6533b7ddfe1ef96bd127525b
RESEARCH PRODUCT
Higher plants possess two different types of ATX1-like copper chaperones.
Salah E. Abdel-ghanyEavan DorceyJason L. BurkheadVicente SancenónLola PeñarrubiaHelena MiraJoseph R. EckerNuria Andrés-colásMarinus PilonSergi PuigKathryn A. GogolinDennis J. ThieleAntoni Garcia-molinasubject
endocrine systemATPaseTwo-hybrid screeningBiophysicsArabidopsischemistry.chemical_elementBiochemistryArabidopsisMolecular BiologyAdenosine TriphosphatasesbiologyArabidopsis ProteinsCell BiologyHistone-Lysine N-Methyltransferasebiology.organism_classificationPhenotypeCopperYeastProtein Structure TertiaryCytosolBiochemistrychemistryChaperone (protein)biology.proteinCopperGenome PlantMolecular ChaperonesTranscription Factorsdescription
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 atx1Δ and sod1Δ 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2007-03-01 | Biochemical and biophysical research communications |