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J. Biol. Chem., Vol. 283, Issue 18, 11924-11934, May 2, 2008

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BAF60a Interacts with p53 to Recruit the SWI/SNF Complex^*

Jaehak Oh¹, Dong H. Sohn¹, Myunggon Ko¹, Heekyoung Chung, Sung H. Jeon^¶, and Rho H. Seong²

From the Department of Biological Sciences, Institute of Molecular Biology and Genetics, and Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea, the Department of Pathology, College of Medicine, Hanyang University, Seoul 133-791, Korea, and the ^¶Department of Life Science and Institute of Bioscience and Biotechnology, Hallym University, Chuncheon 200-702, Korea

To understand the tumor-suppressing mechanism of the SWI/SNF chromatin remodeling complex, we investigated its molecular relationship with p53. Using the pREP4-luc episomal reporter, we first demonstrated that p53 utilizes the chromatin remodeling activity of the SWI/SNF complex to initiate transcription from the chromatin-structured promoter. Among the components of the SWI/SNF complex, we identified BAF60a as a mediator of the interaction with p53 by the yeast two-hybrid assay. p53 directly interacted only with BAF60a, but not with other components of the SWI/SNF complex, such as BRG1, SRG3, SNF5, or BAF57. We found out that multiple residues at the amino acid 108–150 region of BAF60a were involved in the interaction with the tetramerization domain of p53. The N-terminal fragment of BAF60a containing the p53-interacting region as well as small interfering RNA for baf60a inhibited the SWI/SNF complex-mediated transcriptional activity of p53. The uncoupling of p53 with the SWI/SNF complex resulted in the repression of both p53-dependent apoptosis and cell cycle arrest by the regulation of target genes. These results suggest that the SWI/SNF chromatin remodeling complex is involved in the suppression of tumors by the interaction with p53.

Received for publication, July 2, 2007 , and in revised form, February 26, 2008.

^* This work was supported in part by a grant from the Korea Science and Engineering Foundation through the Research Center for Functional Cellulomics (to R. H. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors were supported by the BK21 Program from Ministry of Education and Human Resources Development.

² To whom correspondence should be addressed: Dept. of Biological Sciences, Institute of Molecular Biology and Genetics (Bldg. 105) and Research Center for Functional Cellulomics, Seoul National University, San 56-1, Shinlim-dong, Kwanak-gu, Seoul, 151-742, Republic of Korea. Tel.: 82-2-880-7567; Fax: 82-2-878-9380; E-mail: rhseong{at}snu.ac.kr.

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