Inhibition of HeLa cell protein synthesis under heat shock conditions in the absence of initiation factor eIF-2 alpha phosphorylation.
Subjecting a HeLa cell suspension culture to an increase in incubation temperature (from 37 degrees to 42 degrees 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 (less than 20 min) is due to the phosphorylation of initiation factor eIF-2 in its alpha 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-2 alpha 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-2 alpha phosphorylation.
D015852:Eukaryotic Initiation Factor-2; D006367:HeLa Cells / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D010448:Peptide Initiation Factors / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D019892:eIF-2 Kinase
D015852:Eukaryotic Initiation Factor-2; D006360:Heat-Shock Proteins; D009363:Neoplasm Proteins; D010448:Peptide Initiation Factors; D011506:Proteins; D011494:Protein Kinases; D019892:eIF-2 Kinase