RT Journal Article
SR Electronic
T1 Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
JF Science
JO Science
FD American Association for the Advancement of Science
SP 230
OP 234
DO 10.1126/science.8421783
VO 259
IS 5092
A1 Rabindran, SK
A1 Haroun, RI
A1 Clos, J
A1 Wisniewski, J
A1 Wu, C
YR 1993
UL http://science.sciencemag.org/content/259/5092/230.abstract
AB 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.