Nucleic Acids Research, Vol 24, Issue 2 367-374, Copyright © 1996 by Oxford University Press
J Wisniewski, A Orosz, R Allada and C Wu
The heat shock transcription factor (HSF) is constitutively expressed in
Drosophila cells as an inactive monomer. Upon heat shock HSF undergoes
trimerization and acquires high affinity DNA binding ability leading to
specific interaction with its cognate elements in heat shock promoters.
Here we show that the transactivation function of HSF is conferred by the
extreme C-terminal region of the protein. Deletion analysis of HSF
fragments fused to the GAL4 DNA-binding domain demonstrates that
transactivation is dependent on HSF residues 610-691. This domain is
located beyond the C-terminal heptad repeat (leucine zipper 4) whose
presence or integrity is dispensable for transactivation. The
transactivation domain is functional in the absence of heat shock and can
be replaced by the extreme C-terminal region of human HSF1. The Drosophila
and human HSF transactivation domains are both rich in hydrophobic and
acidic residues and may be structurally conserved, despite limited sequence
identity.
ARTICLES
The C-terminal region of Drosophila heat shock factor (HSF) contains a constitutively functional transactivation domain
Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
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