Abstract
Highly purified preparations of three kinds of HSP70 can inhibit formation of polypeptides made in vitro utilizing either extracts of rabbit reticulocytes or wheat germ and several different mRNAs. Inhibition was dose-dependent over a range of 0.1–0.4 nmoles of HSP70 and more pronounced at low temperatures. When bromo mosaic virus mRNAs were tested, inhibition was greater for the larger polypeptides indicating that HSP70 blocks nascent polypeptide elongation. With Sindbis virus 26S mRNA, the addition of HSP70 affected the formation of the capsid autoprotease activity leading to larger translation products. All of these data suggest that high concentrations of HSP70 can perturb the normal folding of nascent polypeptides and could explain why cells carefully autoregulate the level of HSP70.
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© 1991 Springer-Verlag Berlin Heidelberg
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Schlesinger, M.J., Ryan, C., Sadis, S., Hightower, L.E. (1991). In vitro Inhibition of Nascent Polypeptide Formation by HSP70 Proteins. In: Maresca, B., Lindquist, S. (eds) Heat Shock. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76679-4_12
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DOI: https://doi.org/10.1007/978-3-642-76679-4_12
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