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Science 8 January 1993: Vol. 259. no. 5092, pp. 230 - 234 DOI: 10.1126/science.8421783
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Articles
Science, Vol 259, Issue 5092, 230-234
Copyright © 1993 by American Association for the Advancement of Science
Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
SK Rabindran,
RI Haroun,
J Clos,
J Wisniewski,
and
C Wu
Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
The human and Drosophila heat shock transcription factors (HSFs) are multi-zipper proteins with high-affinity binding to DNA that is regulated by heat shock-induced trimerization. Formation of HSF trimers is dependent on hydrophobic heptad repeats located in the amino-terminal region of the protein. Two subregions at the carboxyl-terminal end of human HSF1 were identified that maintain the monomeric form of the protein under normal conditions. One of these contains a leucine zipper motif that is conserved between vertebrate and insect HSFs. These results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino-terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.
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