Mi H, Kops O, Zimmermann E, Jäschke A, Tropschug M
Institut für Biochemie und Molekularbiologie der Albert-Ludwigs-Universität, Freiburg, Germany.
FEBS Lett. 1996 Dec 2;398(2-3):201-5. doi: 10.1016/s0014-5793(96)01248-3.
Cyclophilins (CyPs) are binding proteins for the immunosuppressive drug cyclosporin A (CsA). CyPs are evolutionarily highly conserved proteins present in both pro- and eukaryotes as well as in different subcellular locations. CyPs possess enzymatic activity, namely peptidyl-prolyl cis-trans isomerase (PPIase) activity; CyPs are involved in cellular protein folding and protein interactions. To date, only cyclosporins and proteins are known to interact with CyPs. Here we describe a novel nuclear cyclophilin (hCyP33) from human T cells with an additional RNA-binding domain. This combines for the first time RNA binding and protein folding in one protein.
亲环蛋白(CyPs)是免疫抑制药物环孢素A(CsA)的结合蛋白。亲环蛋白是进化上高度保守的蛋白质,存在于原核生物和真核生物中,以及不同的亚细胞位置。亲环蛋白具有酶活性,即肽基脯氨酰顺反异构酶(PPIase)活性;亲环蛋白参与细胞蛋白质折叠和蛋白质相互作用。迄今为止,已知只有环孢菌素和蛋白质与亲环蛋白相互作用。在这里,我们描述了一种来自人类T细胞的新型核亲环蛋白(hCyP33),它具有一个额外的RNA结合结构域。这首次将RNA结合和蛋白质折叠结合在一种蛋白质中。