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Nucleic Acids Research 2005 33(15):4857-4864; doi:10.1093/nar/gki776
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Published online 30 August 2005

© The Author 2005. 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}oupjournals.org

Article

dSAP18 and dHDAC1 contribute to the functional regulation of the Drosophila Fab-7 element

Silvia Canudas, Silvia Pérez, Laura Fanti1, Sergio Pimpinelli1, Navjot Singh2, Steven D. Hanes2, Fernando Azorín* and M. Lluïsa Espinás

Departament de Biologia Molecular i Cel.lular, Institut de Biologia Molecular de Barcelona, CSIC Parc Científic de Barcelona, Josep Samitier, 1-5 08028 Barcelona, Spain 1Dipartimento di Genetica e Biologia Molecolare, Università ‘La Sapienza’ 00185 Rome, Italy 2New York State Department of Health, Wadsworth Center, State University of New York Albany, NY 12208, USA

*To whom correspondence should be addressed. Tel: +34 93 4034958; Fax: +34 93 4034979; Email: fambmc{at}ibmb.csic.es

Received May 23, 2005. Revised August 2, 2005. Accepted August 2, 2005.

It was described earlier that the Drosophila GAGA factor [Trithorax-like (Trl)] interacts with dSAP18, which, in mammals, was reported to be a component of the Sin3–HDAC co-repressor complex. GAGA–dSAP18 interaction was proposed to contribute to the functional regulation of the bithorax complex (BX-C). Here, we show that mutant alleles of Trl, dsap18 and drpd3/hdac1 enhance A6-to-A5 transformation indicating a contribution to the regulation of Abd-B expression at A6. In A6, expression of Abd-B is driven by the iab-6 enhancer, which is insulated from iab-7 by the Fab-7 element. Here, we report that GAGA, dSAP18 and dRPD3/HDAC1 co-localize to ectopic Fab-7 sites in polytene chromosomes and that mutant Trl, dsap18 and drpd3/hdac1 alleles affect Fab-7-dependent silencing. Consistent with these findings, chromatin immunoprecipitation analysis shows that, in Drosophila embryos, the endogenous Fab-7 element is hypoacetylated at histones H3 and H4. These results indicate a contribution of GAGA, dSAP18 and dRPD3/HDAC1 to the regulation of Fab-7 function.

Present address: Silvia Canudas, Department of Pathology, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, NY 10016, USA


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