8BVM

Cryo-EM structure of Hfq-Crc-rbsB translation repression complex

8BVM の概要

• エントリーDOI: 10.2210/pdb8bvm/pdb
• EMDBエントリー: 16264 16265 16266
• 分子名称: Catabolite repression control protein, RNA-binding protein Hfq, rbsB mRNA (3 entities in total)
• 機能のキーワード: co-transcriptional rna folding; crc; metabolic regulation; ribonucleoprotein assembly; rna chaperone hfq; translational regulation, rna binding protein
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 234530.22

構造登録者

Dendooven, T.,Luisi, B.F. (登録日: 2022-12-04, 公開日: 2023-01-25, 最終更新日: 2024-07-24)

主引用文献

Dendooven, T.,Sonnleitner, E.,Blasi, U.,Luisi, B.F.
Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.
Embo J., 42:e111129-e111129, 2023

PubMed Abstract: The widely occurring bacterial RNA chaperone Hfq is a key factor in the post-transcriptional control of hundreds of genes in Pseudomonas aeruginosa. How this broadly acting protein can contribute to the regulatory requirements of many different genes remains puzzling. Here, we describe cryo-EM structures of higher order assemblies formed by Hfq and its partner protein Crc on control regions of different P. aeruginosa target mRNAs. Our results show that these assemblies have mRNA-specific quaternary architectures resulting from the combination of multivalent protein-protein interfaces and recognition of patterns in the RNA sequence. The structural polymorphism of these ribonucleoprotein assemblies enables selective translational repression of many different target mRNAs. This system elucidates how highly complex regulatory pathways can evolve with a minimal economy of proteinogenic components in combination with RNA sequence and fold.

PubMed: 36504222
DOI: 10.15252/embj.2022111129

実験手法

ELECTRON MICROSCOPY (3.8 Å)