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PMID: 12196180 Published · ppublish English Journal Article

Plant copper chaperones.

Biochemical Society transactions ·Vol. 30 ·No. 4 ·2002-08-00 ·Pages 732-5

Wintz H, Vulpe C

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.

MeSH Terms
Amino Acid Sequence Animals Arabidopsis/metabolism Arabidopsis Proteins/metabolism Biological Transport Carrier Proteins/metabolism Cation Transport Proteins/metabolism Chlamydomonas reinhardtii/metabolism Copper/metabolism Copper Transport Proteins Databases, Protein Humans Molecular Chaperones/metabolism Molecular Sequence Data Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Arabidopsis Proteins AtCOX17 protein, Arabidopsis CCS protein, human CCS1 protein, S cerevisiae Carrier Proteins Cation Transport Proteins Copper Transport Proteins Molecular Chaperones Saccharomyces cerevisiae Proteins Copper
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wintz H
Department of Nutrition and Toxicology, University of California, Berkeley, CA 95720, USA. wintz@uclink.berkeley.edu
Vulpe C
Article Info
Journal
Biochemical Society transactions
Abbr.
Biochem Soc Trans
ISSN
0300-5127
Published
2002-08-00
Pages
732-5
Language
English
Region
England
NLM ID
7506897
Subset
IM
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