Evidence map›Paper›PMID 29557065›Full record

ArticleProtein & cell2019

Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.

Dejian Zhou, Xing Zhu, Sanduo Zheng, Dan Tan, Meng-Qiu Dong, Keqiong Ye

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Article in Protein & cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

53 citing papers in PubMed.

  1. Article
  2. The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors.

Dejian ZhouGraduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing, 100730, China.
Xing ZhuKey Laboratory of RNA Biology, Institute of Biophysics, CAS Center for Excellence in Biomacromolecules, Chinese Academy of Sciences, Beijing, 100101, China.
Sanduo ZhengNational Institute of Biological Sciences, Beijing, 102206, China.
Dan TanNational Institute of Biological Sciences, Beijing, 102206, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, 102206, China.
Keqiong YeGraduate School of Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing, 100730, China. yekeqiong@ibp.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Cryoelectron MicroscopyModels, MolecularMolecular ConformationProtein DomainsRibosomal ProteinsRibosome Subunits, Large, EukaryoticRNA, RibosomalRNA, Ribosomal, 5.8SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsRibosomal ProteinsRNA, RibosomalRNA, ribosomal, 25SRNA, Ribosomal, 5.8SSaccharomyces cerevisiae Proteinscryo-EMnucleolarpre-60S ribosomeribosome assembly

Identifiers

PMID29557065
PMCPMC6340896

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.