Summary information and primary citation
- PDB-id
- 5z3g; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- ribosome
- Method
- cryo-EM (3.65 Å)
- Summary
- cryo-EM structure of a nucleolar pre-60s ribosome (rpf1-tap)
- Reference
- Zhou D, Zhu X, Zheng S, Tan D, Dong MQ, Ye K (2019): "Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate." Protein Cell, 10, 120-130. doi: 10.1007/s13238-018-0526-7.
- 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.
