Journal
PROTEIN & CELL
Volume 10, Issue 2, Pages 120-130Publisher
SPRINGEROPEN
DOI: 10.1007/s13238-018-0526-7
Keywords
ribosome assembly; cryo-EM; pre-60S ribosome; nucleolar
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Funding
- Strategic Priority Research Program of Chinese Academy of Sciences [XDB08010203]
- National Key R&D Program of China [2017YFA0504600]
- National Natural Science Foundation of China [31430024, 91540201, 31325007]
- Ministry of Science and Technology of China (973) [2014CB84980001]
- 100 Talents Program of CAS
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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.
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