5z3g
From Proteopedia
Cryo-EM structure of a nucleolar pre-60S ribosome (Rpf1-TAP)
Structural highlights
FunctionPublication Abstract from PubMedAssembly 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. Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.,Zhou D, Zhu X, Zheng S, Tan D, Dong MQ, Ye K Protein Cell. 2018 Mar 19. pii: 10.1007/s13238-018-0526-7. doi:, 10.1007/s13238-018-0526-7. PMID:29557065[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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