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Originally published In Press as doi:10.1074/jbc.C100381200 on September 25, 2001

J. Biol. Chem., Vol. 276, Issue 45, 42057-42062, November 9, 2001
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p53 Targets Chromatin Structure Alteration to Repress alpha -Fetoprotein Gene Expression*

Stacey K. OgdenDagger §, Kathleen C. Lee§, Kara Wernke-DollriesDagger , Sabrina A. Stratton||, Bruce Aronow**, and Michelle Craig BartonDagger ||Dagger Dagger

From the Dagger  Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati and ** Children's Hospital Research Foundation, Cincinnati, Ohio 45267 and the || Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030

Many of the functions ascribed to p53 tumor suppressor protein are mediated through transcription regulation. We have shown that p53 represses hepatic-specific alpha -fetoprotein (AFP) gene expression by direct interaction with a composite HNF-3/p53 DNA binding element. Using solid-phase, chromatin-assembled AFP DNA templates and analysis of chromatin structure and transcription in vitro, we find that p53 binds DNA and alters chromatin structure at the AFP core promoter to regulate transcription. Chromatin assembled in the presence of hepatoma extracts is activated for AFP transcription with an open, accessible core promoter structure. Distal (-850) binding of p53 during chromatin assembly, but not post-assembly, reverses transcription activation concomitant with promoter inaccessibility to restriction enzyme digestion. Inhibition of histone deacetylase activity by trichostatin-A (TSA) addition, prior to and during chromatin assembly, activated chromatin transcription in parallel with increased core promoter accessibility. Chromatin immunoprecipitation analyses showed increased H3 and H4 acetylated histones at the core promoter in the presence of TSA, while histone acetylation remained unchanged at the site of distal p53 binding. Our data reveal that p53 targets chromatin structure alteration at the core promoter, independently of effects on histone acetylation, to establish repressed AFP gene expression.

* This work was supported in part by National Institutes of Health Grant (NIH) GM53683 (to M. C. B.), by NIH predoctoral training Grant T32 CA59268, and by a Ryan Foundation Fellowship (provided support for S. K. O.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Equally contributing authors.

Current address: Dept. of Molecular Biology and Genetics, Cornell University, 467 Biotechnology Bldg., Ithaca, NY 14853.

Dagger Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Blvd., Box 117, Houston, TX 77030. E-mail: mbarton@odin.mdacc.tmc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.