Science 258, 942-947
   Abstract »    PDF »
Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins.
S. Nadler, M. Tepper, B Schacter, and C. Mazzucco (1992)
Science 258, 484-486
   Abstract »    PDF »
The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression..
K Abravaya, M P Myers, S P Murphy, and R I Morimoto (1992)
Genes & Dev. 6, 1153-1164
   Abstract »    PDF »
A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.
S. Hardy and L. Randall (1991)
Science 251, 439-443
   Abstract »    PDF »
Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.
R. Beckmann, L. Mizzen, and W. Welch (1990)
Science 248, 850-854
   Abstract »    PDF »
Protein sorting to mitochondria: evolutionary conservations of folding and assembly.
F. Hartl and W Neupert (1990)
Science 247, 930-938
   Abstract »    PDF »



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