Independent Evolution of Heavy Metal-Associated Domains in Copper Chaperones and Copper-Transporting ATPases |
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Authors: | I. King Jordan Darren A. Natale Eugene V. Koonin Michael Y. Galperin |
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Affiliation: | (1) National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA, US |
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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. Received: 14 December 2000 / Accepted: 9 May 2001 |
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Keywords: | : P-type ATPases — Cation transport — Metalloenzyme — Copper poisoning — Wilson disease — Menkes disease — Mercury-binding protein |
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