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J. Biol. Chem., Vol. 282, Issue 19, 13994-14005, May 11, 2007

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The Chromatin Remodeling Factor Mi-2 Acts as a Novel Co-activator for Human c-Myb^*

Thomas Sæther, Tone Berge, Marit Ledsaak, Vilborg Matre, Anne Hege Alm-Kristiansen, Øyvind Dahle, Florence Aubry, and Odd Stokke Gabrielsen¹

From the Department of Molecular Biosciences, University of Oslo, N-0316 Oslo, Norway and Inserm, U625, GERHM, Universitéde Rennes I, Campus de Beaulieu, F-35042 Rennes, France

The c-Myb protein belongs to a group of early hematopoietic transcription factors that are important for progenitor generation and proliferation. These factors have been hypothesized to participate in establishing chromatin patterns specific for hematopoietic genes. In a two-hybrid screening we identified the chromatin remodeling factor Mi-2 as an interaction partner for human c-Myb. The main interacting domains were mapped to the N-terminal region of Mi-2 and the DNA-binding domain of c-Myb. Surprisingly, functional analysis revealed that Mi-2, previously studied as a subunit in the NuRD co-repressor complex, enhanced c-Myb-dependent reporter activation. Consistently, knock-down of endogenous Mi-2 in c-Myb-expressing K562 cells, led to down-regulation of the c-Myb target genes NMU and ADA. When wild-type and helicase-dead Mi-2 were compared, the Myb-Mi-2 co-activation appeared to be independent of the ATPase/DNA helicase activity of Mi-2. The rationale for the unexpected co-activator function seems to lie in a dual function of Mi-2, by which this factor is able to repress transcription in a helicase-dependent and activate in a helicase-independent fashion, as revealed by Gal4-tethering experiments. Interestingly, desumoylation of c-Myb potentiated the Myb-Mi-2 transactivational co-operation, as did co-transfection with p300.

Received for publication, January 26, 2007 , and in revised form, February 26, 2007.

^* This work was supported by the Norwegian Research Council (to T. B., Ø. D., and O. S. G.), The Norwegian Cancer Society (to T. S., M. L., and O. S. G.), and by Anders Jahre Foundation (to O. S. G.). 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 To whom correspondence should be addressed: Dept. of Molecular Biosciences, University of Oslo, P.O. Box 1041, Blindern, N-0316 Oslo, Norway. Tel.: 47-2285-7346; Fax: 47-2285-4443; E-mail: o.s.gabrielsen{at}imbv.uio.no.

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