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Vol. 11, Issue 7, 2335-2347, July 2000
and
*Division of Yeast Genetics, National Institute for Medical
Research, The Ridgeway, London NW7 1AA, United Kingdom;
The Skn7 response regulator has previously been shown to play a
role in the induction of stress-responsive genes in yeast, e.g., in the
induction of the thioredoxin gene in response to hydrogen peroxide. The
yeast Heat Shock Factor, Hsf1, is central to the induction of another
set of stress-inducible genes, namely the heat shock genes. These two
regulatory trans-activators, Hsf1 and Skn7, share
certain structural homologies, particularly in their DNA-binding
domains and the presence of adjacent regions of coiled-coil structure,
which are known to mediate protein-protein interactions. Here, we
provide evidence that Hsf1 and Skn7 interact in vitro and in vivo and
we show that Skn7 can bind to the same regulatory sequences as Hsf1,
namely heat shock elements. Furthermore, we demonstrate that a strain
deleted for the SKN7 gene and containing a
temperature-sensitive mutation in Hsf1 is hypersensitive to oxidative
stress. Our data suggest that Skn7 and Hsf1 cooperate to achieve
maximal induction of heat shock genes in response specifically to
oxidative stress. We further show that, like Hsf1, Skn7 can interact
with itself and is localized to the nucleus under normal growth
conditions as well as during oxidative stress.
Department of Biochemistry and Molecular Biology,
Louisiana State University Health Sciences Center, Shreveport,
Louisiana 71130; §Department of Molecular Microbiology,
Research Institute for Microbial Diseases, Osaka University, Osaka 565, Japan; and Department of Biochemistry and Genetics,
Medical School, University of Newcastle, Newcastle-Upon-Tyne NE2 4HH,
United Kingdom
Corresponding author. E-mail address:
desmond_raitt{at}dfci.harvard.edu.
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