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Molecular and Cellular Biology, September 1998, p. 5128-5139, Vol. 18, No. 9
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of a Novel RING Finger Protein as a Coregulator in Steroid Receptor-Mediated Gene Transcription

Anu-Maarit Moilanen,1 Hetti Poukka,1 Ulla Karvonen,1 Marika Häkli,1 Olli A. Jänne,1,2 and Jorma J. Palvimo1,*

Department of Physiology, Institute of Biomedicine,1 and Department of Clinical Chemistry,2 University of Helsinki, FIN-00014 Helsinki, Finland

Received 19 December 1997/Returned for modification 19 February 1998/Accepted 2 June 1998

Using the DNA-binding domain of androgen receptor (AR) as a bait in a yeast two-hybrid screening, we have identified a small nuclear RING finger protein, termed SNURF, that interacts with AR in a hormone-dependent fashion in both yeast and mammalian cells. Physical interaction between AR and SNURF was demonstrated by coimmunoprecipitation from cell extracts and by protein-protein affinity chromatography. Rat SNURF is a highly hydrophilic protein consisting of 194 amino acid residues and comprising a consensus C3HC4 zinc finger (RING) structure in the C-terminal region and a bipartite nuclear localization signal near the N terminus. Immunohistochemical experiments indicated that SNURF is a nuclear protein. SNURF mRNA is expressed in a variety of human and rat tissues. Overexpression of SNURF in cultured mammalian cells enhanced not only androgen, glucocorticoid, and progesterone receptor-dependent transactivation but also basal transcription from steroid-regulated promoters. Mutation of two of the potential Zn2+ coordinating cysteines to serines in the RING finger completely abolished the ability of SNURF to enhance basal transcription, whereas its ability to activate steroid receptor-dependent transcription was maintained, suggesting that there are separate domains in SNURF that mediate interactions with different regulatory factors. SNURF is capable of interacting in vitro with the TATA-binding protein, and the RING finger domain is needed for this interaction. Collectively, we have identified and characterized a ubiquitously expressed RING finger protein, SNURF, that may function as a bridging factor and regulate steroid receptor-dependent transcription by a mechanism different from those of previously identified coactivator or integrator proteins.

* Corresponding author. Mailing address: Department of Physiology, Institute of Biomedicine, University of Helsinki, P.O. Box 9 (Siltavuorenpenger 20J), FIN-00014 Helsinki, Finland. Phone: 358-9-1918542. Fax: 358-9-1918681. E-mail: jorma.palvimo{at}helsinki.fi.

Molecular and Cellular Biology, September 1998, p. 5128-5139, Vol. 18, No. 9
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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