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Nucleic Acids Research 2006 34(1):364-372; doi:10.1093/nar/gkj400
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Published online 12 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

TACC3 mediates the association of MBD2 with histone acetyltransferases and relieves transcriptional repression of methylated promoters

Tiziana Angrisano1, Francesca Lembo2, Raffaela Pero1, Francesco Natale1, Alfredo Fusco1,4, Vittorio E. Avvedimento1,4, Carmelo B. Bruni1 and Lorenzo Chiariotti1,3,4,*

1Dipartimento di Biologia e Patologia Cellulare e Molecolare ‘L. Califano’, Università degli Studi di Napoli ‘Federico II’ 80131 Naples, Italy 2Dipartimento di Chimica Farmaceutica e Tossicologica, Università degli Studi di Napoli ‘Federico II’ 80131 Naples, Italy 3Dipartimento di Scienze per la Salute, Università degli Studi del Molise 86100 Campobasso, Italy 4NOGEC, Naples Oncogenomic Center, CEINGE Biotecnologie Avanzate Naples, Italy

*To whom correspondence should be addressed. Tel: +39 081 7462056; Fax: +39 081 7703285; Email: chiariot{at}unina.it

Received October 29, 2005. Revised November 18, 2005. Accepted December 1, 2005.

We have recently reported that a novel MBD2 interactor (MBDin) has the capacity to reactivate transcription from MBD2-repressed methylated promoters even in the absence of demethylation events. Here we show that another unrelated protein, TACC3, displays a similar activity on methylated genes. In addition the data reported here provide possible molecular mechanisms for the observed phenomenon. Immunoprecipitation experiments showed that MBD2/TACC3 form a complex in vivo with the histone acetyltransferase pCAF. MBD2 could also associate with HDAC2, a component of MeCP1 repression complex. However, we found that the complexes formed by MBD2 with TACC3/pCAF and with HDAC2 were mutually exclusive. Moreover, HAT enzymatic assays demonstrated that HAT activity associates with MBD2 in vivo and that such association significantly increased when TACC3 was over-expressed. Overall our findings suggest that TACC3 can be recruited by MBD2 on methylated promoters and is able to reactivate transcription possibly by favoring the formation of an HAT-containing MBD2 complex and, thus, switching the repression potential of MBD2 in activation even prior to eventual demethylation.


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