Abstract
Copper chaperones are small cytoplasmic proteins that bind intracellular copper (Cu) and deliver it to Cu-dependent enzymes such as cytochrome oxidase, superoxide dismutase, and amine oxidase. Copper chaperones are similar in sequence and structure to the Cu-binding heavy metal-associated (HMA) domains of Cu-transporting ATPases (Cu-ATPases), and the genes for copper chaperones and Cu-ATPases are often located in the same operon. Phylogenetic analysis shows that Cu chaperones and HMA domains of Cu-ATPases represent ancient and distinct lineages that have evolved largely independently since their initial separation. Copper chaperone–Cu-ATPase operons appear to have evolved independently in different prokaryotic lineages, probably due to a strong selective pressure for coexpression of these genes.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Author information
Authors and Affiliations
Additional information
Received: 14 December 2000 / Accepted: 9 May 2001
Rights and permissions
About this article
Cite this article
Jordan, I., Natale, D., Koonin, E. et al. Independent Evolution of Heavy Metal-Associated Domains in Copper Chaperones and Copper-Transporting ATPases. J Mol Evol 53, 622–633 (2001). https://doi.org/10.1007/s002390010249
Published:
Issue Date:
DOI: https://doi.org/10.1007/s002390010249