Translational control during recovery from heat shock in the absence of heat shock proteins.
Heat shock results in a reduction in translational efficiency and an increase in mRNA stability in plants that is proportional to the severity of the stress. To determine whether the absence of heat shock proteins may affect the observed changes during translation or mRNA turnover, the effect that inhibiting transcription during a heat shock has on the subsequent translation of a reporter mRNA was examined. The presence of actinomycin D repressed heat shock protein synthesis in response to the application of a heat shock by more than 80%. The translational efficiency of the reporter mRNA was subject to a greater degree of repression following a heat shock when transcription was inhibited than it was in heat-shocked cells in which transcription was not inhibited. In contrast, inhibiting transcription during a heat shock did not prevent the heat-mediated increase in mRNA stability. These data suggest that ongoing transcription is needed during a heat shock to support a basal level of translational activity in the subsequent recovery from the stress but does not appear to be required for the heat-mediated increase in mRNA stability.
Gallie
D R
DR
Department of Biochemistry, University of California, Riverside 92521-0129, USA.
Pitto
L
L
D000818:Animals; D002478:Cells, Cultured; D001517:Coleoptera; D003609:Dactinomycin / Q000494:pharmacology; D018552:Daucus carota; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D007700:Kinetics; D008156:Luciferases / Q000096:biosynthesis; D014176:Protein Biosynthesis; D011523:Protoplasts; D012333:RNA, Messenger / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis; D014158:Transcription, Genetic / Q000187:drug effects; D014162:Transfection
D006360:Heat-Shock Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D003609:Dactinomycin; D008156:Luciferases