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Department of Pediatrics, Baylor College of Medicine Houston, Texas 77030
Department of Cell Biology, Baylor College of Medicine Houston, Texas 77030
Address requests for reprints to: Dr. J. Wesley Pike, Ligand Pharmaceuticals, Inc., 9393 Towne Center Drive, Suite 100, San Diego, California 92121.
Abstract
The interaction of the vitamin D receptor with a vitamin D-responsive element (VDRE) derived from the human osteocalcin promoter in vitro has been shown to require a nuclear accessory factor (NAF) derived from monkey kidney cells. In this report we show that this factor is widely distributed in cells and tissues, including those that do not express the vitamin D receptor (VDR). NAF is required for VDR binding to a variety of known VDREs. VDR and NAF independently bind the VDRE weakly, as assessed by elution profiles generated during VDRE affinity chromatography. Together, however, both proteins coelute from this column with a profile that indicates a tighter strength of interaction. Analogous chromatography of the VDR derived from ROS 17/2.8 cells treated with 1,25-dihydroxyvitamin D3 in culture also reveals a dual profile of weak and strong binding, suggesting that in vivo modifications are unlikely to alter receptor DNA binding. NAF is a protein of 55 kDa, as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and cross-linking experiments suggest that the VDR and NAF together form a heterodimer on a single VDRE with a mol wt of 103 kDa. These data demonstrate that NAF is required for VDR binding to specific DNA in vitro and suggest the possibility that NAF may be required for the transactivation capability of the VDR in vivo.
FOOTNOTES
This work was supported by NIH Grant DK-38130 and the Robert Welch Foundation.
* Established Investigator of the American Heart Association.
Received for publication June 28, 1991. Revision received July 26, 1991. Accepted for publication August 7, 1991.
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