Single-particle cryo-EM structure of the RNA chaperone Hfq in a translation repression complex Hfq-Crc-estA
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ABSTRACT:
SUBMITTER: Bonaventura Luisi
PROVIDER: EMPIAR-12206 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.
Dendooven Tom T Sonnleitner Elisabeth E Bläsi Udo U Luisi Ben F BF
The EMBO journal 20221212 3
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 quatern ...[more]
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