A pre-ribosome with a short article tadpole-like structure functions in ATP-dependent maturation of 60S subunits
A pre-ribosome with a short article tadpole-like structure functions in ATP-dependent maturation of 60S subunits
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DOI：
10.1016/j.molcel.2004.06.033
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发表时间：
2004-07-23
期刊：
影响因子：
16
通讯作者：
Hurt, E
中科院分区：
文献类型：
--
作者：
Nissan, TA;Galani, K;Hurt, E
分离的前核糖体的分析产生了动态的，新生的60 S和40 S亚基的生化“快照”，在他们的路径从核仁到细胞质。在这里，我们提出了位于核质中的前60 S核糖体中间体的结构。一个巨大的动力蛋白相关的AAA型ATP酶（真实的）和Rix 1复合物（Rix 1-lpi 1-lpi 3）是一个延伸的（类似于45 nm长）前60 S颗粒的组成部分。抗体交联结合电子显微镜显示，真实的定位于“尾”区和核糖体蛋白的“头”区的延长的“蝌蚪样”结构。此外，在体外用ATP处理诱导真实的从前60 S亚基解离。真实的和Rix 1复合物可以介导60 S亚基的ATP依赖性重塑，并随后从核质输出到细胞质。
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 (Real) and the Rix1 complex (Rix1-lpi1-lpi3) are components of an extended (similar to45 nm long) pre-60S particle. Antibody crosslinking in combination with electron microscopy revealed that the Real 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 Real from the pre-60S subunits. Real and the Rix1 complex could mediate ATP-dependent remodeling of 60S subunits and subsequent export from the nucleoplasm to the cytoplasm.