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Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment

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Abstract

HEAT shock factor (HSF)1,2, the transcriptional activator of eukaryotic heat shock genes, is induced to bind DNA by a monomer to trimer transition involving leucine zipper interactions3,4. Although this mode of regulation is shared among many eukaryotic species, there is variation in the temperature at which HSF binding activity is induced. We investigated the basis of this variation by analysing the response of a human HSF expressed in Drosophila cells and Drosophila HSF expressed in human cells. We report here that the temperature that induces DNA binding and trimerization of human HSF in Drosophila was decreased by ∼10 °C to the induction temperature for the host cell, whereas Drosophila HSF expressed in human cells was constitutively active. The results indicate that the activity of HSF in vivo is not a simple function of the absolute environmental temperature.

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Author notes

  1. Joachim Clos

    Present address: Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht Strasse 74, D-2000, Hamburg, Germany

  2. Sridhar Rabindran

    Present address: Medical Research Division, American Cyanamid Co., 401 N. Middleton Rd., Pearl River, New York, 10965, USA

  3. Carl Wu: To whom correspondence should be addressed.

Authors and Affiliations

  1. >Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Building 37, Rm 4C-09, Bethesda, Maryland, 20892, USA

    Joachim Clos, Sridhar Rabindran, Jan Wisniewski & Carl Wu

Authors
  1. Joachim Clos
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  2. Sridhar Rabindran
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  3. Jan Wisniewski
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  4. Carl Wu
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Clos, J., Rabindran, S., Wisniewski, J. et al. Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment. Nature 364, 252–255 (1993). https://doi.org/10.1038/364252a0

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  • DOI: https://doi.org/10.1038/364252a0

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