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Nucleic Acids Research Advance Access first published online on June 5, 2009
This version published online on June 15, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp469
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© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene Regulation, Chromatin and Epigenetics

Activation of alternative Jdp2 promoters and functional protein isoforms in T-cell lymphomas by retroviral insertion mutagenesis

Mads Heilskov Rasmussen1,2, Bruce Wang3, Matthias Wabl4, Anders Lade Nielsen2 and Finn Skou Pedersen1,*

1Department of Molecular Biology and 2Department of Human Genetics, Aarhus University, Århus, DK 8000, Denmark, 3Picobella, L.L.C., 863 Mitten Road, Suite 101, Burlingame, CA 94010 and 4Department of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA

*To whom correspondence should be addressed. Tel: +45 89422614; Fax: +45 86196500; Email: fsp{at}mb.au.dk

Received March 26, 2009. Revised May 14, 2009. Accepted May 17, 2009.

Retroviral insertional mutagenesis has been instrumental for the identification of genes important in cancer development. The molecular mechanisms involved in retroviral-mediated activation of proto-oncogenes influence the distribution of insertions within specific regions during tumorigenesis and hence may point to novel gene structures. From a retroviral tagging screen on tumors of 1767 SL3-3 MLV-infected BALB/c mice, intron 2 of the AP-1 repressor Jdp2 locus was found frequently targeted by proviruses resulting in upregulation of non-canonical RNA subspecies. We identified several promoter regions within 1000 bp upstream of exon 3 that allowed for the production of Jdp2 protein isoforms lacking the histone acetylase inhibitory domain INHAT present in canonical Jdp2. The novel Jdp2 isoforms localized to the nucleus and over-expression in murine fibroblast cells induced cell death similar to canonic Jdp2. When expressed in the context of oncogenic NRAS both full length Jdp2 and the shorter isoforms increased anchorage-independent growth. Our results demonstrate a biological function of Jdp2 lacking the INHAT domain and suggest a post-genomic application for the use of retroviral tagging data in identifying new gene products with a potential role in tumorigenesis.


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