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Molecular and Cellular Biology, November 2002, p. 7820-7830, Vol. 22, No. 22
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.22.7820-7830.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Activation of the Mouse Histone Deacetylase 1 Gene by Cooperative Histone Phosphorylation and Acetylation

Christoph Hauser, Bernd Schuettengruber, Stefan Bartl,{dagger} Gerda Lagger, and Christian Seiser*

Institute of Medical Biochemistry, Department of Molecular Biology, University of Vienna, Vienna Biocenter, A-1030 Vienna, Austria

Received 28 June 2002/ Accepted 13 August 2002

Histone deacetylase 1 (HDAC1) is a major regulator of chromatin structure and gene expression. Tight control of HDAC1 expression is essential for normal cell cycle progression of mammalian cells. HDAC1 mRNA levels are regulated by growth factors and by changes in intracellular deacetylase activity levels. Stimulation of the mitogen-activated protein kinase cascade by anisomycin or growth factors, together with inhibition of deacetylases by trichostatin A (TSA), leads to stable histone H3 phosphoacetylation and strongly induced HDAC1 expression. In contrast, activation of the nucleosomal response by anisomycin alone results only in transient phosphoacetylation of histone H3 without affecting HDAC1 mRNA levels. The transcriptional induction of the HDAC1 gene by anisomycin and TSA is efficiently blocked by H89, an inhibitor of the nucleosomal response. Detailed studies of the kinetics of histone acetylation and phosphorylation show that the two modifications are synergistic and essential for induced HDAC1 transcription. Activation of the HDAC1 gene by anisomycin together with TSA or by growth factors is accompanied by phosphoacetylation of HDAC1 promoter-associated histone H3. Our results present evidence for a precise regulatory mechanism which allows induction of the HDAC1 gene in response to proliferation signals and modulation of HDAC1 expression dependent on intracellular deacetylase levels.

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

{dagger} Present address: AXON Neuroscience, A-1030 Vienna, Austria.

Molecular and Cellular Biology, November 2002, p. 7820-7830, Vol. 22, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.22.7820-7830.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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