人高亲和力铜转运蛋白1（hNdCTR1）重组细胞外N端结构域的特性及其与Cu(II)和Ag(I)离子的相互作用。

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.

作者信息

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

机构信息

Research centre of advanced functional materials and laser communication systems, ADTS Institute, ITMO, University, 197101 St. Petersburg, Russia.

Institute of Biomedical Systems and Biotechnology, Peter the Great St. Petersburg Polytechnic University, 195251 St. Petersburg, Russia.

出版信息

Dalton Trans. 2023 Mar 14;52(11):3403-3419. doi: 10.1039/d2dt04060c.

DOI:10.1039/d2dt04060c

PMID:36815348

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.

摘要

高亲和力铜转运蛋白1（CTR1）是铜（Cu）从细胞外环境转运至细胞过程中的关键环节。其表达控制系统出现异常或该基因发生突变，会导致整体铜失衡。然而，CTR1介导的铜转运机制仍不清楚。研究表明，合成融合蛋白GB1-NdCTR的转化菌对有毒银离子具有抗性。根据紫外可见分光光度法和等温滴定量热法，电泳纯的GB1-NdCTR能特异性且可逆地结合铜离子和银离子，并且这种结合与聚集有关。纯化后的NdCTR1形成抗SDS的寡聚体。本文讨论了NdCTR1的特殊性质与细胞外空间铜导入机制之间的联系，以及NdCTR1潜在的螯合特性。