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Science 3 August 1990:
Vol. 249. no. 4968, pp. 546 - 549
DOI: 10.1126/science.2200124

Articles

Science, Vol 249, Issue 4968, 546-549
Copyright © 1990 by American Association for the Advancement of Science


articles

Antibody-mediated activation of Drosophila heat shock factor in vitro

V Zimarino, S Wilson, and C Wu

Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

Eukaryotic cells respond to elevated temperatures by rapidly activating the expression of heat shock genes. Central to this activation is heat shock-inducible binding of the transcriptional activator, termed heat shock factor (HSF), to common regulatory elements, which are located upstream of all heat shock genes. The DNA binding activity of the inactive form of Drosophila HSF was induced in vitro by treatment with polyclonal antibodies to the purified, in vivo-activated factor. This finding, together with observations that high temperature and low pH activate HSF binding in vitro, suggests that the inactive form of HSF can directly recognize and transduce the heat shock signal without undergoing a covalent modification of protein structure.


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Mammalian SWI-SNF Complexes Contribute to Activation of the hsp70 Gene.
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Sensitivity of Drosophila Heat Shock Transcription Factor to Low pH.
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Intramolecular Repression of Mouse Heat Shock Factor 1.
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Canonical Heat Shock Element in the alpha B-crystallin Gene Shows Tissue-specific and Developmentally Controlled Interactions with Heat Shock Factor.
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