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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

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

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.[1]

References

  1. Metal mediated sterol receptor-DNA complex association and dissociation determined by electrospray ionization mass spectrometry. Veenstra, T.D., Benson, L.M., Craig, T.A., Tomlinson, A.J., Kumar, R., Naylor, S. Nat. Biotechnol. (1998) [Pubmed]
 
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