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J. Biol. Chem., Vol. 282, Issue 50, 36386-36393, December 14, 2007

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Daxx-like Protein of Drosophila Interacts with Dmp53 and Affects Longevity and Ark mRNA Level^*

László Bodai, Norbert Pardi, Zsuzsanna Újfaludi, Orsolya Bereczki, Orbán Komonyi, Eva Balint¹, and Imre M. Boros²

From the Chromatin Research Group of USZ-HAS, Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, H-6726 Hungary and the Biological Research Center, Institute of Biochemistry, Szeged, H-6726 Hungary

Daxx-like protein (DLP), the Drosophila homolog of Daxx, binds Drosophila melanogaster p53 (Dmp53) through its C-terminal region. We generated DLP mutants and found that although DLP expression is developmentally regulated, it is not essential for the execution of the developmental program. The effects DLP mutations show in the loss of heterozygosity assay and on phenotypes resulting from Dmp53 overexpression indicate a genetic interaction between DLP and Dmp53. In contrast to Dmp53 mutants, however, loss of DLP does not result in radiosensitivity indicating that it does not play an essential role in the activation of Dmp53-dependent response after ionizing radiation, and DLP is also not required for the irradiation-induced activation of reaper. In contrast, DLP is involved in the transcriptional regulation of Ark, because Ark mRNA level is decreased in DLP mutants and increased upon ectopic overexpression of DLP. Interestingly, DLP mutants have reduced longevity and reduced female fertility. Altogether, our data suggest complex functions for DLP, which include an anti-apoptotic effect exerted through repression of some Dmp53 functions, and activation of some proapoptotic genes.

Received for publication, July 6, 2007 , and in revised form, October 12, 2007.

^* This work was supported by grants from the Netherlands Organization for Scientific Research and Hungarian Scientific Research Fund (NWO 048.011.048/OTKA NW42813, OTKA T046414), grants from the Hungarian Ministry of Health (ETT465/2003, ETT078/2003), and by EU FP-6 (LSHG-CT-2004-502950). 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 Figs. S1–S3.

¹ Recipient of the Z. Magyary fellowship from the Foundation for Hungarian Higher Education and Research and the G. Bekesy fellowship provided by the Hungarian Ministry of Education. Present address: BayGen Inst., Bay Zoltan Foundation for Applied Research, Szeged, Hungary.

² To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary. Tel.: 36-62-544686; Fax: 36-62-544887; E-mail: borosi{at}bio.u-szeged.hu.

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