pubmed-article:16204210 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C0027746 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C2004454 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
pubmed-article:16204210 | lifeskim:mentions | umls-concept:C1517945 | lld:lifeskim |
pubmed-article:16204210 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:16204210 | pubmed:dateCreated | 2006-1-30 | lld:pubmed |
pubmed-article:16204210 | pubmed:abstractText | The heat-shock response is a programmed change in gene expression carried out by cells in response to environmental stress, such as heat. This response is universal and is characterized by the synthesis of a small group of conserved protein chaperones. In Drosophila melanogaster the Hsp70 chaperone dominates the profile of protein synthesis during the heat-shock response. We recently generated precise deletion alleles of the Hsp70 genes of D. melanogaster and have used those alleles to characterize the phenotypes of Hsp70-deficient flies. Flies with Hsp70 deletions have reduced thermotolerance. We find that Hsp70 is essential to survive a severe heat shock, but is not required to survive a milder heat shock, indicating that a significant degree of thermotolerance remains in the absence of Hsp70. However, flies without Hsp70 have a lengthened heat-shock response and an extended developmental delay after a non-lethal heat shock, indicating Hsp70 has an important role in recovery from stress, even at lower temperatures. Lack of Hsp70 also confers enhanced sensitivity to a temperature-sensitive lethal mutation and to the neurodegenerative effects produced by expression of a human polyglutamine disease protein. | lld:pubmed |
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