Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.

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 elucida

SUBMITTER: Dendooven T 

PROVIDER: S-EPMC9890229 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature