Abstract:
: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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Wintz H,Vulpe Cdoi
10.1042/bst0300732keywords:
subject
Has Abstractpub_date
2002-08-01 00:00:00pages
732-5issue
4eissn
0300-5127issn
1470-8752journal_volume
30pub_type
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