8AP4

Structure of Escherischia coli heat shock protein Hsp15 in complex with ribosomal 50S subunits bearing peptidyl-tRNA

8AP4 の概要

• エントリーDOI: 10.2210/pdb8ap4/pdb
• EMDBエントリー: 15558
• 分子名称: 50S ribosomal protein L33, 50S ribosomal protein L2, 50S ribosomal protein L3, ... (33 entities in total)
• 機能のキーワード: s4 domain, heat shock, stress response, ribosome quality control, translation
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 33
• 化学式量合計: 1390649.36

構造登録者

Safdari, H.A.,Wilson, D.N. (登録日: 2022-08-09, 公開日: 2022-11-16, 最終更新日: 2025-03-12)

主引用文献

Safdari, H.A.,Kasvandik, S.,Polte, C.,Ignatova, Z.,Tenson, T.,Wilson, D.N.
Structure of Escherichia coli heat shock protein Hsp15 in complex with the ribosomal 50S subunit bearing peptidyl-tRNA.
Nucleic Acids Res., 50:12515-12526, 2022

PubMed Abstract: In Escherichia coli, the heat shock protein 15 (Hsp15) is part of the cellular response to elevated temperature. Hsp15 interacts with peptidyl-tRNA-50S complexes that arise upon dissociation of translating 70S ribosomes, and is proposed to facilitate their rescue and recycling. A previous structure of E. coli Hsp15 in complex with peptidyl-tRNA-50S complex reported a binding site located at the central protuberance of the 50S subunit. By contrast, recent structures of RqcP, the Hsp15 homolog in Bacillus subtilis, in complex with peptidyl-tRNA-50S complexes have revealed a distinct site positioned between the anticodon-stem-loop (ASL) of the P-site tRNA and H69 of the 23S rRNA. Here we demonstrate that exposure of E. coli cells to heat shock leads to a decrease in 70S ribosomes and accumulation of 50S subunits, thus identifying a natural substrate for Hsp15 binding. Additionally, we have determined a cryo-EM reconstruction of the Hsp15-50S-peptidyl-tRNA complex isolated from heat shocked E. coli cells, revealing that Hsp15 binds to the 50S-peptidyl-tRNA complex analogously to its B. subtilis homolog RqcP. Collectively, our findings support a model where Hsp15 stabilizes the peptidyl-tRNA in the P-site and thereby promotes access to the A-site for putative rescue factors to release the aberrant nascent polypeptide chain.

PubMed: 36370110
DOI: 10.1093/nar/gkac1035

実験手法

ELECTRON MICROSCOPY (3 Å)