Properties of recombinant extracellular N-terminal domain of human high-affinity copper transporter 1 (hNdCTR1) and its interactions with Cu(II) and Ag(I) ions.

Iurii A Orlov, Tatiana P Sankova, Alexey N Skvortsov, Sergey A Klotchenko, Elena I Sakhenberg, Aleksandra A Mekhova, Irina V Kiseleva, Ekaterina Yu Ilyechova, Ludmila V Puchkova

Journal: Dalton transactions (Cambridge, England : 2003) 2023;52(11):3403-3419

PMID: 36815348

Full Text on Royal Society of Chemistry View on PubMed

Abstract

High-affinity copper transporter 1 (CTR1) is a key link in the transfer of copper (Cu) from the extracellular environment to the cell. Violation in the control system of its expression, or mutations in this gene, cause a global copper imbalance. However, the mechanism of copper transfer CTR1 remains unclear. It has been shown that transformed bacteria synthesizing the fused GB1-NdCTR become resistant to toxic silver ions. According to UV-Vis spectrophotometry and isothermal titration calorimetry, electrophoretically pure GB1-NdCTR specifically and reversibly binds copper and silver ions, and binding is associated with aggregation. Purified NdCTR1 forms SDS-resistant oligomers. The link between nontrivial properties of NdCTR1 and copper import mechanism from extracellular space, as well as potential chelating properties of NdCTR1, are discussed.

Address: Research centre of advanced functional materials and laser communication systems, ADTS Institute, ITMO, University, 197101 St. Petersburg, Russia. [email protected].; Institute of Biomedical Systems and Biotechnology, Peter the Great St. Petersburg Polytechnic University, 195251 St. Petersburg, Russia.; Laboratory of The Molecular Biology of Stem Cells, Institute of Cytology, RAS, 194064 St. Petersburg, Russia.; Laboratory for the Development of Molecular Diagnostic Systems, Smorodintsev Research Institute of Influenza, 197376 St. Petersburg, Russia.; Laboratory of cell protection mechanisms, Institute of Cytology, RAS, 194064 St. Petersburg, Russia.; Department of Virology, Institute of Experimental Medicine, 197376 St. Petersburg, Russia.; Department of Molecular Genetics, Institute of Experimental Medicine, 197376 St. Petersburg, Russia.

DOI: 10.1039/d2dt04060c

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https://doi.org/10.1039/d2dt04060c

MeSH Terms: Humans, Copper, Copper Transporter 1, Silver