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Biochem Biophys Res Commun. 2007 Mar 9;354(2):385-90. Epub 2007 Jan 9.

Higher plants possess two different types of ATX1-like copper chaperones.

Author information

1
Departament de Bioquímica i Biologia Molecular, Universitat de València, Av. Dr. Moliner, 50, E-46100 Burjassot, Valencia, Spain.

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.

PMID:
17223078
DOI:
10.1016/j.bbrc.2006.12.215
[Indexed for MEDLINE]

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