8R55

Bacillus subtilis MutS2-collided disome complex (collided 70S)

これはPDB形式変換不可エントリーです。

8R55 の概要

• エントリーDOI: 10.2210/pdb8r55/pdb
• 関連するPDBエントリー: 8QPP
• EMDBエントリー: 18586 18901
• 分子名称: 50S ribosomal protein L32, 30S ribosomal protein S3, 30S ribosomal protein S4, ... (53 entities in total)
• 機能のキーワード: muts2, collision, disome, splitting, quality control, ribosome
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 53
• 化学式量合計: 2241420.16

構造登録者

Park, E.,Mackens-Kiani, T.,Berhane, R.,Esser, H.,Erdenebat, C.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Beckmann, R.,Green, R.,Buskirk, A.R. (登録日: 2023-11-16, 公開日: 2024-01-17, 最終更新日: 2024-10-23)

主引用文献

Park, E.N.,Mackens-Kiani, T.,Berhane, R.,Esser, H.,Erdenebat, C.,Burroughs, A.M.,Berninghausen, O.,Aravind, L.,Beckmann, R.,Green, R.,Buskirk, A.R.
B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage.
Embo J., 43:484-506, 2024

PubMed Abstract: Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the recruitment of SmrB, a nuclease that cleaves the mRNA. In B. subtilis, the related protein MutS2 was recently implicated in ribosome rescue. Here we show that MutS2 is recruited to collisions by its SMR and KOW domains, and we reveal the interaction of these domains with collided ribosomes by cryo-EM. Using a combination of in vivo and in vitro approaches, we show that MutS2 uses its ABC ATPase activity to split ribosomes, targeting the nascent peptide for degradation through the ribosome quality control pathway. However, unlike SmrB, which cleaves mRNA in E. coli, we see no evidence that MutS2 mediates mRNA cleavage or promotes ribosome rescue by tmRNA. These findings clarify the biochemical and cellular roles of MutS2 in ribosome rescue in B. subtilis and raise questions about how these pathways function differently in diverse bacteria.

PubMed: 38177497
DOI: 10.1038/s44318-023-00010-3

実験手法

ELECTRON MICROSCOPY (3.57 Å)