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J. Biol. Chem., Vol. 276, Issue 3, 1808-1813, January 19, 2001
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and§¶
From the Posttranslational acetylation of histones is an
important element of transcriptional regulation. The yeast Tup1p
repressor is one of only a few non-enzyme proteins known to interact
directly with the amino-terminal tail domains of histones H3 and H4
that are subject to acetylation. We demonstrated previously that Tup1p interacts poorly with more highly acetylated isoforms of these histones
in vitro. Here we show that two separate classes of
promoters repressed by Tup1p are associated with underacetylated
histones in vivo. This decreased histone acetylation is
dependent upon Tup1p and its partner Ssn6p and is localized to
sequences near the point of Tup1p-Ssn6p recruitment. Increased
acetylation of histones H3 and H4 is observed upon activation of these
genes, but this increase is not dependent on transcription per
se. Direct recruitment of Tup1p-Ssn6p complexes via fusion of
Tup1p to the lexA DNA binding domain is sufficient to confer repression
and induce decreased acetylation of H3 and H4 at a target promoter. Taken together, our results suggest that stable decreases in histone acetylation levels are directed and/or maintained by the Tup1p-Ssn6p repressor complex.
Department of Biochemistry and Molecular
Biology and § Program in Genes and Development, The
University of Texas M. D. Anderson Cancer Center, Houston, Texas
77030
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