Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.
10.1007/s13238-018-0526-7
- Author:
Dejian ZHOU
1
;
Xing ZHU
2
;
Sanduo ZHENG
3
;
Dan TAN
3
;
Meng-Qiu DONG
3
;
Keqiong YE
4
Author Information
1. Graduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing, 100730, China.
2. Key Laboratory of RNA Biology, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences, Beijing, 100101, China.
3. National Institute of Biological Sciences, Beijing, 102206, China.
4. Graduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing, 100730, China. yekeqiong@ibp.ac.cn.
- Publication Type:Journal Article
- Keywords:
cryo-EM;
nucleolar;
pre-60S ribosome;
ribosome assembly
- From:
Protein & Cell
2019;10(2):120-130
- CountryChina
- Language:English
-
Abstract:
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.