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J. Biol. Chem., Vol. 282, Issue 14, 10614-10624, April 6, 2007

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SRG3 Interacts Directly with the Major Components of the SWI/SNF Chromatin Remodeling Complex and Protects Them from Proteasomal Degradation^*

Dong H. Sohn¹, Kyoo Y. Lee¹, Changjin Lee, Jaehak Oh¹, 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, the Department of Pathology, College of Medicine, Hanyang University, Seoul 133-791, and the ^¶Department of Life Science and Institute of Bioscience and Biotechnology, Hallym University, Chuncheon 200-702, Korea

The mammalian SWI/SNF complex is an evolutionarily conserved ATP-dependent chromatin remodeling complex that consists of nine or more components. SRG3, a murine homologue of yeast SWI3, Drosophila MOIRA, and human BAF155, is a core component of the murine SWI/SNF complex required for the regulation of transcriptional processes associated with development, cellular differentiation, and proliferation. Here we report that SRG3 interacts directly with other components of the mammalian SWI/SNF complex such as SNF5, BRG1, and BAF60a. The SWIRM domain and the SANT domain were required for SRG3-SNF5 and SRG3-BRG1 interactions, respectively. In addition, SRG3 stabilized SNF5, BRG1, and BAF60a by attenuating their proteasomal degradation, suggesting its general role in the stabilization of the SWI/SNF complex. Such a stabilization effect of SRG3 was not only observed in the in vitro cell system, but also in cells isolated from SRG3 transgenic mice or knock-out mice haploinsufficient for the Srg3 gene. Taken together, these results suggest the critical role of SRG3 in the post-transcriptional stabilization of the major components of the SWI/SNF complex.

Received for publication, November 14, 2006 , and in revised form, January 24, 2007.

^* This work was supported in part by a grant from 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 Supported by BK21 Program from Ministry of Education and Human Resources Development.

² To whom correspondence should be addressed: Bldg. 105, Research Center for Functional Cellulomics, Seoul National University, San 56-1, Shinlimdong, 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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