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Molecular and Cellular Biology, September 2000, p. 6435-6448, Vol. 20, No. 17
Department of Biochemistry and Molecular
Biology, Louisiana State University Health Sciences Center,
Shreveport, Louisiana 71130
Received 23 February 2000/Returned for modification 4 April
2000/Accepted 16 May 2000
In the nucleus, transcription factors must contend with the
presence of chromatin in order to gain access to their cognate regulatory sequences. As most nuclear DNA is assembled into
nucleosomes, activators must either invade a stable, preassembled
nucleosome or preempt the formation of nucleosomes on newly replicated
DNA, which is transiently free of histones. We have investigated the mechanism by which heat shock factor (HSF) binds to target nucleosomal heat shock elements (HSEs), using as our model a dinucleosomal heat
shock promoter (hsp82-
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Cell Cycle-Dependent Binding of Yeast Heat Shock
Factor to Nucleosomes
HSE1). We find that activated HSF cannot bind a stable, sequence-positioned nucleosome in
G1-arrested cells. It can do so readily, however, following
release from G1 arrest or after the imposition of either an
early S- or late G2-phase arrest. Surprisingly, despite the
S-phase requirement, HSF nucleosomal binding activity is restored in
the absence of hsp82 replication. These results contrast
with the prevailing paradigm for activator-nucleosome interactions and
implicate a nonreplicative, S-phase-specific event as a prerequisite
for HSF binding to nucleosomal sites in vivo.
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130-3932. Phone: (318) 675-5027. Fax:
(318) 675-5180. E-mail: dgross{at}lsuhsc.edu.
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