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J. Biol. Chem., Vol. 279, Issue 15, 15645-15651, April 9, 2004

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Characterization of Four Autonomous Repression Domains in the Corepressor Receptor Interacting Protein 140^*

Mark Christian, Jennifer M. A. Tullet, and Malcolm G. Parker

From the Institute of Reproductive and Developmental Biology, Faculty of Medicine, Imperial College London, London W12 ONN, United Kingdom

Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type.

Received for publication, December 19, 2003 , and in revised form, January 20, 2004.

^* This work was supported by the Wellcome Trust (to M. C.) and the Biotechnology and Biological Sciences Research Council (to J. M. A. T.). 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.

Both authors contributed equally to this work.

To whom correspondence should be addressed. Tel: 440-207594-2177; Fax: 440-207594-2184; E-mail: m.parker{at}imperial.ac.uk.

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