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Originally published In Press as doi:10.1074/jbc.M009891200 on April 23, 2001

J. Biol. Chem., Vol. 276, Issue 26, 23653-23660, June 29, 2001
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The RING Finger Protein SNURF Is a Bifunctional Protein Possessing DNA Binding Activity*

Marika HäkliDagger , Ulla KarvonenDagger , Olli A. JänneDagger §, and Jorma J. PalvimoDagger ||

From the Dagger  Biomedicum Helsinki, Institute of Biomedicine (Physiology),  Institute of Biotechnology, and the § Department of Clinical Chemistry, University of Helsinki, FIN-00014 Helsinki, Finland

The small nuclear C3HC4 finger protein (SNURF), RNF4, acts as transcriptional coactivator for both steroid-dependent and -independent promoters such as those driven by androgen response elements and GC boxes, respectively. However, SNURF does not possess intrinsic transcription activation function, and the precise molecular mechanism of its action is unknown. We have studied herein the interaction of SNURF with DNA in vitro. SNURF binds to linear double-stranded DNA with no apparent sequence specificity in a cooperative fashion that is highly dependent on the length of the DNA fragment used. SNURF interacts efficiently with both supercoiled circular and four-way junction DNA, and importantly, it also recognizes nucleosomes. An intact RING structure of SNURF is not mandatory for DNA binding, whereas mutations of specific positively charged residues in the N terminus (amino acids 8-11) abolish DNA binding. Interestingly, the ability of SNURF to interact with DNA is associated with its capability to enhance transcription from promoters containing GC box elements. Because SNURF can interact with both DNA and protein (transcription) factors, it may promote assembly of nucleoprotein structures.

* This work was supported by grants from the Medical Research Council (Academy of Finland), the Finnish Foundation for Cancer Research, the Sigrid Jusélius Foundation, Biocentrum Helsinki, the Helsinki University Central Hospital, and the Association for the Cure of Cancer of Prostate (CaP Cure).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Biomedicum Helsinki, Inst. of Biomedicine (Physiology), Univ. of Helsinki, P. O. Box 63, FIN-00014 Helsinki, Finland. Tel.: 358-9-19125291; Fax: 358-9-19125302; E-mail: jorma.palvimo@helsinki.fi.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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