2007
DOI: 10.1379/csc-308.1
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The Hsp27 gene is not required for Drosophila development but its activity is associated with starvation resistance

Abstract: Heat shock proteins are induced under stress conditions and they act as molecular chaperones to refold denatured polypeptides. Stress resistances including thermotolerance generally are correlated with levels of the heat shock proteins. We investigated a fruit fly gene encoding a small heat shock protein, Hsp27, to determine if it functions in stress response of Drosophila melanogaster.

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Cited by 46 publications
(26 citation statements)
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“…Hsp27 is expressed highly in fly neuronal tissue where it increases resistance to oxidative stress (Liao et al, 2008). It is essential for development and specifically acts as a molecular chaperone to refold denatured proteins generated under starvation conditions (Hao et al, 2007). Transcription of the other stress protein, Hsp23 is regulated during development by binding of the ecdysone-receptor complex to the promoter region of the Hsp23 gene (Mestril et al, 1986).…”
Section: Resultsmentioning
confidence: 99%
“…Hsp27 is expressed highly in fly neuronal tissue where it increases resistance to oxidative stress (Liao et al, 2008). It is essential for development and specifically acts as a molecular chaperone to refold denatured proteins generated under starvation conditions (Hao et al, 2007). Transcription of the other stress protein, Hsp23 is regulated during development by binding of the ecdysone-receptor complex to the promoter region of the Hsp23 gene (Mestril et al, 1986).…”
Section: Resultsmentioning
confidence: 99%
“…Three day old flies (formulation fed and control) were starved in empty bottles containing filter paper strips soaked with water [61]. Mortality of starved flies was recorded every 12 hours.…”
Section: Methodsmentioning
confidence: 99%
“…Together, these results suggest that Hsp27 may be required for differentiation of muscle cells. In contrast, Drosophila embryos lacking a homolog of human Hsp27 develop normally and, surprisingly, loss of Hsp27 does not alter the resistance of flies to heat shock or oxidative injury (Hao et al 2007). The Drosophila homolog of Hsp27 lacks phosphorylated serines conserved among vertebrate homologs of Hsp27 (Ingolia and Craig 1982) and displays a constitutive localization to the nucleus of cells under control conditions (Marin and Tanguay 1996) not typical of vertebrate Hsp27.…”
Section: Introductionmentioning
confidence: 99%