Nissan Tracy A, Galani Kyriaki, Maco Bohumil, Tollervey David, Aebi Ueli, Hurt Ed
Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120, Germany.
Mol Cell. 2004 Jul 23;15(2):295-301. doi: 10.1016/j.molcel.2004.06.033.
Analyses of isolated pre-ribosomes yielded biochemical "snapshots" of the dynamic, nascent 60S and 40S subunits during their path from the nucleolus to the cytoplasm. Here, we present the structure of a pre-60S ribosomal intermediate located in the nucleoplasm. A huge dynein-related AAA-type ATPase (Rea1) and the Rix1 complex (Rix1-Ipi1-Ipi3) are components of an extended (approximately 45 nm long) pre-60S particle. Antibody crosslinking in combination with electron microscopy revealed that the Rea1 localizes to the "tail" region and ribosomal proteins to the "head" region of the elongated "tadpole-like" structure. Furthermore, in vitro treatment with ATP induces dissociation of Rea1 from the pre-60S subunits. Rea1 and the Rix1 complex could mediate ATP-dependent remodeling of 60S subunits and subsequent export from the nucleoplasm to the cytoplasm.
对分离出的前核糖体进行分析，得到了动态新生60S和40S亚基从核仁到细胞质过程中的生化“快照”。在此，我们展示了位于核质中的前60S核糖体中间体的结构。一种巨大的动力蛋白相关AAA型ATP酶（Rea1）和Rix1复合体（Rix1-Ipi1-Ipi3）是一个延伸的（约45纳米长）前60S颗粒的组成部分。抗体交联结合电子显微镜显示，Rea1定位于细长“蝌蚪状”结构的“尾部”区域，核糖体蛋白定位于“头部”区域。此外，ATP体外处理可诱导Rea1从前60S亚基解离。Rea1和Rix1复合体可能介导60S亚基的ATP依赖性重塑以及随后从核质输出到细胞质。
