A nuclear protein essential for binding of rat 1,25-dihydroxyvitamin D3 receptor to its response elements.

T K Ross; V E Moss; J M Prahl; H F DeLuca

doi:10.1073/pnas.89.1.256

Proc Natl Acad Sci U S A. 1992 Jan 1; 89(1): 256–260.

doi: 10.1073/pnas.89.1.256

PMCID: PMC48215

PMID: 1309609

A nuclear protein essential for binding of rat 1,25-dihydroxyvitamin D3 receptor to its response elements.

T K Ross, V E Moss, J M Prahl, and H F DeLuca

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Abstract

Recombinant 1,25-dihydroxyvitamin D3 receptor from a baculovirus expression system requires a mammalian-derived nuclear accessory protein for binding to a vitamin D response element (DRE). This was established by electrophoretic mobility shift analyses using radiolabeled DNA probes consisting of DREs from two vitamin D-responsive genes. Mammalian nuclear extract was also required for the binding of wild-type porcine vitamin D receptor to a DRE. Surprisingly, the accessory factor-dependent formation of receptor-DRE complex was independent of exogenous 1,25-dihydroxyvitamin D3. A 59- to 64-kDa accessory protein from porcine intestinal nuclear extract was identified by size-exclusion chromatography. Nuclear extracts from rat liver and kidney contained accessory factor, whereas smaller amounts were detected in heart muscle. Spleen and skeletal muscle contained no detectable accessory factor.

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Selected References

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