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Molecular and Cellular Biology, August 1999, p. 5504-5511, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Histone Deacetylase 1 Can Repress Transcription by Binding to Sp1

Angelika Doetzlhofer,1 Hans Rotheneder,1 Gerda Lagger,1 Manfred Koranda,1 Vladislav Kurtev,1 Gerald Brosch,2 Erhard Wintersberger,1 and Christian Seiser1,*

Institute of Molecular Biology, Vienna Biocenter, University of Vienna, Vienna,1 and Institute of Microbiology, University of Innsbruck, Medical School, Innsbruck,2 Austria

Received 6 November 1998/Returned for modification 17 December 1998/Accepted 27 April 1999

The members of the Sp1 transcription factor family can act as both negative and positive regulators of gene expression. Here we show that Sp1 can be a target for histone deacetylase 1 (HDAC1)-mediated transcriptional repression. The histone deacetylase inhibitor trichostatin A activates the chromosomally integrated murine thymidine kinase promoter in an Sp1-dependent manner. Coimmunoprecipitation experiments with Swiss 3T3 fibroblasts and 293 cells demonstrate that Sp1 and HDAC1 can be part of the same complex. The interaction between Sp1 and HDAC1 is direct and requires the carboxy-terminal domain of Sp1. Previously we have shown that the C terminus of Sp1 is necessary for the interaction with the transcription factor E2F1 (J. Karlseder, H. Rotheneder, and E. Wintersberger, Mol. Cell. Biol. 16:1659-1667, 1996). Coexpression of E2F1 interferes with HDAC1 binding to Sp1 and abolishes Sp1-mediated transcriptional repression. Our results indicate that one component of Sp1-dependent gene regulation involves competition between the transcriptional repressor HDAC1 and the transactivating factor E2F1.

* Corresponding author. Mailing address: Institute of Molecular Biology, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria. Phone: 431 4277 61770. Fax: 431 4277 9617. E-mail: cs{at}mol.univie.ac.at.

Molecular and Cellular Biology, August 1999, p. 5504-5511, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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