Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.

Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.
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大核糖体亚基早期前体的冷冻电镜结构揭示了半组装的中间体。

DOI:
10.1007/s13238-018-0526-7
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发表时间:
2019-03
期刊:
影响因子:
21.1
通讯作者:
Ye K
Ye K
中科院分区:
生物学1区
文献类型:
--
作者:
Zhou D;Zhu X;Zheng S;Tan D;Dong MQ;Ye K

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真核生物核糖体的组装是一个复杂的动态过程,涉及到一系列的中间环节。目前还不清楚60 S大核糖体亚基的高度缠结结构是如何建立的。在这里,我们报告的早期核仁前60 S核糖体的结构,通过冷冻电子显微镜在3.7 μ m的分辨率,揭示了半组装的亚基。25 S/5.8S rRNA的结构域I、II和VI紧密地组装成天然样亚结构,但结构域III、IV和V不组装。该结构包含12个装配因子和19个核糖体蛋白,其中许多是大亚基rRNA早期加工所需的。Brx 1-Ebp 2复合物会干扰结构域IV和V的组装。Rpf 1、Mak 16、Nsa 1和Rrp 1形成一个簇,该簇巩固了结构域I和II的连接。我们的结构揭示了在建立60 S亚基的全球架构的道路上的关键中间体。本文的在线版本(10.1007/s13238-018-0526-7)包含补充材料,可供授权用户使用。
Assembly of eukaryotic ribosome is a complicated and dynamic process that involves a series of intermediates. It is unknown how the highly intertwined structure of 60S large ribosomal subunits is established. Here, we report the structure of an early nucleolar pre-60S ribosome determined by cryo-electron microscopy at 3.7 Å resolution, revealing a half-assembled subunit. Domains I, II and VI of 25S/5.8S rRNA pack tightly into a native-like substructure, but domains III, IV and V are not assembled. The structure contains 12 assembly factors and 19 ribosomal proteins, many of which are required for early processing of large subunit rRNA. The Brx1-Ebp2 complex would interfere with the assembly of domains IV and V. Rpf1, Mak16, Nsa1 and Rrp1 form a cluster that consolidates the joining of domains I and II. Our structure reveals a key intermediate on the path to establishing the global architecture of 60S subunits. The online version of this article (10.1007/s13238-018-0526-7) contains supplementary material, which is available to authorized users.
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