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


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Puig, S; Mira, H; Dorcey, E; Sancenón, V; Andrés-Colás, N; Garcia-Molina, A; Burkhead, JL; Gogolin, KA; Abdel-Ghany, SE; Thiele, DJ; Ecker, JR; Pilon, M; Peñarrubia, L

Published Date

  • March 9, 2007

Published In

Volume / Issue

  • 354 / 2

Start / End Page

  • 385 - 390

PubMed ID

  • 17223078

Pubmed Central ID

  • 17223078

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2006.12.215


  • eng

Conference Location

  • United States