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Science 28 July 1989: Vol. 245. no. 4916, pp. 385 - 390 DOI: 10.1126/science.2756425
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Articles
Science, Vol 245, Issue 4916, 385-390
Copyright © 1989 by American Association for the Advancement of Science
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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