Accumulation of heat shock protein 70 RNA and its relationship to protein synthesis after heat shock in mammalian cells.
Heat stress induces a set of heat shock proteins (hsps) in a wide variety of species. In response to either a mild (5 min X 45 degrees C) or severe (30 min X 45 degrees C) heat shock, the timing of expression of the hsps and the recovery of general protein synthesis in rat embryonic fibroblasts was dependent on the duration of the hyperthermic exposure. Synthesis of mRNA coding for an hsp of Mr approximately equal to 70,000 (hsp 70) followed immediately after the mild heat shock but was delayed after the severe heat shock. Appearance of the hsps paralleled the synthesis and decay of RNA and was indicative that new RNA synthesis was required for hsp 70 expression. Inhibition of protein synthesis by cycloheximide after the mild heat shock increased the maximal accumulation of hsp 70 encoding mRNA but did not prevent the subsequent decrease in this mRNA species. These results suggest that mammalian cells control the expression of hsp 70 primarily at the level of transcription, and that the normal pattern of hsp 70 mRNA turnover after an inducing heat stress is not dependent on new protein synthesis.
D000818:Animals; D002460:Cell Line; D003513:Cycloheximide / Q000494:pharmacology; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics*; D006358:Hot Temperature; D008970:Molecular Weight; D009693:Nucleic Acid Hybridization; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D051381:Rats; D014158:Transcription, Genetic
D006360:Heat-Shock Proteins; D012333:RNA, Messenger; D003513:Cycloheximide