人核糖核酸酶P催化活性复合物某些蛋白质亚基的自身抗原特性
Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P.
作者信息
Jarrous N, Eder P S, Guerrier-Takada C, Hoog C, Altman S
机构信息
Department of Biology, Yale University, New Haven, Connecticut 06520, USA.
出版信息
RNA. 1998 Apr;4(4):407-17.
Abstract
At least six proteins co-purify with human ribonuclease P (RNase P), a tRNA processing ribonucleoprotein. Two of these proteins, Rpp30 and Rpp38, are Th autoantigens. Recombinant Rpp30 and Rpp38 are also recognized by Th sera from systemic sclerosis patients. Two of the other proteins associated with RNase P, Rpp20 and Rpp40, do not cross-react with Th sera. Polyclonal antibodies raised against all four recombinant proteins recognize the corresponding proteins associated with RNase P and precipitate active holoenzyme. Catalytically active RNase P holoenzyme can be separated from the nucleolar and mitochondrial RNA processing endoribonuclease, RNase MRP, even though these two enzymes may share some subunits.
摘要
至少有六种蛋白质与人体核糖核酸酶P（RNase P，一种参与tRNA加工的核糖核蛋白）共同纯化。其中两种蛋白质，Rpp30和Rpp38，是Th自身抗原。重组Rpp30和Rpp38也能被系统性硬化症患者的Th血清识别。与RNase P相关的另外两种蛋白质，Rpp20和Rpp40，不会与Th血清发生交叉反应。针对所有四种重组蛋白产生的多克隆抗体可识别与RNase P相关的相应蛋白质，并沉淀出活性全酶。具有催化活性的RNase P全酶可以与核仁及线粒体RNA加工内切核糖核酸酶RNase MRP分离，尽管这两种酶可能共享一些亚基。
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