Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 354, Issue 2, Pages 385-390Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2006.12.215
Keywords
copper homeostasis; heavy metal P-type ATPase; copper chaperone; yeast two-hybrid
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Funding
- NIGMS NIH HHS [GM41840] Funding Source: Medline
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Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATXI, which functionally complements yeast atx1 Delta and sod1 Delta associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATXI, but not full-length CCH, interacts it? vivo with the Arabidopsis RAN1 Cu-transporting P-type ATPase by yeast two-hybrid. We propose that higher plants express two types of ATX1-like Cu chaperones: the ATX1-type with a predominant function in Cu delivery to P-type ATPases, and the CCH-type with additional CTD-mediated plant-specific functions. (c) 2007 Elsevier Inc. All rights reserved.
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