Zheng L, Kennedy M C, Blondin G A, Beinert H, Zalkin H
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153.
Arch Biochem Biophys. 1992 Dec;299(2):356-60. doi: 10.1016/0003-9861(92)90287-7.
The 5' end of porcine mitochondrial aconitase mRNA contains an iron responsive element (IRE)-like secondary structure (T. Dandekar, R. Stripecke, N. K. Gray, B. Goosen, A. Constable, H. E. Johansson, and M. W. Hentze (1991) EMBO J. 10, 1903-1909). A protein from a liver extract binds to a mitochondrial aconitase RNA probe and supports the identification of this sequence as an IRE. Purified cytosolic aconitase but not the mitochondrial enzyme binds to this IRE as well as to a ferritin IRE. All forms of cytosolic aconitase, [4Fe-4S] enzyme, [3Fe-4S] enzyme and apoenzyme bind with similar affinity. A Kd of 0.25 nM was calculated for the apoaconitase-IRE interaction from Scatchard analysis. These results support the conclusion that cytosolic aconitase is an IRE-binding protein which may regulate translation of mitochondrial aconitase mRNA.
猪线粒体乌头酸酶mRNA的5'端含有一个类似铁反应元件(IRE)的二级结构(T.丹德卡尔、R.施特里佩克、N.K.格雷、B.古森、A.康斯特布尔、H.E.约翰松和M.W.亨茨(1991年)《欧洲分子生物学组织杂志》10,1903 - 1909)。肝脏提取物中的一种蛋白质与线粒体乌头酸酶RNA探针结合,支持将该序列鉴定为IRE。纯化的胞质乌头酸酶而非线粒体酶与该IRE以及铁蛋白IRE结合。所有形式的胞质乌头酸酶,[4Fe - 4S]酶、[3Fe - 4S]酶和脱辅基酶以相似的亲和力结合。通过斯卡查德分析计算出脱辅基乌头酸酶与IRE相互作用的解离常数(Kd)为0.25 nM。这些结果支持以下结论:胞质乌头酸酶是一种IRE结合蛋白,可能调节线粒体乌头酸酶mRNA的翻译。