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MBC in Press, published online ahead of print April 3, 2002
Mol. Biol. Cell 10.1091/mbc.01-10-0484

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Submitted on October 9, 2001
Revised on February 19, 2002
Accepted on March 18, 2002

A novel ATPase of the SNF2-like protein family interacts with the androgen receptor and modulates androgen-dependent transcription

Nathalie Rouleau1, Andrii Domans'kyi1, Mati Reeben1, Anu-Maarit Moilanen1, Kristina Havas2, Zhigang Kang1, Tom Owen-Hughes2, Jorma J. Palvimo3, and Olli A. Jänne4*

1 Biomedicum Helsinki, Institute of Biomedicine, University of Helsinki and Helsinki University Central Hospital, Helsinki, Finland
2 Division of Gene Regulation, The Wellcome Trust Biocentre, University of Dundee, Dundee, Scotland
3 Biomedicum Helsinki, Institute of Biomedicine, and Institute of Biotechnology, University of Helsinki and Helsinki University Central Hospital, Helsinki, Finland
4 Biomedicum Helsinki, Institute of Biomedicine, and Department of Clinical Chemistry, University of Helsinki and Helsinki University Central Hospital, Helsinki, Finland

* Corresponding author. E-mail address: olli.janne{at}helsinki.fi.

Nuclear receptor, including the androgen receptor (AR), regulate target cell transcription through interaction with auxiliary proteins to modify chromatin structure. We describe here a novel AR-interacting protein,termed ARIP4, that has structural features typical of the SNF2-like protein family. With regard to the Snf2 domain,the closest homolog of ARIP4 is the ATRX protein. ARIP4 is a nuclear protein and comprises 1466 amino acids. It interacts with AR in vitro and in cultured yeast and mammalian cells. ARIP4 can be labeled with 8-azido-[{gamma}-32P]ATP and exhibits DNA-dependent ATPase activity. Like several ATP-dependent chromatin remodeling proteins, ARIP4 generates superhelical torsion within linear DNA fragments in an ATP-dependent manner. With a stably integrated target promoter, ARIP4 elicits a modest enhancement of AR-dependent transactivation. In transient co-transfection assays, ARIP4 modulates AR function in a promoter-dependent fashion; it enhances receptor activity on minimal promoters, but does not activate more complex promoters. ARIP4 mutants devoid of ATPase activity fail to alter DNA topology and behave as trans-dominant negative regulators of AR function in transient assays.




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