7QGU

Structure of the B. subtilis disome - stalled 70S ribosome

これはPDB形式変換不可エントリーです。

7QGU の概要

• エントリーDOI: 10.2210/pdb7qgu/pdb
• EMDBエントリー: 13952 13955 13956 13958 13959
• 分子名称: 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (54 entities in total)
• 機能のキーワード: ribosome rescue, disome, ribosome collision, stalling, no-go complex, ribosome
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 54
• 化学式量合計: 2195506.03

構造登録者

Kratzat, H.,Buschauer, R.,Berninghausen, O.,Beckmann, R. (登録日: 2021-12-10, 公開日: 2022-03-16, 最終更新日: 2022-03-30)

主引用文献

Saito, K.,Kratzat, H.,Campbell, A.,Buschauer, R.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Green, R.,Beckmann, R.,Buskirk, A.R.
Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria.
Nature, 603:503-508, 2022

PubMed Abstract: Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes. Here, using a genetic screen in Escherichia coli, we discovered a new rescue factor that has endonuclease activity. SmrB cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA (which acts on truncated mRNAs) to rescue upstream ribosomes. SmrB is recruited to ribosomes and is activated by collisions. Cryo-electron microscopy structures of collided disomes from E. coli and Bacillus subtilis show distinct and conserved arrangements of individual ribosomes and the composite SmrB-binding site. These findings reveal the underlying mechanisms by which ribosome collisions trigger ribosome rescue in bacteria.

PubMed: 35264790
DOI: 10.1038/s41586-022-04416-7

実験手法

ELECTRON MICROSCOPY (4.75 Å)