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Molecular and Cellular Biology, October 2001, p. 7065-7077, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.7065-7077.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The p65 (RelA) Subunit of NF-kappa B Interacts with the Histone Deacetylase (HDAC) Corepressors HDAC1 and HDAC2 To Negatively Regulate Gene Expression

Brian P. Ashburner,1,dagger Sandy D. Westerheide,1 and Albert S. Baldwin Jr.1,2,3,*

Lineberger Comprehensive Cancer Center,1 Curriculum in Genetics and Molecular Biology,2 and Department of Biology,3 University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599

Received 29 June 2001/Accepted 11 July 2001

Regulation of NF-kappa B transactivation function is controlled at several levels, including interactions with coactivator proteins. Here we show that the transactivation function of NF-kappa B is also regulated through interaction of the p65 (RelA) subunit with histone deacetylase (HDAC) corepressor proteins. Our results show that inhibition of HDAC activity with trichostatin A (TSA) results in an increase in both basal and induced expression of an integrated NF-kappa B-dependent reporter gene. Chromatin immunoprecipitation (ChIP) assays show that TSA treatment causes hyperacetylation of the wild-type integrated NF-kappa B-dependent reporter but not of a mutant version in which the NF-kappa B binding sites were mutated. Expression of HDAC1 and HDAC2 repressed tumor necrosis factor (TNF)-induced NF-kappa B-dependent gene expression. Consistent with this, we show that HDAC1 and HDAC2 target NF-kappa B through a direct association of HDAC1 with the Rel homology domain of p65. HDAC2 does not interact with NF-kappa B directly but can regulate NF-kappa B activity through its association with HDAC1. Finally, we show that inhibition of HDAC activity with TSA causes an increase in both basal and TNF-induced expression of the NF-kappa B-regulated interleukin-8 (IL-8) gene. Similar to the wild-type integrated NF-kappa B-dependent reporter, ChIP assays showed that TSA treatment resulted in hyperacetylation of the IL-8 promoter. These data indicate that the transactivation function of NF-kappa B is regulated in part through its association with HDAC corepressor proteins. Moreover, it suggests that the association of NF-kappa B with the HDAC1 and HDAC2 corepressor proteins functions to repress expression of NF-kappa B-regulated genes as well as to control the induced level of expression of these genes.

* Corresponding author. Mailing address: Lineberger Comprehensive Cancer Center, CB# 7295, University of North Carolina, Chapel Hill, NC 27599. Phone: (919) 966-3652. Fax: (919) 966-0444. E-mail: jhall{at}med.unc.edu.

dagger Present address: Department of Biological Sciences, Univ. of Toledo, Toledo, Ohio 43606.

Molecular and Cellular Biology, October 2001, p. 7065-7077, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.7065-7077.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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