The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock

Robert Petersen, Susan Lindquist

Research output: Contribution to journalArticlepeer-review

79 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)161-168
Number of pages8
JournalGene
Volume72
Issue number1-2
DOIs
StatePublished - Dec 10 1988

Keywords

  • RNA turnover
  • Recombinant DNA
  • heat shock recovery
  • metallothionein promoter
  • stress response
  • translational control

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