6CB1

Yeast nucleolar pre-60S ribosomal subunit (state 3)

6CB1 の概要

• エントリーDOI: 10.2210/pdb6cb1/pdb
• 関連するPDBエントリー: 6C0F
• EMDBエントリー: 7324 7445
• 分子名称: 35S pre-ribosomal RNA miscRNA, Ribosome production factor 1, Proteasome-interacting protein CIC1, ... (41 entities in total)
• 機能のキーワード: pre-60s, ribosome biogenesis, lsu processome, ribosome
• 由来する生物種: Saccharomyces cerevisiae BY4741 (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 40
• 化学式量合計: 2185204.34

構造登録者

Sanghai, Z.A.,Miller, L.,Barandun, J.,Hunziker, M.,Chaker-Margot, M.,Klinge, S. (登録日: 2018-02-01, 公開日: 2018-03-14, 最終更新日: 2024-03-13)

主引用文献

Sanghai, Z.A.,Miller, L.,Molloy, K.R.,Barandun, J.,Hunziker, M.,Chaker-Margot, M.,Wang, J.,Chait, B.T.,Klinge, S.
Modular assembly of the nucleolar pre-60S ribosomal subunit.
Nature, 556:126-129, 2018

PubMed Abstract: Early co-transcriptional events during eukaryotic ribosome assembly result in the formation of precursors of the small (40S) and large (60S) ribosomal subunits. A multitude of transient assembly factors regulate and chaperone the systematic folding of pre-ribosomal RNA subdomains. However, owing to a lack of structural information, the role of these factors during early nucleolar 60S assembly is not fully understood. Here we report cryo-electron microscopy (cryo-EM) reconstructions of the nucleolar pre-60S ribosomal subunit in different conformational states at resolutions of up to 3.4 Å. These reconstructions reveal how steric hindrance and molecular mimicry are used to prevent both premature folding states and binding of later factors. This is accomplished by the concerted activity of 21 ribosome assembly factors that stabilize and remodel pre-ribosomal RNA and ribosomal proteins. Among these factors, three Brix-domain proteins and their binding partners form a ring-like structure at ribosomal RNA (rRNA) domain boundaries to support the architecture of the maturing particle. The existence of mutually exclusive conformations of these pre-60S particles suggests that the formation of the polypeptide exit tunnel is achieved through different folding pathways during subsequent stages of ribosome assembly. These structures rationalize previous genetic and biochemical data and highlight the mechanisms that drive eukaryotic ribosome assembly in a unidirectional manner.

PubMed: 29512650
DOI: 10.1038/nature26156

実験手法

ELECTRON MICROSCOPY (4.6 Å)