Independent evolution of heavy metal-associated domains in copper chaperones and copper-transporting atpases.
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.
Jordan
I K
IK
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Natale
D A
DA
Koonin
E V
EV
Galperin
M Y
MY
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D008628:Mercury / Q000494:pharmacology; D019216:Metals, Heavy / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012641:Selection, Genetic; D017386:Sequence Homology, Amino Acid
D027682:Cation Transport Proteins; D019216:Metals, Heavy; D018832:Molecular Chaperones; D003300:Copper; D000251:Adenosine Triphosphatases; D008628:Mercury