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J. Biol. Chem., Vol. 281, Issue 24, 16546-16550, June 16, 2006

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New Insights into BS69 Functions^*

From the INSERM U59O and U412, Centre Léon Berard, Université Claude Bernard Lyon I, 28 rue Laennec, F-69008 Lyon, France

The BS69 protein has been commonly described as a co-repressor associated with various transcription factors. However, this hypothesis relied predominately on overexpression of tagged proteins due to the lack of a reliable BS69 antibody. We present for the first time a complete sequence of BS69 and valuable tools to characterize the endogenous protein. We show that the full-length BS69 protein, as well as minor alternatively spliced isoforms, is ubiquitously expressed, nuclear, and associates with chromatin and mitotic chromosomes. Accordingly, BS69 interacts with a set of chromatin remodeling factors, including ATP-dependent helicases, histone deacetylases, and histone methyltransferases, as well as the E2F6 transcription factor. These data strengthen a role for BS69 in gene repression and link BS69 to chromatin remodeling.

Received for publication, January 19, 2006 , and in revised form, March 14, 2006.

^* This work was supported in part by the INSERM Research Institute through the program Avenir. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ Supported by the Association pour la Recherche contre le Cancer (ARC).

² Supported by the INSERM.

³ Supported by the Hospices Civils de Lyon. To whom correspondence should be addressed. Tel.: 33-478785125; Fax: 33-478782720; E-mail: ANSIEAU{at}lyon.fnclcc.fr.

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