Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10767420 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
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, AtATX1, which functionally complements yeast atx1Î and sod1Î associated phenotypes, and localizes to the cytosol of Arabidopsis cells. Interestingly, AtATX1, but not full-length CCH, interacts in 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.
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Authors
Sergi Puig, Helena Mira, Eavan Dorcey, Vicente Sancenón, Nuria Andrés-Colás, Antoni Garcia-Molina, Jason L. Burkhead, Kathryn A. Gogolin, Salah E. Abdel-Ghany, Dennis J. Thiele, Joseph R. Ecker, Marinus Pilon, Lola Peñarrubia,