Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1989-6-5
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock.
pubmed:affiliation
Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.