Copper transfer studies between the N-terminal copper binding domains one and four of human Wilson protein

Biochimica Et Biophysica Acta
Jennifer BunceD L Huffman

Abstract

Human Wilson protein functions in the secretory pathway to insert copper ultimately into the multicopper oxidase ceruloplasmin and also plays a role in the excretion of excess copper to the bile. This copper-transporting P-type ATPase possesses six N-terminal cytosolic copper-binding domains contained within an approximately 72 amino acid consensus motif and the first four of these domains, denoted WLN1-4, are implicated in copper acquisition from the metallochaperone HAH1, whereas the domains closest to the membrane portion of the enzyme, WLN5-6, are essential for copper transport across the membrane. In order to test our hypothesis that copper transfer occurs between domains in the N-terminus of Wilson protein, we expressed and purified to homogeneity copper-binding domains 1, 3, 4, 5-6, and 6, denoted by WLN1, WLN3, WLN4, WLN5-6, and WLN6, respectively. Since we determined WLN1 and WLN4 to have the highest and lowest isoelectric points (6.77 and 3.85, respectively) and thus are readily separated via ion exchange chromatography, we developed a copper transfer assay between these domains. We anaerobically incubated either Cu(I)-WLN1 with apo-WLN4 or apo-WLN1 with Cu(I)-WLN4, then separated these domains and quantified the amou...Continue Reading

Citations

Feb 3, 2007·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Mee Y Bartee, Svetlana Lutsenko
Oct 24, 2009·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Amanda N BarrySvetlana Lutsenko
Oct 25, 2017·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Candan AriözPernilla Wittung-Stafshede
May 6, 2010·Natural Product Reports·Lucia BanciAntonio Rosato
Jan 19, 2007·The Journal of Biological Chemistry·Liliya A Yatsunyk, Amy C Rosenzweig
Oct 19, 2012·Dalton Transactions : an International Journal of Inorganic Chemistry·Elizabeth J New
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