4UE5

Structural basis for targeting and elongation arrest of Bacillus signal recognition particle

4UE5 の概要

• エントリーDOI: 10.2210/pdb4ue5/pdb
• 関連するPDBエントリー: 4UE4
• EMDBエントリー: 2844
• 分子名称: 7S RNA, SRP14, SIGNAL RECOGNITION PARTICLE SUBUNIT SRP68, ... (7 entities in total)
• 機能のキーワード: translation, stalled ribosome
• 由来する生物種: CANIS LUPUS FAMILIARIS (DOG); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 199914.69

構造登録者

Beckert, B.,Kedrov, A.,Sohmen, D.,Kempf, G.,Wild, K.,Sinning, I.,Stahlberg, H.,Wilson, D.N.,Beckmann, R. (登録日: 2014-12-15, 公開日: 2015-09-09, 最終更新日: 2024-05-08)

主引用文献

Beckert, B.,Kedrov, A.,Sohmen, D.,Kempf, G.,Wild, K.,Sinning, I.,Stahlberg, H.,Wilson, D.N.,Beckmann, R.
Translational Arrest by a Prokaryotic Signal Recognition Particle is Mediated by RNA Interactions.
Nat.Struct.Mol.Biol., 22:767-, 2015

PubMed Abstract: The signal recognition particle (SRP) recognizes signal sequences of nascent polypeptides and targets ribosome-nascent chain complexes to membrane translocation sites. In eukaryotes, translating ribosomes are slowed down by the Alu domain of SRP to allow efficient targeting. In prokaryotes, however, little is known about the structure and function of Alu domain-containing SRPs. Here, we report a complete molecular model of SRP from the Gram-positive bacterium Bacillus subtilis, based on cryo-EM. The SRP comprises two subunits, 6S RNA and SRP54 or Ffh, and it facilitates elongation slowdown similarly to its eukaryotic counterpart. However, protein contacts with the small ribosomal subunit observed for the mammalian Alu domain are substituted in bacteria by RNA-RNA interactions of 6S RNA with the α-sarcin-ricin loop and helices H43 and H44 of 23S rRNA. Our findings provide a structural basis for cotranslational targeting and RNA-driven elongation arrest in prokaryotes.

PubMed: 26344568
DOI: 10.1038/NSMB.3086

実験手法

ELECTRON MICROSCOPY (9 Å)