Jordan I K, Natale D A, Koonin E V, Galperin M Y
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
J Mol Evol. 2001 Dec;53(6):622-33. doi: 10.1007/s002390010249.
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.
铜伴侣蛋白是一类小的细胞质蛋白，它们结合细胞内的铜（Cu）并将其传递给依赖铜的酶，如细胞色素氧化酶、超氧化物歧化酶和胺氧化酶。铜伴侣蛋白在序列和结构上与铜转运ATP酶（Cu-ATP酶）的铜结合重金属相关（HMA）结构域相似，并且铜伴侣蛋白和Cu-ATP酶的基因通常位于同一个操纵子中。系统发育分析表明，铜伴侣蛋白和Cu-ATP酶的HMA结构域代表了古老且不同的谱系，自它们最初分离以来在很大程度上是独立进化的。铜伴侣蛋白-Cu-ATP酶操纵子似乎在不同的原核生物谱系中独立进化，这可能是由于这些基因共表达的强大选择压力所致。
