Translational control during heat shock.
Regulation of translation during heat shock of Drosophila and mammalian cells is reviewed. Protein synthesis is severely inhibited by elevated temperatures but synthesis of heat shock proteins (HSPs) is resistant to this inhibition. The primary site of regulation is polypeptide chain initiation. The activities of two initiation factors, eIF-2 and eIF-4F, are modulated during heat shock. A protein kinase which modulates eIF-2 activity appears to be associated with heat shock proteins (HSPs). Evidence is emerging that HSP70 acts as a heat sensor by detecting the presence of accumulating denatured proteins. In the rabbit reticulocyte lysate denatured proteins bind HSP70 releasing an eIF-2 kinase to shut down protein synthesis. It appears highly likely that a similar mechanism is acting in heat shocked cells. Cell-free protein synthesizing systems prepared from heat shocked cells are deficient in eIF-4F. Modulation of eIF-4F can explain in part the apparent preferential translation of HSP mRNAs.
Panniers
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National Institutes of Health, Bethesda, MD 20892, USA.
D000818:Animals; D002478:Cells, Cultured; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D039562:Eukaryotic Initiation Factor-4F; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D010442:Peptide Chain Initiation, Translational; D010448:Peptide Initiation Factors / Q000378:metabolism; D014176:Protein Biosynthesis; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D019892:eIF-2 Kinase
D015852:Eukaryotic Initiation Factor-2; D039562:Eukaryotic Initiation Factor-4F; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D010448:Peptide Initiation Factors; D017346:Protein Serine-Threonine Kinases; D019892:eIF-2 Kinase