Journal of Molecular Evolution

, Volume 53, Issue 6, pp 622–633

Independent Evolution of Heavy Metal-Associated Domains in Copper Chaperones and Copper-Transporting ATPases

  • I. King  Jordan
  • Darren A.  Natale
  • Eugene V.  Koonin
  • Michael Y.  Galperin
Article

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.

Key words: P-type ATPases — Cation transport — Metalloenzyme — Copper poisoning — Wilson disease — Menkes disease — Mercury-binding protein 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Springer-Verlag New York Inc. 2001

Authors and Affiliations

  • I. King  Jordan
    • 1
  • Darren A.  Natale
    • 1
  • Eugene V.  Koonin
    • 1
  • Michael Y.  Galperin
    • 1
  1. 1.National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USAUS

Personalised recommendations