Higher plants possess two different types of ATX1-like copper chaperones |
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Authors: | Puig Sergi Mira Helena Dorcey Eavan Sancenón Vicente Andrés-Colás Nuria Garcia-Molina Antoni Burkhead Jason L Gogolin Kathryn A Abdel-Ghany Salah E Thiele Dennis J Ecker Joseph R Pilon Marinus Peñarrubia Lola |
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Institution: | Departament de Bioquímica i Biologia Molecular, Universitat de València, Av. Dr. Moliner, 50, E-46100 Burjassot, Valencia, Spain. |
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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 atx1Delta and sod1Delta 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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Keywords: | Copper homeostasis Heavy metal P-type ATPase Copper chaperone Yeast two-hybrid |
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