Wintz H, Vulpe C
Department of Nutrition and Toxicology, University of California, Berkeley, CA 95720, USA.
Biochem Soc Trans. 2002 Aug;30(4):732-5. doi: 10.1042/bst0300732.
Copper chaperones, soluble copper-binding proteins, are essential for ensuring proper distribution of copper to cellular compartments and to proteins requiring copper prosthetic groups. They are found in all eukaryotic organisms. Orthologues of the three copper chaperones characterized in yeast, ATX1, CCS and COX17, are present in Arabidopsis thaliana. Plants are faced with unique challenges to maintain metal homoeostasis, and thus their copper chaperones have evolved by diversifying and gaining additional functions. In this paper we present our current knowledge of copper chaperones in A. thaliana based on the information available from the complete sequence of its genome.
铜伴侣蛋白,即可溶性铜结合蛋白,对于确保铜在细胞区室以及需要铜辅基的蛋白质之间的正确分布至关重要。它们存在于所有真核生物中。酵母中已鉴定出的三种铜伴侣蛋白ATX1、CCS和COX17的直系同源物存在于拟南芥中。植物在维持金属稳态方面面临独特挑战,因此其铜伴侣蛋白通过多样化和获得额外功能而进化。在本文中,我们基于拟南芥基因组完整序列所提供的信息,阐述了我们目前对其铜伴侣蛋白的了解。