Structural highlights
Publication Abstract from PubMed
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 A resolution, revealing the Hfq-RNA interaction in exceptional detail.
Structure of an Escherichia coli Hfq:RNA complex at 0.97 A resolution.,Schulz EC, Barabas O Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1492-7. doi:, 10.1107/S2053230X14020044. Epub 2014 Oct 31. PMID:25372815[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schulz EC, Barabas O. Structure of an Escherichia coli Hfq:RNA complex at 0.97 A resolution. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1492-7. doi:, 10.1107/S2053230X14020044. Epub 2014 Oct 31. PMID:25372815 doi:http://dx.doi.org/10.1107/S2053230X14020044