Hiromura M, Sakurai H
Department of Analytical and Bioinorganic Chemistry, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi, Yamashina-ku, Kyoto, 607-8414, Japan.
Biochem Biophys Res Commun. 1999 Nov 19;265(2):509-12. doi: 10.1006/bbrc.1999.1678.
An ATX1 homologue of 503 bp length was cloned from a rat cDNA library, and the deduced protein from the cDNA was found to contain 68 amino acids with a predicted molecular mass of 7.2 kDa. The rat ATX1 homologue protein (Rah1p), which shows 35%, 38%, and 89% identities with Atx1p, CUC-1, and HAH1, respectively, conserves both the MTCXXC copper-binding site in the N terminus and the KTGK lysine-rich region in the C terminus. In Northern blot analysis, rah1 mRNA was found to be expressed at high levels in the liver, small intestine, and testis. Expression of rah1 cDNA complemented a null atx1 mutant strain in yeast. Thus, Rah1p was concluded to be a functional copper chaperone.
从大鼠cDNA文库中克隆出一个长度为503 bp的ATX1同源物，该cDNA推导的蛋白质含有68个氨基酸，预测分子量为7.2 kDa。大鼠ATX1同源蛋白（Rah1p）与Atx1p、CUC-1和HAH1的同源性分别为35%、38%和89%，在N端保留了MTCXXC铜结合位点，在C端保留了富含赖氨酸的KTGK区域。在Northern印迹分析中，发现rah1 mRNA在肝脏、小肠和睾丸中高水平表达。rah1 cDNA的表达补充了酵母中atx1 null突变株。因此，得出结论Rah1p是一种功能性铜伴侣蛋白。
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