Literature DB >> 25372815

Structure of an Escherichia coli Hfq:RNA complex at 0.97 Å resolution.

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


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