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Inhibition of HeLa cell protein synthesis under heat shock conditions in the absence of initiation factor eIF-2α phosphorylation

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
138
Issue
2
Identifiers
DOI: 10.1016/s0006-291x(86)80527-7
Disciplines
  • Biology

Abstract

Subjecting a HeLa cell suspension culture to an increase in incubation temperature (from 37° to 42°C) results in the rapid cessation of polypeptide chain synthesis followed by a gradual increase in the synthesis of a class of polypeptides referred to as the heat-shock proteins. It has been proposed that the initial, rapid shutoff of protein synthesis (<20 min) is due to the phosphorylation of initiation factor eIF-2 in its α subunit, a modification known to result in the inhibition of polypeptide synthesis. Using an in vitro translation system derived from heat-shocked HeLa cells grown in suspension culture, we were unable to find any evidence implicating eIF-2α phosphorylation in the initial shutoff of translation during the heat shock response. These results suggest that the rapid inhibition of protein synthesis observed under heat shock conditions is mediated by a mechanism(s) other than eIF-2α phosphorylation.

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