Metal mediated sterol receptor-DNA complex association and dissociation determined by electrospray ionization mass spectrometry

Timothy D. Veenstra, Linda M. Benson, Theodore A. Craig, Andy J. Tomlinson, Rajiv Kumar, Stephen Naylor

Research output: Contribution to journalArticle

51 Scopus citations


The vitamin D receptor (VDR) binds to specific DNA sequences termed vitamin D response elements (VDREs) thereby enhancing or repressing transcription. We have used electrospray ionization mass spectrometry to examine the interaction between the DNA-binding domain of the vitamin D receptor (VDR) DBD) with a double-stranded DNA (dsDNA) sequence containing the VDRE from the mouse osteopontin gene. The VDR DBD was shown to bind to the appropriate DNA sequence only when bound to 2 moles of zinc (Zn2+) or cadmium (Cd2+) per mole of protein. Additional binding of Zn2+ or Cd2+ by the protein caused the protein to dissociate from the dsDNA. These results show that the VDR DBD/DNA metal-dependent association occurs when the receptor is occupied by 2 moles of Zn2+ per mole of protein and that further binding of Zn2+ to the protein causes dissociation of the complex.

Original languageEnglish (US)
Pages (from-to)262-266
Number of pages5
JournalNature biotechnology
Issue number3
StatePublished - Mar 28 1998



  • Protein/DNA interactions
  • Vitamin D receptor

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Molecular Medicine
  • Biomedical Engineering

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