Xing Zhu
Sanduo Zheng
Dan Tan
Meng-Qiu Dong
Keqiong Ye
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 University of Chinese Academy of Sciences, Beijing 100049, China
Funds: The study was supported by Strategic Priority Research Program of Chinese Academy of Sciences (XDB08010203), National Key R&D Program of China (2017YFA0504600), the National Natural Science Foundation of China (Grant Nos. 31430024, 91540201 and 31325007), the Ministry of Science and Technology of China (973 grant 2014CB84980001 to Meng-Qiu Dong) and 100 Talents Program of CAS.
Received Date: 2018-01-09
Rev Recd Date:2018-03-04
Abstract
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 ? 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.Keywords: ribosome assembly,
cryo-EM,
pre-60S ribosome,
nucleolar
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