Document Type
Article
Publication Date
2000
Publication Title
Molecular and Cellular Biology
First Page
6435
Last Page
6448
DOI
http://dx.doi.org/10.1128/MCB.20.17.6435-6448.2000
Abstract
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-ΔHSE1). 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.
Rights
This article was archived with permission from American Society for Microbiology, all rights reserved. Document also available from Molecular and Cellular Biology.
Recommended Citation
Venturi, Christina Bourgeois; Erkine, Alexander M.; and Gross, David S., "Cell Cycle-Dependent Binding of Yeast Heat Shock Factor to Nucleosomes" (2000). Scholarship and Professional Work – COPHS. 142.
https://digitalcommons.butler.edu/cophs_papers/142
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