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 N-terminal domain could be responsible for functional diversification of the copper ATPases during the course of evolution.
Highlights
Copper is an essential nutrient for most life forms, in excess it can be harmful
We will provide a brief introduction of bacterial CopperATPases, since this information helps to understand the functioning of these proteins in the organisms, which appeared later in the evolution
[3] it can be speculated that CopA in these bacteria exports copper to the periplasmic space where it binds to the cuproproteins such as multicopper oxidases
Summary
Copper-containing proteins appeared early in evolution, likely in response to increasing need to utilize oxygen and oxygen containing molecules. There are four classes of proteins that regulate copper levels in a cell without using copper for enzymatic reactions In eukaryotic cells, such proteins can be divided into membrane bound importers, ATP-driven copper exporters, the soluble copper-delivery molecules, or copperchaperones, and intracellular copper chelators (metallothioneins). The discovery of microfossils in deep sea volcanic rocks led to the proposal that the first life on Earth appeared ~3.2 billion years ago [4] These vents release metals like iron, zinc and copper from the earth’s substratum, and the hot and acidic water further facilitates this leaching process. We will provide a brief introduction of bacterial CopperATPases, since this information helps to understand the functioning of these proteins in the organisms, which appeared later in the evolution
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