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A more recent version of this article appeared on January 12, 2001
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Papers In Press, published online ahead of print October 30, 2000
J. Biol. Chem, 10.1074/jbc.M008668200
Submitted on September 21, 2000
Revised on October 30, 2000
Accepted on October 27, 2000

Recruitment of the yeast Tup1p-Ssn6p repressor is associated with localized decreases in histone acetylation

James R. Bone and Sharon Y. Roth

Biochemistry and Molecular Biology Box 117, UT M.D. Anderson Cancer Center, Houston, Texas 77030

Corresponding Author: syr{at}mdacc.tmc.edu

Post-translational 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. Previously we demonstrated 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 under acetylated 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 to induce decreased acetylation of H3 and H4 at a target promoter. Together our results suggest that stable decreases in histone acetylation levels are directed and/or maintained by the Tup1p-Ssn6p repressor complex.


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