8BVM

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

Summary for 8BVM

• Entry DOI: 10.2210/pdb8bvm/pdb
• EMDB information: 16264 16265 16266
• Descriptor: Catabolite repression control protein, RNA-binding protein Hfq, rbsB mRNA (3 entities in total)
• Functional Keywords: co-transcriptional rna folding; crc; metabolic regulation; ribonucleoprotein assembly; rna chaperone hfq; translational regulation, rna binding protein
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 16
• Total formula weight: 234530.22

Authors

Dendooven, T.,Luisi, B.F. (deposition date: 2022-12-04, release date: 2023-01-25, Last modification date: 2024-07-24)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.8 Å)