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Volume 271, Number 36, Issue of September 6, 1996 pp. 21859-21869
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Purification and Properties of Rat Liver Nuclear Proteins That Interact with the Hepatitis B Virus Enhancer 1

(Received for publication, May 21, 1996, and in revised form, June 19, 1996)

From the Department of Microbiology and the Program in Molecular Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262

The hepatitis B virus enhancer 1 element plays a fundamental role in the liver-specific regulation of hepatitis B virus gene expression. A central region of enhancer 1, the enhancer core domain, contains at least four cis-acting sequence motifs that are essential for enhancer 1 activity. In this study, we have investigated an essential motif within the core domain previously defined as footprint V (FPV). Transient transfection analyses demonstrate that FPV is capable of independently functioning in a liver-specific manner to activate transcription. Therefore, to further examine the liver-specific properties of FPV-mediated enhancer 1 activity, we have carried out the biochemical purification and characterization of FPV binding activity from rat liver nuclei. This study has conclusively identified hepatocyte nuclear factor 3 (HNF-3), a liver-enriched member of the HNF-3/forkhead gene family, as the predominant purified protein that interacts with the FPV motif. Moreover, a cellular protein(s) that copurified with HNF-3 specifically interacts with a novel sequence motif that partially overlaps FPV. Since this novel motif contains a palindromic sequence, we have tentatively referred to the protein(s) that binds to this site as palindrome-binding factor (PBF). Additional evidence indicates that HNF-3 and PBF cooperatively interact with enhancer 1. Therefore, this study supports the hypothesis that FPV-mediated enhancer activity involves a cooperative interplay between HNF-3 and at least one other enhancer 1-binding protein, PBF.

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