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Originally published In Press as doi:10.1074/jbc.M111795200 on February 26, 2002

J. Biol. Chem., Vol. 277, Issue 20, 17836-17844, May 17, 2002
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FOR, a Novel Orphan Nuclear Receptor Related to Farnesoid X Receptor*

Young-Woo Seoabc, Sabyasachi Sanyalacd, Han-Jong Kima, Dong Hwan Wone, Jee-Young Anf, Tosikazu Amanog, Ann Marie Zavackih, Hyuk-Bang Kwona, Yun-Bo Shig, Won-Sun Kimf, Heonjoong Kange, David D. Moorei, and Hueng-Sik Choiaj

From the a Hormone Research Center, d Department of Biology, Chonnam National University, Kwangju 500-757, Republic of Korea, the e Marine Biotechnology Laboratory, School of Earth and Environmental Science, Seoul National University, Republic of Korea, the f Department of Life Science, Sogang University, Seoul 121-742, Republic of Korea, the g Laboratory of Molecular Embryology, NICHD, National Institutes of Health, Bethesda, Maryland 20892-5431, the h Thyroid Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, and the i Department of Cellular and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030

We have identified and characterized a new amphibian orphan member of the nuclear receptor superfamily and termed it FOR1 (farnesoid X receptor (FXR)-like Orphan Receptor) because it shares the highest amino acid identity with the mammalian FXR. We also identified a variant of FOR1, called FOR2, which has 15 additional C-terminal amino acids. Both variants include an unusual insertion of 33 amino acids in the helix 7 region of the canonical ligand binding domain sequence, suggesting a unique structure for FOR. Northern blot analysis demonstrates that the FOR gene is highly expressed in adult and tadpole liver, kidney, and tail bud stage of the embryo. Detailed expression analysis using in situ hybridization indicates that FOR expression is first detectable at stage 30/31 in the presumptive liver region lasting until stage 41 with a peak level evident at stage 35/36. FOR forms heterodimeric complexes with retinoid X receptor (RXR) as demonstrated by biochemical and mammalian two-hybrid approaches. Gel mobility shift assays demonstrate that FORs form specific DNA-protein complexes on an FXR binding element consisting of an inverted repeat DNA element with 1 nucleotide spacing (IR1) from the phospholipid transfer protein gene promoter. Finally, although FORs do not exhibit constitutive transcriptional activity, frog gallbladder extract significantly augments the transcriptional activities of FORs.

* This work was supported by KOSEF through the Hormone Research Center (HRC1999L0001) and in part by KOSEF Grant 96-0401-08-01-3 (to H. S. C.), by Grant 00-J-LF-01-B-78 from Critical Technology 21 on Life Phenomena and Function Research of the ministry of Science & Technology (to H. K.), and by Grant KRF-1999-015-DI0093 from the Korea Research Foundation (to W. S. K.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF456451, AF456452, and AF456453.

c Both authors contributed equally to this work.

b Present address: Korea Basic Science Institute, Kwangju Branch, Kwangju 500-757, Republic of Korea.

j To whom correspondence should be addressed. Tel.: 82-62-530-0503; Fax: 82-62-530-0500; E-mail: hsc@chonnam.chonnam.ac.kr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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