【摘 要】
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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
【机 构】
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Graduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100
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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 A 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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