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Title | Architectural principles for Hfq/Crc-mediated regulation of gene expression. |
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Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Feb 13, 2019 |
Authors | Xue Yuan Pei / Tom Dendooven / Elisabeth Sonnleitner / Shaoxia Chen / Udo Bläsi / Ben F Luisi / |
PubMed Abstract | In diverse bacterial species, the global regulator Hfq contributes to post-transcriptional networks that control expression of numerous genes. Hfq of the opportunistic pathogen inhibits translation ...In diverse bacterial species, the global regulator Hfq contributes to post-transcriptional networks that control expression of numerous genes. Hfq of the opportunistic pathogen inhibits translation of target transcripts by forming a regulatory complex with the catabolite repression protein Crc. This repressive complex acts as part of an intricate mechanism of preferred nutrient utilisation. We describe high-resolution cryo-EM structures of the assembly of Hfq and Crc bound to the translation initiation site of a target mRNA. The core of the assembly is formed through interactions of two cognate RNAs, two Hfq hexamers and a Crc pair. Additional Crc protomers are recruited to the core to generate higher-order assemblies with demonstrated regulatory activity in vivo. This study reveals how Hfq cooperates with a partner protein to regulate translation, and provides a structural basis for an RNA code that guides global regulators to interact cooperatively and regulate different RNA targets. |
External links | Elife / PubMed:30758287 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.13 - 3.37 Å |
Structure data | EMDB-0590: Architectural principles for Hfq/Crc-mediated regulation of gene expression Hfq-Crc-amiE 2:2:2 complex (core complex) |
Source |
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Keywords | RNA BINDING PROTEIN/RNA/Hydrolase / Hfq / Crc / amiE / Carbon catabolite repression / RNA-protein interaction / RNA-mediated gene regulation / RNA BINDING PROTEIN / RNA BINDING PROTEIN-RNA-Hydrolase complex |