| Literature DB >> 25372815 |
Eike C Schulz1, Orsolya Barabas1.
Abstract
In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq-RNA interaction in exceptional detail.Entities:
Keywords: Escherichia coli; Hfq; RNA chaperones
Mesh:
Substances:
Year: 2014 PMID: 25372815 PMCID: PMC4231850 DOI: 10.1107/S2053230X14020044
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056