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J. Biol. Chem., Vol. 278, Issue 10, 7755-7764, March 7, 2003
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From the Department of Biochemistry and Molecular Biology,
Louisiana State University Health Sciences Center,
Shreveport, Louisiana 71130
The activation domains (ADs) of transcription
activators recruit a multiplicity of enzymatic activities to gene
promoters. The mechanisms by which such recruitment takes place are not
well understood. Using chromatin immunoprecipitation, we demonstrate dynamic alterations in the abundance of histones H2A, H3, and H4 at
promoters of genes regulated by the HSF and Gal4 activators of
Saccharomyces cerevisiae. Transcriptional activation of
these genes, particularly those regulated by HSF, is accompanied by a
significant reduction in both acetylated and unacetylated histones at
promoters and may involve the transient displacement of histone octamers. To gain insight into the function of ADs, we conducted a
genetic screen to identify polypeptides that could substitute for the
340-residue C-terminal activator of HSF and rescue the temperature sensitivity caused by its deletion. We found that the
ts
Dynamic Chromatin Alterations Triggered by Natural and
Synthetic Activation Domains*
and
phenotype of HSF(1-493) could be
complemented by peptides as short as 11 amino acids. Such peptides are
enriched in acidic and hydrophobic residues, and exhibit both
trans-activating and chromatin-modifying activities when
fused to the Gal4 DNA-binding domain. We also demonstrate that a
previously identified 14-amino acid histone H3-binding module of human
CTF1/NF1, which is similar to synthetic ADs, can substitute for the HSF
C-terminal activator in conferring temperature resistance and can
mediate the modification of promoter chromatin structure. Possible
mechanisms of AD function, including one involving direct interactions
with histones, are discussed.
*
This work was supported by National Institute of General
Medical Sciences Grant GM45842 and the Center for Excellence in Cancer Research at Louisiana State University Health Sciences Center, Shreveport, LA (to D. S. G.) and by National Science Foundation Grant
MCB-0215758 (to A. M. E.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Department of
Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130-3932. Tel.: 318-675-8204; Fax:
318-675-5180; E-mail: aerkin@lsuhsc.edu.
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