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

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.

Copper cofactor delivery in plant cells.

Copper (Cu) is a micronutrient that has roles in photosynthesis, respiration, antioxidant activity, cell wall metabolism and hormone perception. Excess Cu is toxic and therefore its delivery has to be tightly regulated. Recent progress in the study of Cu homeostasis has revealed not only components of the Cu delivery machinery but also regulatory systems that control Cu-protein expression and coordinate the activity of Cu-delivery systems.

AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7.

In plant chloroplasts two superoxide dismutase (SOD) activities occur, FeSOD and Cu/ZnSOD, with reciprocal regulation in response to copper availability. This system presents a unique model to study the regulation of metal-cofactor delivery to an organelle. The Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD.