Abstract
Copper is an essential nutrient for most life forms, however in excess it can be harmful. The ATP-driven copper pumps (Copper-ATPases) play critical role in living organisms by maintaining appropriate copper levels in cells and tissues. These evolutionary conserved polytopic membrane proteins are present in all phyla from simplest life forms (bacteria) to highly evolved eukaryotes (Homo sapiens). The presumed early function in metal detoxification remains the main function of Copper-ATPases in prokaryotic kingdom. In eukaryotes, in addition to removing excess copper from the cell, Copper-ATPases have another equally important function - to supply copper to copper dependent enzymes within the secretory pathway. This review focuses on the origin and diversification of Copper ATPases in eukaryotic organisms. From a single Copper ATPase in protozoans, a divergence into two functionally distinct ATPases is observed with the evolutionary appearance of chordates. Among the key functional domains of Copper-ATPases, the metal-binding Nterminal domain could be responsible for functional diversification of the copper ATPases during the course of evolution.
Keywords: ATPase, ATP7B, Copper, CopA, Evolution, diversification, Eukaryotic Organisms, functional domains, Homo sapiens, metalloproteins
Current Genomics
Title:Evolution of Copper Transporting ATPases in Eukaryotic Organisms
Volume: 13 Issue: 2
Author(s): Arnab Gupta, Svetlana Lutsenko
Affiliation:
Keywords: ATPase, ATP7B, Copper, CopA, Evolution, diversification, Eukaryotic Organisms, functional domains, Homo sapiens, metalloproteins
Abstract:
Copper is an essential nutrient for most life forms, however in excess it can be harmful. The ATP-driven copper pumps (Copper-ATPases) play critical role in living organisms by maintaining appropriate copper levels in cells and tissues. These evolutionary conserved polytopic membrane proteins are present in all phyla from simplest life forms (bacteria) to highly evolved eukaryotes (Homo sapiens). The presumed early function in metal detoxification remains the main function of Copper-ATPases in prokaryotic kingdom. In eukaryotes, in addition to removing excess copper from the cell, Copper-ATPases have another equally important function - to supply copper to copper dependent enzymes within the secretory pathway. This review focuses on the origin and diversification of Copper ATPases in eukaryotic organisms. From a single Copper ATPase in protozoans, a divergence into two functionally distinct ATPases is observed with the evolutionary appearance of chordates. Among the key functional domains of Copper-ATPases, the metal-binding Nterminal domain could be responsible for functional diversification of the copper ATPases during the course of evolution.
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Cite this article as:
Arnab Gupta, Svetlana Lutsenko , Evolution of Copper Transporting ATPases in Eukaryotic Organisms, Current Genomics 2012; 13 (2) . https://dx.doi.org/10.2174/138920212799860661
DOI https://dx.doi.org/10.2174/138920212799860661 |
Print ISSN 1389-2029 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5488 |
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