The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock.
When heat-shocked Drosophila cells are returned to normal temperatures, heat-shock protein (HSP) synthesis is repressed and normal protein synthesis is restored. The repression of HSP70 synthesis is accompanied by the selective degradation of its mRNA. We have engineered cells to produce a modified hsp70 mRNA that behaves exactly as the wild-type message. That is, it is stable during heat shock but degraded during recovery when protein synthesis returns to normal. When this message, placed under the control of the metallothionein promoter, is induced at normal temperatures it is rapidly degraded, with a half life of 15-30 min. Apparently, the hsp70 message is inherently unstable. During heat-shock, degradation of the message is suspended; during recovery degradation is restored.
Petersen
R
R
Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.
Lindquist
S
S
D000818:Animals; D004330:Drosophila / Q000235:genetics*; D005786:Gene Expression Regulation; D005796:Genes; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics*; D006358:Hot Temperature; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism; D013045:Species Specificity; D014158:Transcription, Genetic
D006360:Heat-Shock Proteins; D012333:RNA, Messenger