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Molecular and Cellular Biology, September 1998, p. 5121-5127, Vol. 18, No. 9
Department of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, Boston,
Massachusetts 02115
Received 15 May 1998/Returned for modification 3 June 1998/Accepted 16 June 1998
Eukaryotic organisms contain a multiprotein complex that includes
Rpd3 histone deacetylase and the Sin3 corepressor. The Sin3-Rpd3 complex is recruited to promoters by specific DNA-binding proteins, whereupon it represses transcription. By directly analyzing the chromatin structure of a repressed promoter in yeast cells, we demonstrate that transcriptional repression is associated with localized histone deacetylation. Specifically, we observe decreased acetylation of histones H3 and H4 (preferentially lysines 5 and 12)
that depends on the DNA-binding repressor (Ume6), Sin3, and Rpd3.
Mapping experiments indicate that the domain of histone deacetylation
is highly localized, occurring over a range of one to two nucleosomes.
Taken together with previous observations, these results define a novel
mechanism of transcriptional repression which involves targeted
recruitment of a histone-modifying activity and localized perturbation
of chromatin structure.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Targeted Recruitment of the Sin3-Rpd3 Histone
Deacetylase Complex Generates a Highly Localized Domain of
Repressed Chromatin In Vivo
and
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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.
Present address: Department of Microbiology and Immunology,
University of California, San Francisco, CA 94143.
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