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Molecular and Cellular Biology, April 2001, p. 2726-2735, Vol. 21, No. 8
Department of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, Boston,
Massachusetts, 02115
Received 28 November 2000/Returned for modification 17 January
2001/Accepted 22 January 2001
We analyzed the relationship between histone acetylation and
transcriptional regulation at 40 Saccharomyces cerevisiae
promoters that respond to specific activators and repressors. In accord with the general correlation between histone acetylation and
transcriptional activity, Gcn4 and the general stress activators (Msn2
and Msn4) cause increased acetylation of histones H3 and H4.
Surprisingly, Gal4-dependent activation is associated with a dramatic
decrease in histone H4 acetylation, whereas acetylation of histone H3
is unaffected. A specific decrease in H4 acetylation is also observed, to a lesser extent, at promoters activated by Hap4, Adr1, Met4, and
Ace1. Activation by heat shock factor has multiple effects; H4
acetylation increases at some promoters, whereas other promoters show
an apparent decrease in H3 and H4 acetylation that probably reflects
nucleosome loss or gross alteration of chromatin structure. Repression
by targeted recruitment of the Sin3-Rpd3 histone deacetylase is
associated with decreased H3 and H4 acetylation, whereas repression by
Cyc8-Tup1 is associated with decreased H3 acetylation but variable effects on H4 acetylation; this suggests that Cyc8-Tup1 uses multiple mechanisms to reduce histone acetylation at promoters. Thus, individual activators confer distinct patterns of histone acetylation on target
promoters, and transcriptional activation is not necessarily associated
with increased acetylation. We speculate that the activator-specific decrease in histone H4 acetylation is due to blocking the access or
function of an H4-specific histone acetylase such as Esa1.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.8.2726-2735.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Histone Acetylation at Promoters Is Differentially
Affected by Specific Activators and Repressors
*
Corresponding author. Mailing address: Department of
Biological Chemistry and Molecular Pharmacology, Harvard Medical
School, Boston, MA 02115. Phone: (617) 432-2104. Fax: (617) 432-2529. E-mail: kevin{at}hms.harvard.edu.
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