Abstract
In eukaryotic cells, the synthesis of heat shock proteins is subject to transcriptional and post-transcriptional control in eukaryotic cells (reviewed by Craig, 1985; Lindquist, 1986). Heat shock-inducible transcription is mediated by a positive control element, the heat shock element (HSE), defined as three repeats of a 5-nucleotide [-GAA-] module, arranged in alternating orientation (Pelham, 1982; Amin etal., 1988; Xiao and Lis, 1988). Multiple copies of the HSE are found upstream of all heat shock genes. A heat shock transcriptional activator, termed heat shock factor (HSF), binds to HSEs and activates transcription of heat shock genes in vitro (Wu, 1984a; Wu, 1984b; Parker and Topol, 1984; Topol etal., 1985). Although the sequence of the HSE has been highly conserved in evolution, HSF purified from yeast, Drosophila, and human cells differ in molecular size (150 kD, 110 kD and 83 kD, respectively; Sorger and Pelham, 1987; Wu et al., 1987; Goldenberg etal., 1988). Yeast and higher eukaryotes also differ in the regulation of HSF activity. In yeast, HSF bound constitutively to the HSE apparently stimulates transcription when phosphorylated under heat shock conditions. In Drosophila and vertebrate cells, HSF is unable to bind to the HSE unless the cells are heat shocked (for a review, see Wu etal., 1990). The heat-inducible binding of HSF appears to be a major regulatory step in the pathway to heat shock gene activation in higher eukaryotes.
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© 1991 Springer-Verlag Berlin Heidelberg
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Wu, C., Clos, J., Westwood, J.T., Zimarino, V., Becker, P.B., Wilson, S. (1991). Structure and Function of Drosophila Heat Shock Factor. In: Maresca, B., Lindquist, S. (eds) Heat Shock. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76679-4_2
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DOI: https://doi.org/10.1007/978-3-642-76679-4_2
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